{"title":"FineTest Protein","description":"","products":[{"product_id":"recombinant-sars-cov-2-nucleoprotein-bhp10800001","title":"Recombinant SARS-CoV-2 Nucleoprotein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSARS-CoV-2 Nucleoprotein\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e 2019-nCoV nucleocapsid protein, NC, Nucleoprotein, Protein N.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eIn RUO virology and host–pathogen research, \u003cstrong\u003eSARS-CoV-2 Nucleoprotein\u003c\/strong\u003e is commonly used to study viral assembly\/entry processes, host-factor engagement, and immune recognition in experimental systems. Recombinant viral proteins are frequently used as defined antigens, binding reagents, and standards in assay development and mechanistic studies.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how SARS-CoV-2 Nucleoprotein participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect SARS-CoV-2 Nucleoprotein to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Coronavirus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-419\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 47.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eSARS-CoV-2 Nucleoprotein\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant SARS-CoV-2 Nucleoprotein is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871362413,"sku":"P3003-50UG","price":260.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871395181,"sku":"P3003-200UG","price":520.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013871427949,"sku":"P3003-1MG","price":1560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD.jpg?v=1770539250"},{"product_id":"recombinant-human-pct-bhp10800002","title":"Recombinant Human PCT","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePCT\u003c\/strong\u003e is provided as a recombinant protein reagent for research use only (RUO), offering a defined input for assay development and mechanistic studies.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePCT\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003eimmune signaling, cytokine\/chemokine networks, and innate\/adaptive immune mechanisms; vascular biology, cardiac stress signaling, and remodeling pathways in research models; cell-fate decisions, differentiation, and morphogen signaling (RUO)\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how PCT participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect PCT to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 21-141\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 15 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ePCT\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant PCT is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871460717,"sku":"P0010-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871493485,"sku":"P0010-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013871526253,"sku":"P0010-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_b94b19b0-1851-48cc-9c4b-0da762354b2a.jpg?v=1770539250"},{"product_id":"recombinant-human-copeptin-bhp10800003","title":"Recombinant Human copeptin","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ecopeptin\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e copeptin.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ecopeptin\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003ereceptor- and kinase-driven signaling networks and downstream transcriptional programs\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how copeptin participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect copeptin to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 126-164\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 25 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 60% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ecopeptin\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant copeptin is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871559021,"sku":"P0022-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871591789,"sku":"P0022-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013871624557,"sku":"P0022-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_5a80c3df-f124-45e9-a7d2-dcc716a2fe0c.jpg?v=1770539250"},{"product_id":"recombinant-human-asprosin-bhp10800004","title":"Recombinant Human Asprosin","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAsprosin\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibrillin-1, FBN1, FBN.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAsprosin\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Asprosin participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Asprosin to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2732-2871\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eAsprosin\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Asprosin is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871657325,"sku":"P0055-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871690093,"sku":"P0055-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013871722861,"sku":"P0055-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_9eb45813-3558-499c-ac60-3a8905af672e.jpg?v=1770539251"},{"product_id":"recombinant-human-actb-bhp10800005","title":"Recombinant Human ACTB","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eACTB\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e A26C1A, A26C1B, ACTB, ACTB_HUMAN, Actin beta, Actin cytoplasmic 1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eACTB\u003c\/strong\u003e is frequently used in RUO studies focused on \u003cstrong\u003ecell-cycle regulation, DNA replication\/repair, and growth control networks; vascular biology, cardiac stress signaling, and remodeling pathways in research models; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics\u003c\/strong\u003e. Recombinant protein reagents help researchers build defined systems for biochemical characterization, binding assays, and assay development where reproducibility and traceability matter.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how ACTB participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect ACTB to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 14-167\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eACTB\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant ACTB is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871755629,"sku":"P0067-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871788397,"sku":"P0067-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013871821165,"sku":"P0067-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_8c1ee645-387f-483a-84f0-61a03815b49e.jpg?v=1770539251"},{"product_id":"recombinant-human-lmna-bhp10800006","title":"Recombinant Human LMNA","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLMNA\u003c\/strong\u003e is provided as a recombinant protein reagent for research use only (RUO), offering a defined input for assay development and mechanistic studies.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLMNA\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003eself-renewal and lineage commitment programs in stem\/progenitor models; cell-fate decisions, differentiation, and morphogen signaling (RUO)\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how LMNA participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect LMNA to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 26-198\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 21.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eLMNA\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant LMNA is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871853933,"sku":"P0068-50UG","price":455.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871886701,"sku":"P0068-200UG","price":910.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013871919469,"sku":"P0068-1MG","price":2730.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_67bdbe6f-95ca-4bcf-95a7-735ffa197f8e.jpg?v=1770539251"},{"product_id":"recombinant-human-hspa5-bhp10800007","title":"Recombinant Human HSPA5","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHSPA5\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Endoplasmic reticulum chaperone BiP, EC 3.6.4.10, 78 kDa glucose-regulated protein, GRP-78, Binding-immunoglobulin protein, BiP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eIn RUO virology and host–pathogen research, \u003cstrong\u003eHSPA5\u003c\/strong\u003e is commonly used to study viral assembly\/entry processes, host-factor engagement, and immune recognition in experimental systems. Recombinant viral proteins are frequently used as defined antigens, binding reagents, and standards in assay development and mechanistic studies.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how HSPA5 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect HSPA5 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 19-654\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 65 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eHSPA5\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant HSPA5 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013871952237,"sku":"P0108-50UG","price":650.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013871985005,"sku":"P0108-200UG","price":1300.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872017773,"sku":"P0108-1MG","price":3900.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_07be2333-35bf-4169-8ef7-1bbc5cd541de.jpg?v=1770539251"},{"product_id":"recombinant-egfp-protein-bhp10800008","title":"Recombinant EGFP protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eEGFP\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e CFP, eGFP, eYFP, GFP, GFP tag, YFP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eEGFP\u003c\/strong\u003e is widely used in RUO research as a genetically encoded reporter for protein expression, localization, and assay readouts. Purified recombinant reporter proteins are often used as calibration reagents, positive controls, or binding partners in biophysical and biochemical assays.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how EGFP participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect EGFP to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Jellyfish\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa full length\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 27 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eEGFP\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant EGFP is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872050541,"sku":"P0113-50UG","price":533.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872083309,"sku":"P0113-200UG","price":1066.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872116077,"sku":"P0113-1MG","price":3198.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_aa08a21d-3b10-4a58-8c95-23f4d40d6299.jpg?v=1770539252"},{"product_id":"recombinant-human-gapdh-bhp10800009","title":"Recombinant Human GAPDH","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGAPDH\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e aging-associated gene 9 protein, EC 1.2.1, EC 1.2.1.12, EC 2.6.99.-, G3PD, G3PDH.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGAPDH\u003c\/strong\u003e is frequently used in RUO studies focused on \u003cstrong\u003evascular biology, cardiac stress signaling, and remodeling pathways in research models; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics\u003c\/strong\u003e. Recombinant protein reagents help researchers build defined systems for biochemical characterization, binding assays, and assay development where reproducibility and traceability matter.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how GAPDH participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect GAPDH to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2-335\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 35.9 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eGAPDH\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant GAPDH is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872148845,"sku":"P0116-50UG","price":455.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872181613,"sku":"P0116-200UG","price":910.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872214381,"sku":"P0116-1MG","price":2730.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_05819a73-a1a8-40ef-a392-14b4c5830b5d.jpg?v=1770539252"},{"product_id":"recombinant-human-yy1-bhp10800010","title":"Recombinant Human YY1","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eYY1\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Delta transcription factor, DELTA, INO80SYY-1, NF-E1, NF-E1INO80 complex subunit S, transcriptional repressor protein YY1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eYY1\u003c\/strong\u003e is often investigated in RUO gene regulation research for its role in transcriptional control and protein–DNA\/protein–protein interactions. Recombinant regulatory proteins are commonly used in binding assays, complex reconstitution, and mechanistic studies linking signaling to transcriptional outputs.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how YY1 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect YY1 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 35-146\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 37 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Regulatory proteins often engage in PTM-driven control (e.g., phosphorylation, acetylation, ubiquitination) that affects localization and partner binding. Recombinant constructs may model only a subset of these states. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Transcription factors often act through multi-protein complexes and context-specific DNA binding. Researchers typically interpret \u003cstrong\u003eYY1\u003c\/strong\u003e-related findings alongside chromatin state, cofactor availability, and downstream gene-expression signatures described in research studies.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant YY1 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872247149,"sku":"P0117-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872279917,"sku":"P0117-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872312685,"sku":"P0117-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_5c97aaec-e99f-45a6-929a-7eef1e5d6b70.jpg?v=1770539252"},{"product_id":"recombinant-human-txn-bhp10800011","title":"Recombinant Human TXN","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTXN\u003c\/strong\u003e is provided as a recombinant protein reagent for research use only (RUO), offering a defined input for assay development and mechanistic studies.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTXN\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emetabolic pathway regulation, energy homeostasis, and cellular bioenergetics; oncogenic signaling, proliferation control, and tumor–microenvironment biology (RUO)\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how TXN participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect TXN to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-105\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 11.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eTXN\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant TXN is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872378221,"sku":"P0119-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872410989,"sku":"P0119-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872443757,"sku":"P0119-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_a87fed5b-64b1-4e72-a856-f4e197e2fe81.jpg?v=1770539253"},{"product_id":"recombinant-mouse-txn-bhp10800012","title":"Recombinant Mouse txn","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003etxn\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e ADF, ATL derived factor, SASP, Thioredoxin, TRDX, TRX.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003etxn\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how txn participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect txn to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-105\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 11.6 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003etxn\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant txn is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872476525,"sku":"P0120-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872509293,"sku":"P0120-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872542061,"sku":"P0120-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_5dd65d14-eee8-446a-b518-57ddb2dfab84.jpg?v=1770539253"},{"product_id":"recombinant-human-fabp2-bhp10800013","title":"Recombinant Human FABP2","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP2\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e FABP2, FABPI, fatty acid binding protein 2, intestinal, Fatty acid-binding protein 2, fatty acid-binding protein.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP2\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003ereceptor- and kinase-driven signaling networks and downstream transcriptional programs; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics; vascular biology, cardiac stress signaling, and remodeling pathways in research models\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP2 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP2 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2-132\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 15 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP2\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP2 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872574829,"sku":"P0122-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872607597,"sku":"P0122-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872640365,"sku":"P0122-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_ebf2a55d-1d98-405c-a1cd-7d3ebd44eb28.jpg?v=1770539254"},{"product_id":"recombinant-human-fabp4-bhp10800014","title":"Recombinant Human FABP4","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP4\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Adipocyte lipid-binding protein, Adipocyte-type fatty acid-binding protein, AFABP, A-FABP, A-FABPAFABP, ALBP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP4\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003ereceptor- and kinase-driven signaling networks and downstream transcriptional programs; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics; vascular biology, cardiac stress signaling, and remodeling pathways in research models\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP4 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP4 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2-132\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 14.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP4\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP4 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872673133,"sku":"P0124-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872705901,"sku":"P0124-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872738669,"sku":"P0124-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_b2861b75-eaa0-4eb5-8b51-59f30ae6414a.jpg?v=1770539254"},{"product_id":"recombinant-human-fabp5-bhp10800015","title":"Recombinant Human FABP5","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP5\u003c\/strong\u003e is provided as a recombinant protein reagent for research use only (RUO), offering a defined input for assay development and mechanistic studies.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP5\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003evascular biology, cardiac stress signaling, and remodeling pathways in research models; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics; cell-fate decisions, differentiation, and morphogen signaling (RUO)\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP5 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP5 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2-135\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 15 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP5\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP5 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872771437,"sku":"P0125-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872804205,"sku":"P0125-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872836973,"sku":"P0125-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_610722b7-34ce-42ef-b402-dcc4bbab387c.jpg?v=1770539254"},{"product_id":"recombinant-human-fabp6-bhp10800016","title":"Recombinant Human FABP6","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP6\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e FABP6, fatty acid binding protein 6, ileal, Fatty acid-binding protein 6, Gastrotropin, I-15P.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP6\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP6 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP6 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2-135\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 14.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP6\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP6 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872869741,"sku":"P0126-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013872902509,"sku":"P0126-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013872935277,"sku":"P0126-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_51ae3712-2063-45f0-91c2-0b9a12d500af.jpg?v=1770539255"},{"product_id":"recombinant-human-fabp7-bhp10800017","title":"Recombinant Human FABP7","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP7\u003c\/strong\u003e is provided as a recombinant protein reagent for research use only (RUO), offering a defined input for assay development and mechanistic studies.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP7\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003ereceptor- and kinase-driven signaling networks and downstream transcriptional programs; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics; cell-fate decisions, differentiation, and morphogen signaling (RUO)\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP7 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP7 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-132\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 14.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP7\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP7 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013872968045,"sku":"P0127-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873000813,"sku":"P0127-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873033581,"sku":"P0127-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_4dbc3fba-2171-4979-853c-29bcd91217cf.jpg?v=1770539255"},{"product_id":"recombinant-human-fabp-8-bhp10800018","title":"Recombinant Human FABP-8","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP-8\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e FABP8, MFABP, M-FABP, MP2, myelin P2 protein, P2.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eIn RUO virology and host–pathogen research, \u003cstrong\u003eFABP-8\u003c\/strong\u003e is commonly used to study viral assembly\/entry processes, host-factor engagement, and immune recognition in experimental systems. Recombinant viral proteins are frequently used as defined antigens, binding reagents, and standards in assay development and mechanistic studies.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP-8 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP-8 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 2-132\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 14.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP-8\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP-8 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873066349,"sku":"P0128-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873099117,"sku":"P0128-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873131885,"sku":"P0128-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_a447e201-af23-4171-aef5-5a5c03ca4a09.jpg?v=1770539255"},{"product_id":"recombinant-human-fabp9-bhp10800019","title":"Recombinant Human FABP9","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP9\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e FABP9, FABP-9, Fatty Acid Binding Protein 9, Testis, Fatty Acid-Binding Protein 9, Lipid-Binding Protein.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP9\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP9 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP9 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-132\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 15 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP9\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP9 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873164653,"sku":"P0129-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873197421,"sku":"P0129-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873230189,"sku":"P0129-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_fe7bd906-03dd-4d7d-b3c3-a497f49719c4.jpg?v=1770539255"},{"product_id":"recombinant-mouse-fabp4-bhp10800020","title":"Recombinant Mouse FABP4","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP4\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Adipocyte lipid-binding protein, Adipocyte-type fatty acid-binding protein, AFABP, A-FABP, A-FABPAFABP, ALBP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFABP4\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how FABP4 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect FABP4 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-132\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 14.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eFABP4\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant FABP4 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873262957,"sku":"P0130-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873295725,"sku":"P0130-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873328493,"sku":"P0130-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_eb9b18c6-1b16-4486-b947-d9c33437b28d.jpg?v=1770539256"},{"product_id":"recombinant-human-cygb-bhp10800021","title":"Recombinant Human CYGB","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCYGB\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e CYGB, cytoglobin, HGB, Histoglobin, STAP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCYGB\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003evascular biology, cardiac stress signaling, and remodeling pathways in research models\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CYGB participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CYGB to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 1-190\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 21.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eCYGB\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CYGB is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873361261,"sku":"P0132-50UG","price":455.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873394029,"sku":"P0132-200UG","price":910.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873426797,"sku":"P0132-1MG","price":2730.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_53f4a007-ba43-4607-8313-3de9c8952a68.jpg?v=1770539256"},{"product_id":"recombinant-bovine-uter-bhp10800023","title":"Recombinant Bovine Uter","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Blastokinin, CC10, CC10Urine protein 1, CC16, CCPBP, CCSP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Uter participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Uter to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Bovine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 22-91\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 7.6 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eUter\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Uter is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873459565,"sku":"P0136-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873492333,"sku":"P0136-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873525101,"sku":"P0136-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_58d8e7e8-5d18-49c7-9255-8b49312659e0.jpg?v=1770539256"},{"product_id":"recombinant-human-uter-bhp10800024","title":"Recombinant Human Uter","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Blastokinin, CC10, CC10Urine protein 1, CC16, CCPBP, CCSP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003ereceptor- and kinase-driven signaling networks and downstream transcriptional programs\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Uter participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Uter to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 22-91\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 7.9 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eUter\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Uter is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873557869,"sku":"P0137-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873590637,"sku":"P0137-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873623405,"sku":"P0137-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_b903b492-b016-4a82-9d9c-f1393a06ed65.jpg?v=1770539257"},{"product_id":"recombinant-hamster-uter-bhp10800025","title":"Recombinant Hamster Uter","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHamster Uter\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Blastokinin, CC10, CC10Urine protein 1, CC16, CCPBP, CCSP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHamster Uter\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Hamster Uter participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Hamster Uter to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Hamster\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 22-96\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 8.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eHamster Uter\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Hamster Uter is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873656173,"sku":"P0138-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873688941,"sku":"P0138-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873721709,"sku":"P0138-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_cd2bccdd-c7fc-4699-a490-b2113f4b6f63.jpg?v=1770539257"},{"product_id":"recombinant-mouse-uter-bhp10800026","title":"Recombinant Mouse Uter","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Blastokinin, CC10, CC10Urine protein 1, CC16, CCPBP, CCSP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Uter participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Uter to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 22-96\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 8.3 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eUter\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Uter is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873754477,"sku":"P0139-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873787245,"sku":"P0139-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873820013,"sku":"P0139-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_85b3315b-1a5e-45a2-b140-d296e7f72187.jpg?v=1770539257"},{"product_id":"recombinant-rat-uter-bhp10800027","title":"Recombinant Rat Uter","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Blastokinin, CC10, CC10Urine protein 1, CC16, CCPBP, CCSP.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUter\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Uter participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Uter to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 20-96\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 8.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003eUter\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Uter is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873852781,"sku":"P0140-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873885549,"sku":"P0140-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013873918317,"sku":"P0140-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_736188c8-8d3e-4bc5-989a-7bffba5eebeb.jpg?v=1770539258"},{"product_id":"recombinant-bovine-pai-1-bhp10800028","title":"Recombinant Bovine PAI-1","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Endothelial plasminogen activator inhibitor, Nexin, PAI1, PAI-1, PAI1PAI-1, PAISerpin E1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how PAI-1 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect PAI-1 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Bovine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-402\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 43 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ePAI-1\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant PAI-1 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013873951085,"sku":"P0141-50UG","price":533.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013873983853,"sku":"P0141-200UG","price":1066.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013874016621,"sku":"P0141-1MG","price":3198.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_21a8b3f9-32d7-49ec-aa61-544060402df2.jpg?v=1770539258"},{"product_id":"recombinant-human-pai-1-bhp10800029","title":"Recombinant Human PAI-1","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Endothelial plasminogen activator inhibitor, Nexin, PAI1, PAI-1, PAI1PAI-1, PAISerpin E1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003eoncogenic signaling, proliferation control, and tumor–microenvironment biology (RUO); vascular biology, cardiac stress signaling, and remodeling pathways in research models; metabolic pathway regulation, energy homeostasis, and cellular bioenergetics\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how PAI-1 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect PAI-1 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-402\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 42.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ePAI-1\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant PAI-1 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013874049389,"sku":"P0142-50UG","price":455.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013874082157,"sku":"P0142-200UG","price":910.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013874114925,"sku":"P0142-1MG","price":2730.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_0e5b9c4d-a619-480b-b219-aedb068362a2.jpg?v=1770539259"},{"product_id":"recombinant-mouse-pai-1-bhp10800030","title":"Recombinant Mouse PAI-1","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Endothelial plasminogen activator inhibitor, Nexin, PAI1, PAI-1, PAI1PAI-1, PAISerpin E1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how PAI-1 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect PAI-1 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 23-402\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 41 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ePAI-1\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant PAI-1 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013874147693,"sku":"P0143-50UG","price":533.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013874180461,"sku":"P0143-200UG","price":1066.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013874213229,"sku":"P0143-1MG","price":3198.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_fe8b7b2a-1057-4067-b822-72aab394c3a8.jpg?v=1770539260"},{"product_id":"recombinant-porcine-pai-1-bhp10800031","title":"Recombinant Porcine PAI-1","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Endothelial plasminogen activator inhibitor, Nexin, PAI1, PAI-1, PAI1PAI-1, PAISerpin E1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how PAI-1 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect PAI-1 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Porcine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-402\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 43 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ePAI-1\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant PAI-1 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013874245997,"sku":"P0144-50UG","price":533.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013874278765,"sku":"P0144-200UG","price":1066.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013874311533,"sku":"P0144-1MG","price":3198.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_2a2aeab6-b99b-45cb-b70e-906ed4e5eb7a.jpg?v=1770539259"},{"product_id":"recombinant-rat-pai-1-bhp10800032","title":"Recombinant Rat PAI-1","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Endothelial plasminogen activator inhibitor, Nexin, PAI1, PAI-1, PAI1PAI-1, PAISerpin E1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePAI-1\u003c\/strong\u003e is studied in RUO research to understand \u003cstrong\u003emolecular and cellular biology research\u003c\/strong\u003e and related molecular pathways. recombinant proteins are used as defined reagents to support mechanistic experiments, interaction mapping, and assay development in controlled settings.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how PAI-1 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect PAI-1 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-402\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 42.6 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e Post-translational modifications (PTMs) can influence stability, binding, and activity for many proteins. Whether PTMs are present depends on expression system and protein class. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In experimental systems, changes involving \u003cstrong\u003ePAI-1\u003c\/strong\u003e may reflect shifts in upstream regulation, protein stability, or interaction networks. published studies commonly emphasize combining multiple readouts to interpret mechanism rather than relying on a single measurement.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant PAI-1 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013874344301,"sku":"P0145-50UG","price":533.0,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013874377069,"sku":"P0145-200UG","price":1066.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013874409837,"sku":"P0145-1MG","price":3198.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_ca4da980-e262-4d68-a642-44c5cc479616.jpg?v=1770539260"},{"product_id":"recombinant-bovine-ifng-bhp10800033","title":"Recombinant Bovine IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG, IFI, IFN gamma, IFNG, IFN-γ, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Bovine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-166\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 16.9 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876212077,"sku":"P0146-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876244845,"sku":"P0146-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876277613,"sku":"P0146-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_8ed73916-3d1e-43e1-863e-0b29ef5f8dfa.jpg?v=1770539260"},{"product_id":"recombinant-chicken-ifng-bhp10800034","title":"Recombinant Chicken IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG, IFI, IFN gamma, IFNG, IFN-γ, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Chicken\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 20-164\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 16.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876310381,"sku":"P0147-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876343149,"sku":"P0147-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876375917,"sku":"P0147-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_3033a1d3-5933-40ea-9e34-fa2b7d47f759.jpg?v=1770539260"},{"product_id":"recombinant-canine-ifng-bhp10800035","title":"Recombinant Canine IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG, IFI, IFN gamma, IFNG, IFN-γ, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Canine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-166\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 16.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876408685,"sku":"P0148-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876441453,"sku":"P0148-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876474221,"sku":"P0148-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_4b7b72f8-331f-4790-838d-e0f5bad0195a.jpg?v=1770539260"},{"product_id":"recombinant-human-ifng-bhp10800036","title":"Recombinant Human IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Interferon gamma, IFN-gamma, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-166\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 16 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 95% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 0.01 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 5% Sucrose, 4% Mannitol, 0.02% Tween 80, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial at 10000 rpm for 30 s before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured in anti-viral assays using HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 0.2-0.7 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876506989,"sku":"P0149-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876539757,"sku":"P0149-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876572525,"sku":"P0149-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_e38273db-0933-4c7a-bc40-b1d2763905b6.jpg?v=1770539261"},{"product_id":"recombinant-mouse-ifng-bhp10800037","title":"Recombinant Mouse IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG, IFI, IFN gamma, IFNG, IFN-γ, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 23-155\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 14 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 95% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 0.01 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 4 mM HCl.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial at 10000 rpm for 30 s before opening, reconstitute in 4 mM HCl to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured in an anti-viral assay using L-929 mouse fibroblast cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 0.4-1 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876605293,"sku":"P0150-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876638061,"sku":"P0150-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876670829,"sku":"P0150-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_904aacbc-3bb4-46b5-bb57-0cc1023c2d98.jpg?v=1770539261"},{"product_id":"recombinant-porcine-ifng-bhp10800038","title":"Recombinant Porcine IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG, IFI, IFN gamma, IFNG, IFN-γ, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Porcine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-166\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 16.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876703597,"sku":"P0151-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876736365,"sku":"P0151-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876769133,"sku":"P0151-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_e7c19901-8a2c-4a46-adf4-60749d123f7d.jpg?v=1770539261"},{"product_id":"recombinant-rat-ifng-bhp10800039","title":"Recombinant Rat IFNG","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFNG\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IFG, IFI, IFN gamma, IFNG, IFN-γ, Immune interferon.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eIFNG\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how IFNG participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect IFNG to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 23-156\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 15.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured in an anti-viral assay using L-929 mouse fibroblast cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 0.2-0.6 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eIFNG\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant IFNG is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876801901,"sku":"P0152-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876834669,"sku":"P0152-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876867437,"sku":"P0152-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_9338f951-9909-4a95-bc6a-c330606cfcc7.jpg?v=1770539262"},{"product_id":"recombinant-bovine-tnfa-bhp10800040","title":"Recombinant Bovine TNFA","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTNFA\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e APC1 protein, Cachectin, Cachetin, DIF, TNF, monocyte-derived.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eTNFA\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how TNFA participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect TNFA to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Bovine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 78-234\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eTNFA\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant TNFA is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876900205,"sku":"P0153-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013876932973,"sku":"P0153-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013876965741,"sku":"P0153-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_76ba5fb9-8bd3-41f6-b48f-aaa8a53d10c4.jpg?v=1770539262"},{"product_id":"recombinant-canine-tnfa-bhp10800041","title":"Recombinant Canine TNFA","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTNFA\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e APC1 protein, Cachectin, Cachetin, DIF, TNF, monocyte-derived.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eTNFA\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how TNFA participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect TNFA to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Canine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 77-233\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eTNFA\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant TNFA is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013876998509,"sku":"P0154-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877031277,"sku":"P0154-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877064045,"sku":"P0154-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_14f700c0-965a-4fd8-9ed2-efec5e8cff4d.jpg?v=1770539262"},{"product_id":"recombinant-guinea-pig-tnfa-bhp10800042","title":"Recombinant Guinea Pig TNFA","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGuinea Pig TNFA\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e APC1 protein, Cachectin, Cachetin, DIF, TNF, monocyte-derived.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eGuinea Pig TNFA\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Guinea Pig TNFA participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Guinea Pig TNFA to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Guinea Pig\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 80-234\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17.1 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eGuinea Pig TNFA\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Guinea Pig TNFA is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877096813,"sku":"P0155-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877129581,"sku":"P0155-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877162349,"sku":"P0155-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_c70d3e40-5f6a-4ac2-8633-83175bdc4097.jpg?v=1770539262"},{"product_id":"recombinant-mouse-tnfa-bhp10800043","title":"Recombinant Mouse TNFA","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTNFA\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e APC1 protein, Cachectin, Cachetin, DIF, TNF, monocyte-derived.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eTNFA\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how TNFA participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect TNFA to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 80-235\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured in a cytotoxicity assay using L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin. The ED50 for this effect is 20-60 pg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eTNFA\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant TNFA is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877195117,"sku":"P0157-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877227885,"sku":"P0157-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877260653,"sku":"P0157-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_dbd9f9c1-0a0f-4da0-8219-25383d46edb4.jpg?v=1770539263"},{"product_id":"recombinant-porcine-tnfa-bhp10800044","title":"Recombinant Porcine TNFA","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTNFA\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e APC1 protein, Cachectin, Cachetin, DIF, TNF, monocyte-derived.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eTNFA\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how TNFA participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect TNFA to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Porcine\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 78-232\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 17.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eTNFA\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant TNFA is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877293421,"sku":"P0158-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877326189,"sku":"P0158-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877358957,"sku":"P0158-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_d21a1ced-78bf-4399-ab38-050f9645f188.jpg?v=1770539263"},{"product_id":"recombinant-guinea-pig-ccl2-bhp10800045","title":"Recombinant Guinea Pig CCL2","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGuinea Pig CCL2\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e AI323594, Ccl2, chemokine (C C motif) ligand 2, HC11, JE, MCAF.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eGuinea Pig CCL2\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how Guinea Pig CCL2 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect Guinea Pig CCL2 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Guinea Pig\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-120\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 11.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eGuinea Pig CCL2\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant Guinea Pig CCL2 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877391725,"sku":"P0159-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877424493,"sku":"P0159-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877457261,"sku":"P0159-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_5ea0be07-386c-4f06-990b-6c126795dfc3.jpg?v=1770539264"},{"product_id":"recombinant-human-ccl2-bhp10800046","title":"Recombinant Human CCL2","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCCL2\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e AI323594, Ccl2, chemokine (C C motif) ligand 2, HC11, JE, MCAF.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eCCL2\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CCL2 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CCL2 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-99\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 9.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CCR2A. The ED50 for this effect is 10-30 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eCCL2\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CCL2 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877490029,"sku":"P0160-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877522797,"sku":"P0160-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877555565,"sku":"P0160-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_f0588837-134e-43b5-b064-caa945f4f5bb.jpg?v=1770539264"},{"product_id":"recombinant-mouse-ccl2-bhp10800047","title":"Recombinant Mouse CCL2","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCCL2\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e AI323594, Ccl2, chemokine (C C motif) ligand 2, HC11, JE, MCAF.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eCCL2\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CCL2 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CCL2 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-96\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 8.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CCR2A. The ED50 for this effect is typically 5-15 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eCCL2\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CCL2 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877588333,"sku":"P0161-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877621101,"sku":"P0161-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877653869,"sku":"P0161-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_8d822306-b1da-4d9a-b7ad-c09c3e618096.jpg?v=1770539264"},{"product_id":"recombinant-mouse-ccl7-bhp10800048","title":"Recombinant Mouse CCL7","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCCL7\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e C-C motif chemokine 7, CCL7, chemokine (C-C motif) ligand 7, FIC, MARC, MCP-3.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eCCL7\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CCL7 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CCL7 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-97\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 8.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReported bioactivity (supplier data):\u003c\/strong\u003e Measured by its ability to chemoattract 2-day cultured human monocytes. The ED50 for this effect is 1-3 µg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eCCL7\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CCL7 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877686637,"sku":"P0162-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877719405,"sku":"P0162-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877752173,"sku":"P0162-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_2915f305-0487-4e75-905e-79bba290340a.jpg?v=1770539265"},{"product_id":"recombinant-rat-cxcl2-bhp10800049","title":"Recombinant Rat CXCL2","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL2\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e chemokine (C-X-C motif) ligand 2, CINC-2a, CINC3, CINC-3, C-X-C Motif Chemokine 2, CXCL2.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eCXCL2\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CXCL2 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CXCL2 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 32-100\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 7.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eCXCL2\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CXCL2 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877784941,"sku":"P0163-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877817709,"sku":"P0163-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877850477,"sku":"P0163-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_45c7160f-2dcf-4ab7-a26a-15d7d79868fa.jpg?v=1770539265"},{"product_id":"recombinant-human-cxcl9-bhp10800050","title":"Recombinant Human CXCL9","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL9\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e chemokine (C-X-C motif) ligand 9, CMK, crg-10, C-X-C motif chemokine 9, CXCL9, Gamma-interferon-induced monokine.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eCXCL9\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CXCL9 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CXCL9 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 23-125\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 11.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eCXCL9\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CXCL9 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877883245,"sku":"P0164-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013877916013,"sku":"P0164-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013877948781,"sku":"P0164-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_eef4478d-fd06-4bc6-a4ef-5a998e573c9d.jpg?v=1770539266"},{"product_id":"recombinant-human-ccl11-bhp10800051","title":"Recombinant Human CCL11","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCCL11\u003c\/strong\u003e is used in \u003cstrong\u003eresearch use only (RUO)\u003c\/strong\u003e settings as a defined recombinant protein reagent. Bench researchers commonly leverage recombinant proteins to create controlled experimental conditions for mechanistic studies, assay development, interaction mapping, and quantitative benchmarking across model systems.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e C-C motif chemokine 11, CCL11, chemokine (C-C motif) ligand 11, Eosinophil chemotactic protein, Eotaxin, eotaxin-1.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eproteins like \u003cstrong\u003eCCL11\u003c\/strong\u003e are studied as soluble signaling factors that coordinate cell–cell communication through receptor-mediated pathways. Researchers frequently use recombinant ligands to probe dose-responsive signaling programs, map receptor interactions, and benchmark functional assays in controlled experimental conditions.\u003c\/p\u003e\u003cp\u003eMechanistically, researchers often analyze how CCL11 participates in pathway networks through molecular interactions, localization, and regulated activity. Depending on the target class, this can involve receptor-mediated signaling, enzymatic catalysis, complex assembly, or structural organization that shapes downstream cellular phenotypes.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eResearch relevance:\u003c\/strong\u003e RUO studies frequently connect CCL11 to perturbations such as immune stimulation, stress signaling, differentiation cues, metabolic remodeling, or engineered genetic modulation—then interpret downstream readouts using complementary pathway markers.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular features matter in RUO experiments:\u003c\/strong\u003e domain boundaries, oligomerization state, and PTM sensitivity can influence binding behavior, stability, and functional readouts in vitro.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eConstruct \/ expression region:\u003c\/strong\u003e aa 24-97\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eApprox. molecular weight:\u003c\/strong\u003e 8.3 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e Greater than 90% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEndotoxin level:\u003c\/strong\u003e \u0026lt; 1 EU\/µg as determined by LAL test.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized powder\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a 0.2 μm filtered solution of 10 mM Hepes, 150 mM NaCl with 5% trehalose, pH 7.4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg\/ml by gently pipetting 2-3 times, don't vortex.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e For many extracellular ligands and receptor ectodomains, \u003cstrong\u003edisulfide bonds\u003c\/strong\u003e and \u003cstrong\u003eglycosylation\u003c\/strong\u003e can influence stability and binding. PTM dependence is target- and assay-specific. Prokaryotic expression typically yields non-glycosylated protein; consider whether eukaryotic PTMs are required for your assay context.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e This protein is produced in a \u003cstrong\u003eprokaryotic (E. coli)\u003c\/strong\u003e system, which typically yields a defined, non-glycosylated form. This can be advantageous for mechanistic studies, binding assays, and antigen\/standard use where mammalian PTMs are not required.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification transparency (research credibility):\u003c\/strong\u003e In research-grade recombinant protein production, constructs are commonly purified via affinity and polishing steps (e.g., chromatography) to reduce contaminants and improve batch-to-batch consistency. When present, affinity tags (e.g., His\/GST\/Fc) can simplify purification; tag presence or removal can influence certain binding or structural assays.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eForm and handling context:\u003c\/strong\u003e Lyophilized proteins are frequently used in RUO labs to support stability during storage and shipment, while formulation components and reconstitution conditions can impact solubility and aggregation—important considerations when comparing studies across publications.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e In cell-based research models, changes in signaling factor levels or responsiveness to \u003cstrong\u003eCCL11\u003c\/strong\u003e can reflect altered receptor expression, pathway feedback, or microenvironmental cues. Researchers often interpret results alongside orthogonal markers (e.g., pathway phosphorylation, transcriptional programs, or secreted mediator panels) to separate direct ligand effects from downstream network responses.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUsing recombinant protein as a defined reagent:\u003c\/strong\u003e recombinant CCL11 is commonly used as a quantitative input for assay calibration, antibody\/ligand binding studies, pathway reconstitution, and controlled perturbation experiments. Researchers often consider isoforms, fragments, or construct boundaries when comparing results across studies.\u003c\/p\u003e","brand":"Fine Test","offers":[{"title":"50 ug","offer_id":53013877981549,"sku":"P0165-50UG","price":374.4,"currency_code":"USD","in_stock":true},{"title":"200 ug","offer_id":53013878014317,"sku":"P0165-200UG","price":748.8,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53013878047085,"sku":"P0165-1MG","price":2246.4,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E8_9B_8B_E7_99_BD_4177bae2-012d-4721-9c38-a0d39ff24ac9.jpg?v=1770539266"}],"url":"https:\/\/www.ebiohippo.com\/collections\/finetest-protein.oembed","provider":"BioHippo","version":"1.0","type":"link"}