{"title":"Cell Biology Proteins \u0026 Peptides","description":null,"products":[{"product_id":"ulp1-sumo-protease-ulp1-peptidase-bhp13700001","title":"Ulp1 (SUMO Protease \/Ulp1 peptidase)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUlp1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Ulp1 peptidase; SUMO Protease.\u003c\/p\u003e\u003cp\u003eRecombinant Yeast Ulp1 protein expressed in E.coli.\u003c\/p\u003e\u003cp\u003eSUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eUlp1\u003c\/strong\u003e is connected to ubiquitin\/SUMO-dependent regulation of protein stability, localization, and signaling duration. These modification pathways act as reversible molecular switches that help tune pathway outputs during stress, cell-cycle control, and quality-control processes. This target is frequently investigated in research themes such as \u003cstrong\u003eMetabolism \u0026amp; Enzymology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 28.7 KD\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant yeast ULP1 consists of 219 amino acids and has a predicted molecular mass of 28.7 KD. The apparent molecular mass of the ULP1 is approximately 28 KD in SDS-PAGE under reducing conditions due to glycosylation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from ULP1 isoform (Q02724) (403-621 aa + N-terminal Poly-6*His tag C-terminal Poly-6*His tag) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For ubiquitin\/SUMO pathway enzymes, catalytic activity often depends on correct folding and active-site integrity rather than glycosylation.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e Many recombinant proteins incorporate affinity tags (e.g., His, GST, Fc) to aid purification and capture in binding assays. Where relevant, tag status can be considered when comparing activity or interaction data.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris , 500 mM NaCl pH8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Ubiquitin\/SUMO pathway measurements can reflect changes in protein turnover, signaling dwell time, and stress-adaptation programs. Mechanistic interpretation is often strengthened by pairing modification-state readouts with measurements of substrate abundance, localization, and interaction partners.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"500 U","offer_id":52997734433133,"sku":"PRP3001-500U","price":69.0,"currency_code":"USD","in_stock":true},{"title":"1000 U","offer_id":52997734465901,"sku":"PRP3001-1000U","price":129.0,"currency_code":"USD","in_stock":true},{"title":"5000 U","offer_id":52997734498669,"sku":"PRP3001-5000U","price":499.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-bfgf-protein-bhp13700014","title":"Human bFGF Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFGF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e BFGF; FGF-2; FGFB; HBGF-2; Fibroblast growth factor 2; FGF2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman bFGF protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eFGF\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 17.3 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human bFGF protein consists of 158 amino acids and predicts a molecular mass of 17.3 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human bFGF soluble form (NP_09038) (Ala135-Ser288) was expressed, with an initial Met at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 150mM NaCl 20mM Tris , pH 7.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997734793581,"sku":"PRP1010-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997734826349,"sku":"PRP1010-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997734859117,"sku":"PRP1010-100UG","price":219.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997734891885,"sku":"PRP1010-1MG","price":1129.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1010.png?v=1770191155"},{"product_id":"mouse-bfgf-protein-bhp13700015","title":"Mouse bFGF Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFGF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e BFGF; FGF-2; FGFB; HBGF-2; Fibroblast growth factor 2; FGF2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse bFGF protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eFGF\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 18.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse bFGF protein consists of 146 amino acids and predicts a molecular mass of 18.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse bFGF soluble form (NP_15655) (Pro10-Ser154) was expressed, with an initial Met at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 150 mM NaCl 20mM PB , pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997734924653,"sku":"PRP1011-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997734957421,"sku":"PRP1011-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997734990189,"sku":"PRP1011-100UG","price":219.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735022957,"sku":"PRP1011-1MG","price":1129.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1011-2.png?v=1770191156"},{"product_id":"human-il-1-protein-bhp13700021","title":"Human IL-1? Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IL-1; IL-1 beta; IL-1B; IL1-BETA; IL1F2; Interleukin-1 beta; IL1B.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-1β protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.01 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 17 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human IL-1β consists of 154 amino acids and has a predicted molecular mass of 17 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human IL-1β (NP_000567.1)(Ala 117-Ser 269) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Immobilized human IL-1β at 5 μg\/mL (100 μl\/well) can bind Human IL-1R1 with a linear range of 3.125-200 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997735743853,"sku":"PRP1019-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997735776621,"sku":"PRP1019-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735809389,"sku":"PRP1019-100UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735842157,"sku":"PRP1019-1MG","price":3769.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1019.png?v=1770191159"},{"product_id":"mouse-il-1-protein-bhp13700022","title":"Mouse IL-1? Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IL-1; IL-1 beta; IL-1B; IL1-BETA; IL1F2; Interleukin-1 beta; IL1B.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IL-1β protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1.0 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 17 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse IL-1β protein consists of 153 amino acids and predicts a molecular mass of 17 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse IL-1β protein isoform (P10749)(Val118-Ser269) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997735874925,"sku":"PRP1119-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997735907693,"sku":"PRP1119-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735940461,"sku":"PRP1119-100UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735973229,"sku":"PRP1119-1MG","price":3769.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1119.png?v=1770191159"},{"product_id":"human-mcp2-protein-sumo-tag-bhp13700023","title":"Human MCP2 Protein, SUMO tag","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMCP2\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e CCL; HC14; MCP-2; SCYA8; SCYA10.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman MCP2 protein, SUMO tag, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1.0 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eMCP2\u003c\/strong\u003e is connected to ubiquitin\/SUMO-dependent regulation of protein stability, localization, and signaling duration. These modification pathways act as reversible molecular switches that help tune pathway outputs during stress, cell-cycle control, and quality-control processes. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 20.3 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human MCP2 consisting of 184 amino acids and has a calculated molecular mass of 20.3 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human MCP2 (Gln24-Pro99) was fused with the SUMO tag at the N-terminus .\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For ubiquitin\/SUMO pathway enzymes, catalytic activity often depends on correct folding and active-site integrity rather than glycosylation.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e SUMO tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Ubiquitin\/SUMO pathway measurements can reflect changes in protein turnover, signaling dwell time, and stress-adaptation programs. Mechanistic interpretation is often strengthened by pairing modification-state readouts with measurements of substrate abundance, localization, and interaction partners.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997736005997,"sku":"PRP1020-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997736038765,"sku":"PRP1020-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997736071533,"sku":"PRP1020-100UG","price":569.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1020.png?v=1770191160"},{"product_id":"mouse-lif-protein-his-tag-bhp13700028","title":"Mouse LIF Protein, His tag","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLIF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Leukemia inhibitory factor; Differentiation-stimulating factor; lif; D factor.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse LIF protein, C-His tag, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.01 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLIF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 20.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse LIF protein consists of 186 amino acids and has a predicted molecular mass of 20.5 KD.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse LIF protein (P09056)(Ser23-Phe202) was expressed with a polyhistidine tag at the C-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measured by its ability to induce proliferation in M-NFS-60 cells.The ED50 for this effect is 8.023 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997736563053,"sku":"PRP1126-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997736595821,"sku":"PRP1126-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997736628589,"sku":"PRP1126-100UG","price":379.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997736661357,"sku":"PRP1126-1MG","price":2509.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1126.png?v=1770191162"},{"product_id":"human-il-36-protein-bhp13700029","title":"Human IL-36à Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Interleukin-36 Alpha; FIL1 Epsilon; Interleukin-1 Epsilon; IL-1 Epsilon; Interleukin-1 Family Member 6; IL-1F6; IL36A; FIL1E; IL1E; IL1F6.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-36α protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 17 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-36α consists of 153 amino acids and has a predicted molecular mass of 17 KD.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IL-36α (Q9UHA7)(Lys6-Phe158) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997736694125,"sku":"PRP1027-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997736726893,"sku":"PRP1027-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997736759661,"sku":"PRP1027-100UG","price":219.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997736792429,"sku":"PRP1027-1MG","price":999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1027.png?v=1770191163"},{"product_id":"rat-il-1-protein-bhp13700030","title":"Rat IL-1β Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IL-1; IL-1 beta; IL-1B; IL1-BETA; IL1F2; Interleukin-1 beta; IL1B.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Rat.\u003c\/p\u003e\u003cp\u003eRat IL-1β protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1.0 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 17.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Rat IL-1β consists of 152 amino acids and has a predicted molecular mass of 17.4 KDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Rat IL-1β (Q63264) (Val117-Ser268) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM Tris with 150 mM NaCl,, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997736825197,"sku":"PRP1219-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997736857965,"sku":"PRP1219-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997736890733,"sku":"PRP1219-100UG","price":469.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997736923501,"sku":"PRP1219-1MG","price":2999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1219.png?v=1770191163"},{"product_id":"human-trail-protein-bhp13700031","title":"Human TRAIL Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRAIL\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tumor Necrosis Factor Ligand Superfamily Member 10; Apo-2 Ligand; Apo-2L; TNF-Related Apoptosis-Inducing Ligand; Protein TRAIL; CD253; TNFSF10; APO2L; TRAIL.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman TRAIL protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1.0 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRAIL\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 19.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human TRAIL consists of 168 amino acids and has a predicted molecular mass of 19.5 KDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human TRAIL isoform (P50591-1) (Val114-Gly281) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 92 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measured by its ability to induce cytotoxicity in the presence of the metabolic inhibitor actinomycin D.The ED50 for this effect is 26.27 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris, 150 mM NaCl, pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997736956269,"sku":"PRP1028-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997736989037,"sku":"PRP1028-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997737021805,"sku":"PRP1028-100UG","price":229.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997737054573,"sku":"PRP1028-1MG","price":999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1028.png?v=1770191163"},{"product_id":"rat-bfgf-protein-bhp13700106","title":"Rat bFGF Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFGF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibroblast Growth Factor 2; FGF-2; Basic Fibroblast Growth Factor; bFGF; Heparin-Binding Growth Factor 2; HBGF-2; FGF2; FGFB.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Rat.\u003c\/p\u003e\u003cp\u003eRat bFGF protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1.0 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eFGF\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 16.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Rat bFGF protein consists of 145 amino acids (N-Met) and has a predicted molecular mass of 16.2 KD. The apparent molecular mass of the Rat FGF2 is approximately 16.2 KD in SDS-PAGE under reducing conditions due to glycosylation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Rat FGF2 isoform (P13109) (Ala11-Ser154) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris,150 mM NaCl, pH8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997737677165,"sku":"PRP1210-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997737709933,"sku":"PRP1210-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997737742701,"sku":"PRP1210-100UG","price":379.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-il-36-protein-bhp13700112","title":"Human IL-36? Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1E\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Interleukin 36 GammaInterleukin-1 Homolog 1; Interleukin-1 Epsilon; IL-1RP2; IL-1F9; IL-1H1; IL1H1; IL1E; Interleukin 1-Related Protein 2; Interleukin-36 Gamma; IL1RP2; IL1F9.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-36γ protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1E\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 16.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-36-gamma consists of 152 amino acids and has a predicted molecular mass of 16.7 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IL-36γ(Q9NZH8)(Ser18-Asp169) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM tris 50 mM NaCl, pH 6.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997737939309,"sku":"PRP1029-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997737972077,"sku":"PRP1029-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738004845,"sku":"PRP1029-100UG","price":229.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997738037613,"sku":"PRP1029-1MG","price":1879.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1029.jpg?v=1770191169"},{"product_id":"human-il-1-il1a-protein-bhp13700126","title":"Human IL-1à\/IL1A Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1A\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e BAF; Hematopoietin-1; IL1 alpha; IL-1 alpha; IL1; IL1A; IL-1A; IL1-ALPHA; IL1F1; IL-1F1; IL1F1hematopoietin-1; interleukin 1, alpha; interleukin-1 alpha; LAF; LEM; preinterleukin 1 alpha; pro-interleukin-1-alpha.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-1α\/IL1A protein, expressed in E.coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1A\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 18 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-1α protein consists of 160 amino acids (N-Met) and has a predicted molecular mass of 18 kDa. The apparent molecular mass of the Human IL-1α protein is approximately 18 kDa in SDS-PAGE under reducing conditions due to glycosylation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IL-1α protein isoform (P01583-1, Ser113-Ala271) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris, 150 mM NaCl, pH7.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"2 ug","offer_id":52997738463597,"sku":"PRP1021-2UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"10 ug","offer_id":52997738496365,"sku":"PRP1021-10UG","price":139.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738529133,"sku":"PRP1021-100UG","price":569.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1021.jpg?v=1770191173"},{"product_id":"mouse-rankl-protein-bhp13700128","title":"Mouse RANKL Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eRANKL\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tumor necrosis factor ligand superfamily member 11; RANKL; CD254; ODF; OPGL; TNFSF11; TRANCE.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse RANKL protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eRANKL\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 19 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse sRANKL consists of 174 amino acids(N-Met) and has a predicted molecular mass of 19 kDa. The apparent molecular mass of the Mouse sRANKL protein is approximately 19 kDa in SDS-PAGE under reducing conditions.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse RANKL soluble form (O35235)(Pro143-Asp316) was expressed\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e ≥ 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Immobilized Mouses RANKL at 1μg\/mL(100μl\/well)can bind Human OPG(C-Fc),The EC50 of Human OPG is 55 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris, 150 mM NaCl pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997738725741,"sku":"PRP1114-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997738758509,"sku":"PRP1114-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738791277,"sku":"PRP1114-100UG","price":769.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997738824045,"sku":"PRP1114-1MG","price":6369.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1114.png?v=1770191172"},{"product_id":"human-transferrin-protein-his-tag-bhp13700134","title":"Human Transferrin Protein, His tag","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRANSFERRIN\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e PRO2086 Protein; TFQTL1 Protein; HEL-S-71p Protein, Human; PRO1557 Protein; Transferrin Protein,Siderophilin, partially saturated; PRO1558 Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman Transferrin protein, expressed in HEK293 Cells\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per µg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRANSFERRIN\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 76.6 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human Transferrin protein consists of 690 amino acids and has a predicted molecular mass of 76.6 kDa. The apparent molecular mass of the Human Transferrin protein is approximately 70-100 kDa in SDS-PAGE under reducing conditions.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human Transferrin protein isoform (P02787, Met 1-Pro 698) with a polyhistidine tag at the C-terminus was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e ≥ 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Mammalian expression can support native-like folding, disulfide bond formation, and glycosylation—features that are often important for secreted proteins, receptors, and adhesion molecules.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e HEK293 Cells. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997739512173,"sku":"PRP2041-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997739544941,"sku":"PRP2041-50UG","price":249.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997739577709,"sku":"PRP2041-100UG","price":429.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739610477,"sku":"PRP2041-1MG","price":3739.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2041.jpg?v=1770191176"},{"product_id":"human-annexin-v-anxa5-protein-bhp13700140","title":"Human Annexin V\/ANXA5 protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eANNEXIN\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Annexin A5; Anchorin CII; Annexin V; Annexin-5; Calphobindin I; CBP-I; Endonexin II; Lipocortin V; Placental Anticoagulant Protein 4; PP4; Placental Anticoagulant Protein I; PAP-I; Thromboplastin Inhibitor; Vascular Anticoagulant-Alpha; VAC-Alpha; ANXA5; ANX5; ENX2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman Annexin V\/ANXA5 protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eAnnexin V (ANXA5 or Annexin A5) is a member of the annexin family of intracellular proteins that binds to phosphatidylserine (PS) in a calcium-dependent manner. Annexin V is a multifunctional protein that is highly expressed on the apical surfaces of syncytiotrophoblasts, this protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex and plays an important role in haemostatic regulations, maintaining blood fluidity of the placenta. Annexin V is also a protein kinase C and phospholipase A2 inhibitor. It participate in inflammation, cellular signal transduction, growth and differentiation.Annexin V is important for normal CFTR chloride channel activity.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eANNEXIN\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 36 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human Annexin V\/ANXA5 consists of 320 amino acids and migrates with an apparent molecular mass of 36 kDa as estimated in SDS-PAGE under reducing conditions.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human Annexin V\/ANXA5 (P08758) (Met1-Asp320) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e ≥ 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Binds to phosphatidylserine (PS). Exhibits anti-phospholipase activity\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"100 ug","offer_id":52997740101997,"sku":"PRP3003-100UG","price":229.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997740134765,"sku":"PRP3003-1MG","price":1899.0,"currency_code":"USD","in_stock":true},{"title":"10 mg","offer_id":52997740167533,"sku":"PRP3003-10MG","price":6999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP3003.png?v=1770191178"},{"product_id":"human-cxcl3-protein-his-tag-animal-free-bhp13700145","title":"Human CXCL3 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL3\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e GRO-γ: MGSAγ, MIP-2β, GRO3; CXCL3,CXCL-3,GRO-γ:MGSAγ,MIP-2β,GRO3.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 3 (CXCL3) also named Growth-regulated oncogene gamma (GROγ), which is a chemokine of the intercrine alpha family. CXCL3 is a 8kDa protein containing 73 amino acid residues. During inflammation, CXCL3 is activated by the TNF and IL-1 which mediates the monocytes migration and adhesion by targeting the CXCR2. CXCL3 activates the JNK activity which induce the cell differentiation.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL3\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 8.67 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human CXCL3 consists of 73 amino acids and predicts a molecular mass of 8.67 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human CXCL3 (Ala35-Asn107) (P19876) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with human CXCR3.The ED₅₀ for this effect is \u0026lt;2 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997740724589,"sku":"PRP1006-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997740757357,"sku":"PRP1006-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740790125,"sku":"PRP1006-100UG","price":619.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997740822893,"sku":"PRP1006-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1006.png?v=1770191181"},{"product_id":"human-sonic-hedgehog-protein-bhp13700150","title":"Human Sonic Hedgehog Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSONIC\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e HHG1 Protein, Human; HLP3 Protein, Human; HPE3 Protein, Human; MCOPCB5 Protein, Human; SMMCI Protein, Human; Sonic hedgehog Protein, Human; TPT Protein, Human; TPTPS Protein, Human; HHG1 Protein; HLP3 Protein; HPE3 Protein; MCOPCB5 Protein; SMMCI Protein; Sonic hedgehog Protein; TPT Protein; TPTPS Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman Sonic Hedgehog Protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSONIC\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 23.84 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human SHH consists of 176 amino acids with 6×His tag at N terminus and predicts a molecular mass of 23.84 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human SHH (Q15465.1) (Gly25-Gly197) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from PBS, pH 7.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"20 ug","offer_id":52997741379949,"sku":"PRP1032-20UG","price":219.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997741412717,"sku":"PRP1032-100UG","price":699.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997741445485,"sku":"PRP1032-1MG","price":1699.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1032.png?v=1770191184"},{"product_id":"human-galectin-1-protein-bhp13700151","title":"Human Galectin-1 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGALECTIN-1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e GAL1 Protein; Galectin-1 Protein; GBP Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman Galectin-1 Protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGALECTIN-1\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 14 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human Galectin-1 consists of 135 amino acids and predicts a molecular mass of 14 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human Galectin-1 (NP_002296.1)(Met1- Asp135) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 97 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM PB with 50 mM NaCl, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"20 ug","offer_id":52997741478253,"sku":"PRP1033-20UG","price":79.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997741511021,"sku":"PRP1033-100UG","price":309.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997741543789,"sku":"PRP1033-1MG","price":1099.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1033.png?v=1770191185"},{"product_id":"human-baff-protein-bhp13700153","title":"HumanÿBAFF Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBAFF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e BAFF Protein, Human; BLYS Protein, Human; CD257 Protein, Human; DTL Protein, Human; TALL-1 Protein, Human; TALL1 Protein, Human; THANK Protein, Human; TNFSF20 Protein, Human; ZTNF4 Protein, Human; BAFF Protein; BLYS Protein; CD257 Protein; DTL Protein; TALL-1 Protein; TALL1 Protein; THANK Protein; TNFSF20 Protein; ZTNF4 Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman BAFF Protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBAFF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 22.9 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human SHH consists of 152 amino acids with 6×His tag at N terminus and predicts a molecular mass of 22.9 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human BAFF (Q9Y275-1) (Ala 134-Leu 285) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 99 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Immobilized Human BAFF at 1μg\/mL (100μl\/well) can bind Human BCMA(C-mFc),The EC50 of Human BCMA is 0.2 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from PBS, pH 7.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997741674861,"sku":"PRP1035-10UG","price":99.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997741707629,"sku":"PRP1035-50UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997741740397,"sku":"PRP1035-1MG","price":4699.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-mouse-rat-activin-a-protein-bhp13700160","title":"Human\/Mouse\/Rat Activin A Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eActivin A\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e rHuActivin A; Inhibin beta A chain; INHBA; Activin A ACV-A; Activin A；rHuActivin A.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human\/Mouse\/Rat.\u003c\/p\u003e\u003cp\u003eHuman\/Mouse\/Rat Activin A Protein,expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eActivin A\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\/Mouse\/Rat\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13.0 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The Human\/Mouse\/Rat Activin A consists of 116 amino acids and predicts a molecular mass of 13.0 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human Activin A (NP_002183.1)(Gly311-Ser426) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 97 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM Tris, 50mM NaCl, pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"20 ug","offer_id":52997742330221,"sku":"PRP1042-20UG","price":79.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997742362989,"sku":"PRP1042-100UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997742395757,"sku":"PRP1042-500UG","price":1169.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1042.png?v=1770191193"},{"product_id":"human-bmp-13-protein-bhp13700161","title":"Human BMP-13 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBMP-13\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Bone morphogenetic protein 13; Human BMP-13 Protein; Bone morphogenetic protein 13；BMP-13.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman BMP-13 Protein,expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBMP-13\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human BMP-13 consists of 120 amino acids and predicts a molecular mass of 13.5 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human BMP-13 (NP_001001557.1) (Thr335-Arg454) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 96 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM Tris, 50mM NaCl, pH 7.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997742461293,"sku":"PRP1043-10UG","price":79.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997742494061,"sku":"PRP1043-50UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997742526829,"sku":"PRP1043-500UG","price":1669.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1043.png?v=1770191194"},{"product_id":"human-g-csf-protein-bhp13700163","title":"Human G-CSF Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGM-CSF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e CSF-3; MGI-1G; GM-CSF beta; MGC45931; Pluripoietin; Human G-CSF Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman G-CSF Protein,expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGM-CSF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 18.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human G-CSF protein consists of 174 amino acids with a Met in N terminal and predicts a molecular mass of 18.7 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human G-CSF (Thr31-Pro204) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;98% as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measured by its ability to induce proliferation in M-NFS-60 cells. The ED50 for this effect is 0.2569 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Liquid in from PBS. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997742690669,"sku":"PRP1045-5UG","price":79.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997742723437,"sku":"PRP1045-20UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997742756205,"sku":"PRP1045-100UG","price":1669.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997742788973,"sku":"PRP1045-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1045.png?v=1770191195"},{"product_id":"human-bmp-3-protein-bhp13700165","title":"Human BMP-3 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eOSTEOGENIC\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e BMP; BMP-3; BMP-3A; Bone morphogenetic protein; Bone morphogenetic protein 3; bone morphogenetic protein 3 (osteogenic); Bone morphogenetic protein 3A; bone morphogenetic protein-3; Osteogenin; Human BMP-3 Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman BMP-3 Protein,expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eOSTEOGENIC\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 12.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human BMP-3 consists of 111 amino acids and predicts a molecular mass of 12.5 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human BMP-3 (Gln363-\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997742920045,"sku":"PRP1047-10UG","price":79.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997742952813,"sku":"PRP1047-50UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997742985581,"sku":"PRP1047-500UG","price":1669.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1047.png?v=1770191196"},{"product_id":"human-gdf3-protein-bhp13700187","title":"Human GDF3 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGDF3\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e C78318; ecat9; GDF 3; GDF-3; GDF3; GDF3_HUMAN; Growth differentiation factor 3; Growth\/differentiation factor 3; KFS3; MCOP7; MCOPCB6; MGC123990; MGC123991; RGD1564178; Vgr 2; Vgr2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eGDF-3 (previously called Vgr-2) is a TGF-beta superfamily member belonging to the growth\/differentiation factor family. GDF-3 is expressed in undifferentiated embryonic stem (ES) cells, white adipose tissue and the brain. The 366 amino acid (aa) mouse GDF-3 contains a 22 aa signal sequence, a 230 aa propeptide and a 114 aa mature protein that contains one potential N-glycosylation site. The mature region contains a cysteine-knot structure that is conserved throughout family members. However, it lacks the fourth cysteine which is responsible for the formation of an inter-molecular disulfide bond, so GDF-3 may exist as a non-covalent homodimer. Mature human GDF-3 shares 83%, 83% aa sequence identity with mouse and rat GDF-3. Most of GDF-3 is present as the uncleaved prepro form. The uncleaved and the mature forms both appear to have activity, but that activity may differ. All forms can oppose BMPs. In ES cells, inhibition of BMP2 signaling by GDF-3 maintains pluripotency. GDF-3 also influences early cell fate decisions; for example, deletion of mouse GDF-3 produces defects in the anterior visceral endoderm of the pre-gastrulation embryo. GDF-3 cooperates with GDF-1 in embryogenesis, and the mature protein has nodal-like activity. Although GDF family members signal through BMP receptors (ALK1, 2, 3 and 6), which activate Smads 1, 5 and 8, GDF-3 signaling through ALK4 and ALK7, which activate Smads 2 and 3, has also been reported. In adipocytes, GDF-3 is induced by a high fat diet, promoting adipogenesis and obesity.\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per µg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGDF3\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human GDF 3 consists of 141 amino acids and predicts a molecular mass of 13 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human GDF 3(Q9NR23) (Ala251-Gly364) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 96% as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from 20mM Tris 150mM NaCl PH 8.0. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997745901933,"sku":"PRP1070-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997745934701,"sku":"PRP1070-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997745967469,"sku":"PRP1070-100UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997746000237,"sku":"PRP1070-1MG","price":2369.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-cxcl6-protein-his-tag-animal-free-bhp13700189","title":"Human CXCL6 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL6\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Granulocyte Chemotactic Protein-2,GCP-2; CXCL6,CXCL-6,CXCL 6，Granulocyte Chemotactic Protein-2,GCP-2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 6 (CXCL6) also named granulocyte chemotactic protein 2 (GCP-2), which is a chemokine of the intercrine alpha family. CXCL6 is a 8.3kDa protein containing 75 amino acid residues. CXCL6 has a significant role in resistance of gram-positive and gram-negative bacteria which is a chemotaxis for neutrophil granulocytes. CXCL6 has a role in in the process of carcinogenesis which affects proliferation and metastasis of OS cells by the interaction with CXCR1 \/CXCR2.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL6\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 8.97 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human CXCL6 consists of 75 amino acids and predicts a molecular mass of 8.97 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human CXCL6 (Val40-Asn114) (P80162) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with human CXCL6.The ED₅₀ for this effect is \u0026lt;10 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997746164077,"sku":"PRP1072-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997746196845,"sku":"PRP1072-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997746229613,"sku":"PRP1072-100UG","price":739.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997746262381,"sku":"PRP1072-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1072.png?v=1770191208"},{"product_id":"human-gdf-5-protein-bhp13700190","title":"Human GDF 5 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGDF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e growth differentiation factor 5; Growth\/differentiation factor 5; H-GDF-5.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the Human GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of Human GDF-5 is a homodimer of two 120 amino-acid polypeptide chain (monomers) linked by a single disulfide bond. Recombinant Human GDF-5 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGDF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human GDF5 consists of 120 amino acids and predicts a molecular mass of 13.5 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human GDF5 (Ala382-Arg501)(P43026) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from 40 mM Tris-HCl pH 8.0, 50 mM NaCl.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997746295149,"sku":"PRP1073-5UG","price":39.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997746327917,"sku":"PRP1073-20UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997746360685,"sku":"PRP1073-100UG","price":169.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997746393453,"sku":"PRP1073-1MG","price":1289.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-areg-protein-bhp13700192","title":"Human AREG Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAREG\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e AR; SDGF; AREGB; CRDGF.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eAREG is a one-way membrane protein consisting of 252 amino acids. AREG belongs to AREG family and contains an EGF-like domain. AREG is expressed in many tissues, including ovary, placenta, lung, kidney, stomach, colon and breast. It is related to epidermal growth factor (EGF) and transforming growth factor α (TGF-α). As an EGF-related growth factor, AREG interacts with EGF\/TGF-α receptor to promote the growth of normal epithelial cells and inhibit the growth of some invasive cancer cell lines.\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAREG\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 11.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human AREG consists of 98 amino acids and predicts a molecular mass of 11.4 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human AREG (NC_000004.12) (Ser101-Lys198) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM Tris, 800mM NaCl, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997746557293,"sku":"PRP1075-5UG","price":39.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997746590061,"sku":"PRP1075-20UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997746622829,"sku":"PRP1075-100UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997746655597,"sku":"PRP1075-1MG","price":2369.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-mouse-bmp-2-protein-bhp13700193","title":"Human\/Mouse BMP-2 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBMP-2\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e BMP2; BMP2A; Bone morphogenetic protein 2; BMP-2; Bone morphogenetic protein 2A; BMP-2A.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human\/Mouse.\u003c\/p\u003e\u003cp\u003eBone morphogenetic protein-2 (BMP-2) is a kind of bone growth regulator, belonging to protein transforming growth factor-β(TGF-β) superfamily. BMP-2 protein is involved in hedgehog pathway, TGF-β signaling pathway and cytokine-cytokine receptor interaction. BMP-2 and BMP-7 are osteogenic BMP, which have been proved to be effective in inducing osteoblast differentiation in many cell types. The active form of BMP-2 can be composed of dimers of two identical proteins or heterodimers of two related bone morphogenetic proteins.\u003c\/p\u003e\u003cp\u003eEndotoxin: Please contact us for more information.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBMP-2\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\/Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human\/Mouse BMP-2 consists of 114 amino acids and predicts a molecular mass of 13 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human\/Mouse BMP-2 (Gln283-Arg396)(P21274.3) was expressed\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM Tris,50mM NaCl, pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997746688365,"sku":"PRP1076-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997746721133,"sku":"PRP1076-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997746753901,"sku":"PRP1076-100UG","price":379.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997746786669,"sku":"PRP1076-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1076.png?v=1770191213"},{"product_id":"human-haptoglobin-protein-his-tag-bhp13700195","title":"Human Haptoglobin Protein, His tag","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHAPTOGLOBIN\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Haptoglobin.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHaptoglobin is a glycoprotein, which is synthesized in the liver and circulates in the blood. Haptoglobin is usually produced by liver cells, but it is also produced by other tissues, such as skin, lung and kidney. It is a positive acute phase protein, which binds to free hemoglobin and removes it from circulation to prevent kidney injury and iron loss after hemolysis. Decreased levels can be seen in hemolysis and impaired liver function. A high level is a sign of acute or chronic inflammation. Hemoglobin deficiency or hypohaptoglobinemia is caused by mutation of haptoglobin gene and\/or its regulatory region. Haptoglobin is also related to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, susceptibility to primary sclerosing cholangitis, idiopathic Parkinson's disease and the reduction of the incidence of plasmodium falciparum malaria.\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHAPTOGLOBIN\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 29.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human Haptoglobin consists of 245 amino acids and predicts a molecular mass of 29.5 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human Haptoglobin (AAA88080.1) (Ile162-Asn406) was expressed with 6×His tag at N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997746950509,"sku":"PRP1078-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997746983277,"sku":"PRP1078-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997747016045,"sku":"PRP1078-100UG","price":709.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997747048813,"sku":"PRP1078-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1078.png?v=1770191211"},{"product_id":"human-s100a9-protein-bhp13700198","title":"Human S100A9 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eS100A9\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e S100A9; 60B8AG; CAGB; CFAG; CGLB; L1AG; LIAG; MAC387; MIF; MRP14; NIF; P14; S100 calcium-binding protein A9; S100 calcium-binding protein A9 (calgranulin B); calgranulin B.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eProtein S100-A9, also known as S100 calcium binding protein A9, S100A9, and CAGB, is a member of the S-100 family. S100A9 is expressed by macrophages in acutely inflammed tissues and in chronic inflammation. It is also expressed in epithelial cells constitutively or induced during dermatoses. S100A9 is a calcium-binding protein. It has anti-microbial activity towards bacteria and fungi.\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eS100A9\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human S100A9 consists of 113 amino acids and migrates with an apparent molecular mass of 13.2 kDa as estimated in SDS-PAGE under reducing conditions.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Recombinant Human S100 Calcium Binding Protein A9\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 97 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 150mM NaCl,20mM Tris , pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997747343725,"sku":"PRP1081-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997747376493,"sku":"PRP1081-100UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997747409261,"sku":"PRP1081-500UG","price":619.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997747442029,"sku":"PRP1081-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1081.png?v=1770191212"},{"product_id":"human-mouse-rat-activin-a-protein-animal-free-bhp13700205","title":"Human\/Mouse\/Rat Activin A Protein (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eActivin A\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Inhibin beta A chain, Activin beta-A chain, Erythroid differentiation protein; Human\/Mouse\/Rat Activin A Protein (Animal-Free)，Activin A，Inhibin beta A chain, Activin beta-A chain, Erythroid differentiation protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman\/Mouse\/Rat Activin A Protein (Animal-Free), expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt;0.1 EU per 1 μg of the protein by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eActivin A\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13.1 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human\/Mouse\/Rat Activin A Protein consists of 116 amino acids and predicts a molecular mass of 13.1 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human\/Mouse\/Rat Activin A Protein (Gly311-Ser426) (Human: P08476, Mouse: Q04998, Rat: P18331) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997748293997,"sku":"PRP1088-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997748326765,"sku":"PRP1088-20UG","price":199.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997748359533,"sku":"PRP1088-100UG","price":669.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997748392301,"sku":"PRP1088-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/human_20mouse_20rat_20Activin_20A.png?v=1770191385"},{"product_id":"human-g-csf-protein-his-tag-animal-free-bhp13700210","title":"Human G-CSF Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGM-CSF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e CSF-3, MGI-1G, GM-CSF beta, pluripoietin; Human G-CSF Protein, His tag (Animal-Free)，G-CSF，CSF-3, MGI-1G, GM-CSF beta, pluripoietin.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman G-CSF Protein, His tag (Animal-Free), expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt;0.1 EU per 1 μg of the protein by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eGM-CSF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 19.48 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human G-CSF Protein consists of 174 amino acids and predicts a molecular mass of 19.48 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human G-CSF (Thr31-Pro204) (NP_757373) was expressed with 6×His tag at the N-terminus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 97% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to induce proliferation in NFS-60 cells.The ED₅₀ for this effect is \u0026lt;50 pg\/mL. The specific activity of recombinant human G-CSF is \u0026gt; 2 x 10⁷ IU\/mg.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH7.4. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997748949357,"sku":"PRP1093-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997748982125,"sku":"PRP1093-20UG","price":199.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997749014893,"sku":"PRP1093-100UG","price":669.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997749047661,"sku":"PRP1093-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/human_20G-CSF.png?v=1770191387"},{"product_id":"human-cxcl10-protein-his-tag-animal-free-bhp13700214","title":"Human CXCL10 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL10\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IP-10, Gamma-Interferon Inducible Protein 10, Crg-2; Human CXCL10 Protein, His tag (Animal-Free)，CXCL10，IP-10, Gamma-Interferon Inducible Protein 10, Crg-2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman CXCL10 Protein, His tag (Animal-Free), expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt;0.1 EU per 1 μg of the protein by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL10\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 9.45 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human CXCL10 Protein consists of 77 amino acids and predicts a molecular mass of 9.45 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human CXCL10 (Val22-Pro98) (P02778) was expressed with 6×His tag at the N-terminus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 97% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract human PBMCs using a concentration range of 10.0 - 100.0 ng\/mL. Note: Results may vary from different PBMC donors.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH7.4. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997749473645,"sku":"PRP1097-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997749506413,"sku":"PRP1097-20UG","price":199.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997749539181,"sku":"PRP1097-100UG","price":539.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997749571949,"sku":"PRP1097-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/human_20CXCL10.png?v=1770191388"},{"product_id":"human-mmp2-active-protein-his-tag-animal-free-bhp13700215","title":"Human MMP2 (active) Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMMP2\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Gelatinase A, TBE-1, MMP-II, MONA; Human MMP2 (active) Protein, His tag (Animal-Free)，MMP2 (active)，Gelatinase A, TBE-1, MMP-II, MONA.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman MMP2 (active) Protein, His tag (Animal-Free), expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt;0.1 EU per 1 μg of the protein by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMMP2\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 63.00 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human MMP2 Protein consists of 551 amino acids and predicts a molecular mass of 63 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human MMP2 (Tyr110-Cys660) (P08253) was expressed with 6×His tag at the C-terminus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH8.0. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997749604717,"sku":"PRP1098-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997749637485,"sku":"PRP1098-20UG","price":199.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997749670253,"sku":"PRP1098-100UG","price":539.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997749703021,"sku":"PRP1098-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/human_20MMP2_20_active.png?v=1770191388"},{"product_id":"human-lif-protein-his-tag-animal-free-bhp13700216","title":"Human LIF Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLIF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor (MLPLI), Interleukin 6 family cytokine; Human LIF Protein, His tag (Animal-Free)，LIF，Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor (MLPLI), Interleukin 6 family cytokine.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman LIF Protein, His tag (Animal-Free), expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt;0.1 EU per 1 μg of the protein by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLIF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 20.52 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human LIF Protein consists of 197 amino acids and predicts a molecular mass of 19.6 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human LIF (Ser24-Phe220) (P15018) was expressed with 6×His tag at the N-terminus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to induce TF-1 cells proliferation.The ED₅₀ for this effect is \u0026lt;0.2 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997749735789,"sku":"PRP1099-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997749768557,"sku":"PRP1099-20UG","price":199.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997749801325,"sku":"PRP1099-100UG","price":539.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997749834093,"sku":"PRP1099-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/human_20LIF.png?v=1770191389"},{"product_id":"mouse-m-csf-protein-his-tag-bhp13700218","title":"Mouse M-CSF protein,His tag","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eM-CSF\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Macrophage colony-stimulating factor 1; CSF-1; MCSF; Csf1; Csfm.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eGranulocyte-Macrophage Colony Stimulating Factor (GM-CSF) is secreted by a number of different cell types (including activated T cells,Bcells,macrophages,mast cells,endothelial cells and fibroblasts) in response to cytokine or immune and inflammatory stimulation.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eM-CSF\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 26 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse M-CSF consists of 230 amino acids and predicts a molecular mass of 26.1 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse M-CSF (Lys33-Glu262 ) (P07141-1) was expressed with 6×His tag.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95% as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measured by its ability to induce proliferation in M-NFS-60 cells. The ED50 for this effect is 0.1179 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from 20 mM Tris-HCl, 150mM NaCl, pH8.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997749997933,"sku":"PRP1101-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997750030701,"sku":"PRP1101-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997750063469,"sku":"PRP1101-100UG","price":419.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997750096237,"sku":"PRP1101-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1101.png?v=1770191217"},{"product_id":"human-cxcl4-protein-his-tag-animal-free-bhp13700219","title":"Human CXCL4 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL4\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Platelet Factor-4,PF-4, Oncostatin A, Ironplact; CXCL4，CXCL-4，CXCL 4，Platelet Factor-4,PF-4, Oncostatin A, Ironplact.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 4 (CXCL4) also named platelet factor 4 (PF4), which is a chemokine of the intercrine alpha family. CXCL4 is a 8kDa protein containing 70 amino acid residues. CXCL4 is produced by the activated platelets which plays an important role in immune responses. CXCL4 inhibit the cell proliferation, platelet aggregation and wound repair. CXCL4 also suppresses the hematopoiesis.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL4\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 8.58 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human CXCL4 consists of 70 amino acids and predicts a molecular mass of 8.58 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human CXCL4 (Glu32-Ser101) (P02776) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to inhibit human CXCL4-induce proliferation in HUVEC cells.The ED₅₀ for this effect is \u0026lt;5 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997750129005,"sku":"PRP1102-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997750161773,"sku":"PRP1102-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997750194541,"sku":"PRP1102-100UG","price":549.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997750227309,"sku":"PRP1102-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1102.png?v=1770191217"},{"product_id":"human-cxcl7-protein-his-tag-animal-free-bhp13700222","title":"Human CXCL7 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL7\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Neutrophil Activating Protein-2, NAP-2, PBP (parent molecule), CTAP-III (precursor); CXCL7，CXCL-7，CXCL 7，Neutrophil Activating Protein-2, NAP-2, PBP (parent molecule), CTAP-III (precursor).\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 7 (CXCL7) also named Pro-Platelet basic protein (PPBP), which is a chemokine of the intercrine alpha family. CXCL7is a 7.7 kDa protein containing 70 amino acid residues. CXCL7 is expressed by the platelets, which are activated. During vascular injury, CXCL7 controls the glucose metabolism, mitogenesis and neutrophil recruitment by the interaction with CXCR2.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL7\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 8.43 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human CXCL7 consists of 70 amino acids and predicts a molecular mass of 8.43 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human CXCL7 (Ala59-Asp128) (P02775) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with human CXCR7.The ED₅₀ for this effect is \u0026lt;0.5 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997750522221,"sku":"PRP1105-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997750554989,"sku":"PRP1105-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997750587757,"sku":"PRP1105-100UG","price":739.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997750620525,"sku":"PRP1105-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1105.png?v=1770191219"},{"product_id":"human-cxcl13-protein-his-tag-animal-free-bhp13700223","title":"Human CXCL13 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL13\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e B-cell Attracting Chemokine-1, BLR1 Ligand, BCA-1\/BLC; CXCL13，CXCL-13，CXCL 13，B-cell Attracting Chemokine-1, BLR1 Ligand, BCA-1\/BLC.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 13 (CXCL13) also named B lymphocyte chemoattractant (BLC), which is a chemokine of the intercrine alpha family. CXCL13 is a 7.9kDa protein containing 72 amino acid residues. CXCL13 is a chemotaxis for B lymphocyte. CXCL13 induces the cell proliferation though the AKT signal pathway which plays a key role intestinal cancer model. CXCL13 \/CXCR5 axis is highly existed in gut, spleen and lymph nodes.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL13\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 9.49 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human CXCL13 consists of 72 amino acids and predicts a molecular mass of 9.49 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human CXCL13 (Val23-Arg94) (O43927) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with human CXCR13.The ED₅₀ for this effect is \u0026lt;20 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997750653293,"sku":"PRP1106-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997750686061,"sku":"PRP1106-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997750718829,"sku":"PRP1106-100UG","price":479.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997750751597,"sku":"PRP1106-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1106.png?v=1770191220"},{"product_id":"mouse-cxcl3-protein-his-tag-animal-free-bhp13700232","title":"Mouse CXCL3 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL3\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e C-X-C motif chemokine 3, Dci, Dcip1, Gm1960; CXCL3，CXCL-3，CXCL 3，C-X-C motif chemokine 3, Dci, Dcip1, Gm1960.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 3 (CXCL3) also named Growth-regulated oncogene gamma (GROγ), which is a chemokine of the intercrine alpha family. CXCL3 is a 8 kDa protein containing 73 amino acid residues. During inflammation, CXCL3 is activated by the TNF and IL-1 which mediates the monocytes migration and adhesion by targeting the CXCR2. CXCL3 activates the JNK activity which induce the cell differentiation.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL3\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 8.72 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse CXCL3 consists of 73 amino acids and predicts a molecular mass of 8.72 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse CXCL3 (Ala28-Ser100) (Q6W5C0) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with mouse CXCR3. The ED₅₀ for this effect is \u0026lt;80 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997751865709,"sku":"PRP1117-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997751898477,"sku":"PRP1117-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997751931245,"sku":"PRP1117-100UG","price":549.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997751964013,"sku":"PRP1117-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1117.png?v=1770191224"},{"product_id":"mouse-cxcl9-protein-his-tag-animal-free-bhp13700233","title":"Mouse CXCL9 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL9\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e C-X-C motif chemokine 9, Monokine Induced by Interferon-γ, MIG; CXCL9，CXCL-9，CXCL 9，C-X-C motif chemokine 9, Monokine Induced by Interferon-γ, MIG.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 9 (CXCL9) also named monokine induced by gamma interferon (MIG), which is a chemokine of the intercrine alpha family. CXCL9 is a 11.7 kDa protein containing 10⁵ amino acid residues. CXCL9 controls the immune cells by binding the CXCR3 which is including the cell migration and activation. During inflammation, CXCL9 is a chemotaxis for lymphocyte and macrophages. CXCL9 is participated in the process of tumor proliferation and metastasis.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL9\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 13.00 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse CXCL9 consists of 105 amino acids and predicts a molecular mass of 13.0 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse CXCL9 (Thr22-Thr126) (AAA39706.1) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with mouse CXCR9. The ED₅₀ for this effect is \u0026lt;0.3 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997751996781,"sku":"PRP1120-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997752029549,"sku":"PRP1120-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997752062317,"sku":"PRP1120-100UG","price":409.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997752095085,"sku":"PRP1120-1MG","price":0.0,"currency_code":"USD","in_stock":true}]},{"product_id":"mouse-cxcl16-protein-his-tag-animal-free-bhp13700234","title":"Mouse CXCL16 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCXCL16\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e C-X-C motif chemokine 16, SRPSOX; CXCL16，CXCL-16，CXCL 16，.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eC-X-C motif chemokine 16 (CXCL16) is a chemokine of the intercrine alpha family which is a 9.8 kDa protein containing 88 amino acid residues. In mediate the innate immunity, CXCL16 is a chemotaxis for T cells and NKT cells, which expressed the CXC chemokine receptor (CXCR) 6. CXCL16 also can be enhanced the expression level by the TNFα, IL-1 and IFNγ. CXCL16 protects the host by against the gram positive and gram negitive bactreials.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eCXCL16\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 10.74 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse CXCL16 consists of 88 amino acids and predicts a molecular mass of 10.74 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse CXCL16 (Asn 27-Pro 114) (Q8BSU2) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to chemoattract BaF3 cells transfected with mouse CXCR16 The ED₅₀ for this effect is \u0026lt;3 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997752127853,"sku":"PRP1121-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997752160621,"sku":"PRP1121-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997752193389,"sku":"PRP1121-100UG","price":479.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997752226157,"sku":"PRP1121-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1121.png?v=1770191226"},{"product_id":"human-rspo1-r-spondin-1-protein-his-sumo-tag-animal-free-bhp13700235","title":"Human RSPO1\/R-spondin 1 Protein, His-SUMO tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eRSPO1\/R-spondin 1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e RSPO1, Roof plate-specific spondin-1; RSPO1, Roof plate-specific spondin-1，R-spondin 1.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eR-spondin 1 (RSPO1, Roof plate-specific Spondin 1) is a cysteine-rich secreted glycoprotein that belongs to the R-Spondin family. Structurally, R-spondin 1 harbors an N-terminal signal peptide, two cysteine-rich furin-like (FU1-FU2) domains, a thrombospondin (TSP) domain, and a basic amino acid-rich (BR) C-terminal domain. R-spondin 1 acts as a ligand for the leucine-rich repeat-containing G-protein coupled receptor (LGR) family (LGR4\/5\/6), subsequent clearing negative regulators ZNRF3\/RNF43 from the membrane, leading to the availability of Wnt receptor and activating Wnt\/β-catenin signaling. The signal cascade is essential for regulating stem cell proliferation, embryonic development, and tissue homeostasis.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eRSPO1\/R-spondin 1\u003c\/strong\u003e is connected to ubiquitin\/SUMO-dependent regulation of protein stability, localization, and signaling duration. These modification pathways act as reversible molecular switches that help tune pathway outputs during stress, cell-cycle control, and quality-control processes. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 46.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human RSPO1\/R-spondin 1 consists of 243 amino acids and predicts a molecular mass of 46.8 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human RSPO1\/R-spondin 1 (Ser21-Ala263) (Q2MKA7) was expressed with His-SUMO tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e R-Spondin-1 enhances BMP-2-mediated differentiation of MC3T3-E1 cells. The ED₅₀ for this effect is 1-3 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Mammalian expression can support native-like folding, disulfide bond formation, and glycosylation—features that are often important for secreted proteins, receptors, and adhesion molecules. For ubiquitin\/SUMO pathway enzymes, catalytic activity often depends on correct folding and active-site integrity rather than glycosylation.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e HEK 293. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His-SUMO tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Ubiquitin\/SUMO pathway measurements can reflect changes in protein turnover, signaling dwell time, and stress-adaptation programs. Mechanistic interpretation is often strengthened by pairing modification-state readouts with measurements of substrate abundance, localization, and interaction partners.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997752258925,"sku":"PRP1122-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997752291693,"sku":"PRP1122-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997752324461,"sku":"PRP1122-100UG","price":549.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997752357229,"sku":"PRP1122-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1122.png?v=1770191225"},{"product_id":"mouse-il-1-protein-bhp13700239","title":"Mouse IL-1à protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-1A\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e IL-1A; IL-1A,IL-1α.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IL-1α protein expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.01 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-1A\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 18 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse IL-1α consists of 161 amino acids and has a predicted molecular mass of 18 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse IL-1α (NP_034684.2) (Ser 115-Ser 270) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Immobilized Mouse IL-1α at 1 μg\/mL (100 μl\/well) can bind mouse IL1R1, The EC50 of mouse IL1R1 is 0.65 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM Tris，0.15M NaCl, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997752783213,"sku":"PRP1127-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997752815981,"sku":"PRP1127-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997752848749,"sku":"PRP1127-100UG","price":499.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997752881517,"sku":"PRP1127-1MG","price":1209.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1127.jpg?v=1770191227"},{"product_id":"human-il-17d-protein-his-tag-animal-free-bhp13700242","title":"Human IL-17D Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-17D\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e interleukin 17D, UNQ3096\/PRO2117, IL17, IL17D; IL-17D，IL17D，IL 17D，interleukin 17D, UNQ3096\/PRO2117, IL17.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eInterleukin 17D (IL-17D) is a 20.2 kDa member of IL-17 family with 185 amino acid residues. IL-17D is expressed by skeletal muscle, brain, adipose tissue, heart, lung, pancreas and secreted to blood. IL-17D can stimulate the production of cytokines such as IL-6, IL-8, GM-CSF, and stimulate local infiltration and proliferation of leukocytes.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-17D\u003c\/strong\u003e mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 21.00 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-17D consists of 185 amino acids and predicts a molecular mass of 21.0 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IL-17D (Ala18-Pro202) (Q8TAD2) was expressed with 6×His tag at the N-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS，pH 8.0.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997753110893,"sku":"PRP1130-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997753143661,"sku":"PRP1130-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997753176429,"sku":"PRP1130-100UG","price":739.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997753209197,"sku":"PRP1130-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1130.png?v=1770191229"},{"product_id":"mouse-sonic-hedgehog-protein-bhp13700244","title":"Mouse Sonic Hedgehog Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSONIC\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e HHG1 Protein; HLP3 Protein; HPE3 Protein; MCOPCB5 Protein; SMMCI Protein; Sonic hedgehog Protein; TPT Protein; TPTPS Protein.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse Sonic Hedgehog Protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin : \u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSONIC\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 19.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse SHH consists of 174 amino acids and has a predicted molecular mass of 19.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse SHH (Q62226) (Cys25-Gly198) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 96 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"10 ug","offer_id":52997753373037,"sku":"PRP1132-10UG","price":99.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997753405805,"sku":"PRP1132-50UG","price":289.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997753438573,"sku":"PRP1132-1MG","price":4699.0,"currency_code":"USD","in_stock":true}]},{"product_id":"mouse-trail-protein-his-tag-animal-free-bhp13700279","title":"Mouse TRAIL Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRAIL\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e TNFSF10, Apo2 Ligand, TL2, Apo2L, CD253; Mouse TRAIL Protein, His tag (Animal-Free)，TNF-α，TNFSF2, Cachectin, Differentiation-inducing factor (DIF), Necrosin, Cytotoxin, TNSF1A.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse TRAIL Protein, His tag (Animal-Free), expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt;0.1 EU per 1 μg of the protein by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTRAIL\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 21.00 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse TRAIL Protein consists of 174 amino acids and predicts a molecular mass of 21.0 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse TRAIL (Met118-Asn291) (P50592) was expressed with 6×His tag and a Met at the C-terminus\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98% as determined by SDS-PAGE.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to induce cytotoxicity in L929 cells in the presence of actinomycin D.The ED₅₀ for this effect is \u0026lt;1 ng\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e The protein was lyophilized from sterile PBS, pH 7.4. If you have any concerns or special requirements, please confirm with us.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997757960557,"sku":"PRP1168-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997757993325,"sku":"PRP1168-20UG","price":199.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997758026093,"sku":"PRP1168-100UG","price":589.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997758058861,"sku":"PRP1168-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/mouse_20TRAIL.png?v=1770191396"},{"product_id":"human-bmp-5-protein-his-tag-animal-free-bhp13700309","title":"Human BMP-5 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBMP-5\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e bone morphogenetic protein 5, BMP5; BMP-5，BMP 5，BMP5，bone morphogenetic protein 5.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eBone Morphogenetic Protein-5 (BMP-5) is an extracellular multifunctional signaling cytokine that is also a member of the TGF-β family. BMP-5 can bind with TGF-β receptors and trigger SMAD protein signal transduction. It is involved in many negatively regulated physiological processes, such as the aldosterone biosynthetic process and epithelial to mesenchymal transition. BMP-5 also plays a vital role in cartilage synthesis.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBMP-5\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMetabolism \u0026amp; Enzymology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 16.57 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human BMP-5 consists of 138 amino acids and predicts a molecular mass of 16.57 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human BMP-5 (Ala317-His454) (P22003) was expressed with 6×His tag at the C-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 98 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to induce alkaline phosphatase production by ATDC5 cells. The ED₅₀ for this effect is \u0026lt;0.17 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM sodium citrate,0.2 M NaCl, pH 3.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997761991021,"sku":"PRP1198-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997762023789,"sku":"PRP1198-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997762056557,"sku":"PRP1198-100UG","price":739.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997762089325,"sku":"PRP1198-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1198.png?v=1770191258"},{"product_id":"human-bmp-7-protein-his-tag-animal-free-bhp13700310","title":"Human BMP-7 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eOP-1\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e bone morphogenetic protein 7, Osteogenic Protein-1 (OP-1), BMP7; BMP7，BMP 7，BMP-7，bone morphogenetic protein 7, Osteogenic Protein-1 (OP-1).\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eBone Morphogenetic Protein-7 (BMP-7) is an extracellular multifunctional cytokine that is also a member of the TGF-β family. BMP7 can significantly inhibit TGF-β through binding with TGF-β receptor and trigger SMAD transcription factors, such as SMAD 1 \/5\/8. It plays a vital role in inhibiting the expansion of kidney damage and promoting the differentiation of osteoblasts.\u003c\/p\u003e\u003cp\u003eEndotoxin :\u0026lt; 0.1 EU per 1 μg of the protein as determined by the LAL method.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eOP-1\u003c\/strong\u003e is used in RUO research to interrogate molecular mechanisms, interaction networks, and pathway-linked phenotypes in experimental systems. This target is frequently investigated in research themes such as \u003cstrong\u003eMetabolism \u0026amp; Enzymology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Human\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 14.00 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human BMP-7 consists of 117 amino acids and predicts a molecular mass of 14.00 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human BMP-7 (Met 315-His 431) (P18075) was expressed with 6×His tag at the C-terminus.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 95 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measure by its ability to induce alkaline phosphatase production by ATDC5 cells. The ED₅₀ for this effect is \u0026lt;0.65 μg\/mL.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e His tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20mM sodium citrate,0.2 M NaCl, pH 3.5.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997762122093,"sku":"PRP1199-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997762154861,"sku":"PRP1199-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997762187629,"sku":"PRP1199-100UG","price":809.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997762220397,"sku":"PRP1199-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1199.png?v=1770191258"}],"url":"https:\/\/www.ebiohippo.com\/collections\/rt-cell-biology-proteins-peptides.oembed?page=692","provider":"BioHippo","version":"1.0","type":"link"}