{"title":"Abbkine Proteins","description":"","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-il-6-protein-bhp13700012","title":"Human IL-6 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-6\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 BSF2; HGF; HSF; IFNB2; IL-6; Interleukin-6.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-6 protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 0.1 EU per μg of the protein by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-6\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\u003eImmunology \u0026amp; Inflammation\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 20.6 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human IL-6 consists of 187 amino acids and migrates with an apparent molecular mass of 20.6 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 mature form of human IL-6 (NP_000591.1)(Val 30-Met 212) 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\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measured in a cell proliferation assay using TF -1. The ED50 for this effect is typically 2.25 ng\/mL. The specific activity of recombinant Human IL6 is approximately \u0026gt;4.44 x 105 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. 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 7.4.. 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":52997734531437,"sku":"PRP1012-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997734564205,"sku":"PRP1012-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997734596973,"sku":"PRP1012-100UG","price":379.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997734629741,"sku":"PRP1012-1MG","price":999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1012_28b7da5f-f33e-4d18-b561-a869d772fc9a.png?v=1770191155"},{"product_id":"human-tnf-protein-bhp13700013","title":"Human TNF-α Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTNF-Α\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 DIF; TNF-α; TNFA; TNFSF2; Tumor necrosis factor; TNF.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman TNF-α protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eTumor necrosis factor α (TNF-α), also known as TNF, TNFA or TNFSF2, is the prototypic cytokine of the TNF superfamily, and is a multifunctional molecule involved in the regulation of a wide spectrum of biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. Two receptors, TNF-R1 (TNF receptor type 1; CD120a; p55\/60) and TNF-R2 (TNF receptor type 2; CD120b; p75\/80), bind to TNF-α. TNF-α protein is produced mainly by macrophages, and large amounts of this cytokine are released in response to lipopolysaccharide, other bacterial products, and Interleukin-1 (IL-1).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eTNF-Α\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\u003eImmunology \u0026amp; Inflammation\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 17.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human TNF-α consists of 158 amino acids and has a predicted molecular mass of 17.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human TNF-α soluble form (NP_000585.2) (Val 77-Leu 233) 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 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":52997734662509,"sku":"PRP1013-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997734695277,"sku":"PRP1013-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997734728045,"sku":"PRP1013-100UG","price":219.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997734760813,"sku":"PRP1013-1MG","price":999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1013.png?v=1770191155"},{"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-ifn-protein-bhp13700016","title":"Human IFN-? Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFN-Γ\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 IFG; IFI; IFN gamma; Interferon Gamma; Interferon gamma; IFNG.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IFN-γ protein, His Tag, expressed in E. coli\u003c\/p\u003e\u003cp\u003eIFN-γ, also known as IFNG, is a secreted protein which belongs to the type I I interferon family. IFN-γ is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN-γ has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN-γ is critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. Aberrant IFN-γ expression is associated with a number of autoinflammatory and autoimmune diseases. The importance of IFN-γ in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIFN-Γ\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\u003eImmunology \u0026amp; Inflammation\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 16.91 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IFN-γ protein consists of 144 amino acids and predicts a molecular mass of 16.91 KDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IFN-γ soluble form (NP_01579.1) (Gln24-Gln166) 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\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 7.0.. 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":"20 ug","offer_id":52997735055725,"sku":"PRP1014-20UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735088493,"sku":"PRP1014-100UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997735121261,"sku":"PRP1014-500UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735154029,"sku":"PRP1014-1MG","price":999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1014.png?v=1770191157"},{"product_id":"mouse-ifn-protein-his-tag-bhp13700017","title":"Mouse IFN-? Protein, His Tag","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFN-Γ\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 IFG; IFI; IFN gamma; Interferon Gamma; Interferon gamma; IFNG.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IFN-γ protein, His Tag, expressed in E. coli\u003c\/p\u003e\u003cp\u003eIFN-γ, also known as IFNG, is a secreted protein which belongs to the type I I interferon family. IFN-γ is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN-γ has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN-γ is critical for innate and adaptive immunity against viral and intracellular bacterial infections and for tumor control. Aberrant IFN-γ expression is associated with a number of autoinflammatory and autoimmune diseases. The importance of IFN-γ in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIFN-Γ\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\u003eImmunology \u0026amp; Inflammation\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 16.9 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse IFN-γ protein consists of 154 amino acids and predicts a molecular mass of 16.9 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse IFN-γ protein soluble form (NP_P01580) (His23-Cys155) was expressed, was expressed with a polyhistidine 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\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 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 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":"20 ug","offer_id":52997735186797,"sku":"PRP1015-20UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735219565,"sku":"PRP1015-100UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997735252333,"sku":"PRP1015-500UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735285101,"sku":"PRP1015-1MG","price":999.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1015.png?v=1770191158"},{"product_id":"human-gm-csf-protein-bhp13700018","title":"Human GM-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 GM-CSF; GMCSF; Granulocyte-macrophage colony-stimulating factor; CSF2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman GM-CSF 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\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\u003eImmunology \u0026amp; Inflammation\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 GM-CSF consists of 128 amino acids and has a predicted molecular mass of 14 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human GM-CSF isoform (P04141-1) (Ala18-Glu144) 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 in a cell proliferation assay using TF-1 human erythroleukemia cells. The ED50 for this effect is 0.05-0.5 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.\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":52997735317869,"sku":"PRP1016-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997735350637,"sku":"PRP1016-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735383405,"sku":"PRP1016-100UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735416173,"sku":"PRP1016-1MG","price":3769.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1016.png?v=1770191157"},{"product_id":"human-il-33-protein-bhp13700019","title":"Human IL-33 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-33\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 C9orf26; DVS27; IL1F11; NF-HEV; NFEHEV; Interleukin-33; IL33.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-33 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-33\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\u003eImmunology \u0026amp; Inflammation\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 18.1 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human IL-33 consists of 160 amino acids (N-Met) and has a predicted molecular mass of 18.1 kDa. The apparent molecular mass of the human IL-33 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-33 isoform (O95760) (Ser112-Thr270) 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 5.0,1 mM DTT and 1 mM EDTA.. 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":52997735448941,"sku":"PRP1018-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997735481709,"sku":"PRP1018-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735514477,"sku":"PRP1018-100UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735547245,"sku":"PRP1018-1MG","price":3769.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1018.png?v=1770191158"},{"product_id":"mouse-il-33-protein-bhp13700020","title":"Mouse IL-33 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-33\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 C9orf26; DVS27; IL1F11; NF-HEV; NFEHEV; Interleukin-33; IL33.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IL-33 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-33\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\u003eImmunology \u0026amp; Inflammation\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 17.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Mouse IL-33 consists of 159 amino acids (N-Met) and has a predicted molecular mass of 17.7 kDa. The apparent molecular mass of the Mouse IL-33 is approximately 17 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 Mouse IL-33 isoform (Q8BVZ5)(Ser109-Ile266) 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":52997735580013,"sku":"PRP1118-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997735612781,"sku":"PRP1118-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997735645549,"sku":"PRP1118-100UG","price":469.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997735678317,"sku":"PRP1118-1MG","price":1809.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1118.png?v=1770191158"},{"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":"human-gm-csf-protein-his-tag-animal-free-bhp13700025","title":"Human GM-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 GM-CSF; GMCSF; Granulocyte-macrophage colony-stimulating factor; CSF2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman GM-CSF protein (Animal-Free), expressed in HEK293 Cells\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\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\u003eImmunology \u0026amp; Inflammation\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 14.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human GM-CSF consists of 127 amino acids and predicts a molecular mass of 14.5 kDa. It migrates as an approximately 23.8 kDa band 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 GM-CSF (NP_000749.2) (Met1-Glu144) was expressed with a 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 Measured in a cell proliferation assay using TF-1 cells. The ED50 for this effect is 0.3187 ng\/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.\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":"5 ug","offer_id":52997736235373,"sku":"PRP2016-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997736268141,"sku":"PRP2016-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997736300909,"sku":"PRP2016-100UG","price":569.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2016.png?v=1770191161"},{"product_id":"mouse-il-4-protein-his-tag-animal-free-bhp13700026","title":"Mouse IL-4 protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-4\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-4; Interleukin 4; BCGF1; BSF1.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IL-4 protein (Animal-Free), expressed in HEK293 Cells\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-4\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\u003eImmunology \u0026amp; Inflammation\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 15-19 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant mouse IL-4 consists of 118 amino acids and predicts a molecular mass of 13.3 kD. The apparent molecular mass of the mouse IL-4 is approximately 15-19 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 IL-4 (P07750) (Met 1-Ser140) was expressed with a 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\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 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 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 0.22 µm filtered protein solution is in 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 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":52997736333677,"sku":"PRP2117-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997736366445,"sku":"PRP2117-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997736399213,"sku":"PRP2117-100UG","price":569.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2117.png?v=1770191161"},{"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":"mouse-il-6-protein-his-tag-animal-free-bhp13700036","title":"Mouse IL-6 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-6\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-6; IL-6; B-Cell Hybridoma Growth Factor; Interleukin HP-1; Il6; Il-6.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IL-6 protein, His tag (Animal-Free), expressed in HEK293 Cells\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-6\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\u003eImmunology \u0026amp; Inflammation\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 21.9 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant mouse IL-6 consists of 193 amino acids and predicts a molecular mass of 21.9 KD. The apparent molecular mass of the mouse IL-6 is approximately 25 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 mouse IL-6 (P08505) (Met 1-Thr211) was expressed with a 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 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. 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 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 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":52997737087341,"sku":"PRP2112-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997737120109,"sku":"PRP2112-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997737152877,"sku":"PRP2112-100UG","price":379.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2112.png?v=1770191164"},{"product_id":"human-il-13-protein-bhp13700051","title":"Human IL-13 protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-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 ALRH; IL-13; P600; Interleukin-13; IL13.\u003c\/p\u003e\u003cp\u003eHuman IL-13 protein, expressed in CHO Stable Cells\u003c\/p\u003e\u003cp\u003eInterleukin 13 (IL-13) is a single-chain glycosylated polypeptide, which belongs to the IL-13\/IL-4 family. IL-13 protein is secreted by many cell types, but especially by T helper type 2 (Th2) cells. IL-13 exerts its effects through a multi-subunit receptor comprising the α chain of the IL-4 receptor (IL-4Rα) and at least one of two known IL-13-specific binding chains (IL-13 Rα1 and IL-13 Rα2). As a cytokine, IL-13 protein is critical in regulating inflammatory, immune responses and diseases. In addition, it inhibits the production of pro-inflammatory cytokines and chemokines, and thus down-regulates macrophage activity. IL-13 protein and antibody is more importantly implicated as a central mediator of immunoregulatory processes in various cell types.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-13\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\u003eImmunology \u0026amp; Inflammation\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 12.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human IL-13 consists of 112 amino acids and migrates as an approximately 12.5 kDa band in SDS-PAGE under reducing conditions as predicted.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from human IL-13 (AAK53823.1) (Met 1-Asn 132) was expressed and purified.\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 in a cell proliferation assay using TF1 human erythroleukemic cells (Kitamura, T. et al. 1989, J. Cell Physiol. 140:323.). The ED50 for this effect is typically 0.5-3 ng\/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 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 CHO Stable 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 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 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":52997737185645,"sku":"PRP100108-5UG","price":189.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP100108-1.jpg?v=1770191166"},{"product_id":"mouse-tgf-1-protein-bhp13700101","title":"Mouse TGF-?1 protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTGF-Β1\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 Transforming growth factor beta-1; TGFB1.\u003c\/p\u003e\u003cp\u003eMouse TGF-β1 protein, expressed in HEK293 Cells\u003c\/p\u003e\u003cp\u003eTGF-β1 is a member of the transforming growth factor β (TGF-β) family. The transforming growth factor-β family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-β1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-α and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-β1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-β1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-β1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-β1 also has the opposite effect on cells of myeloid origin. TGF-β1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-β1-mediated growth inhibition, autocrine TGF-β signaling can promote tumorigenesis. Elevated levels of TGF-β1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eTGF-Β1\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\u003eOncology \u0026amp; Angiogenesis\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 12.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant rat TGF-β1 comprises 112 amino acids and predicts a molecular mass of 12.8 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from rat TGF-β1 (Ala279-Ser390) was expressed. Rat and Mouse mature TGFB1 sequences are identical.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 90 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Measured by its ability to inhibit cell proliferation of Mv-1-lu mink lung epithelial cells. The ED50 for this effect is 0.2-0.8 ng\/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 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 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 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 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":52997737349485,"sku":"PRP110618-5UG","price":169.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997737382253,"sku":"PRP110618-100UG","price":1179.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997737415021,"sku":"PRP110618-1MG","price":6249.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP110618-1.jpg?v=1770191167"},{"product_id":"human-fgf1-fgf-acidic-protein-bhp13700104","title":"Human FGF1\/FGF acidic Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFGF1\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 1; FGF-1; Acidic Fibroblast Growth Factor; aFGF; Heparin-Binding Growth Factor 1; HBGF-1; Fgf1; Fgf-1; Fgfa.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman FGF1\/FGF acidic 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\u003eFGF1\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\u003eOncology \u0026amp; Angiogenesis\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 15.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human FGF1\/FGF acidic protein consists of 140 amino acids and has a predicted molecular mass of 15.5 KD.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human FGF1 (P05230) (Phe16-Asp155) 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 Balb\/3T3 cells. The ED50 for this effect is 23.73 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 20mM tris, 50mM 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":52997737447789,"sku":"PRP1001-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997737480557,"sku":"PRP1001-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997737513325,"sku":"PRP1001-100UG","price":219.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1001.png?v=1770191168"},{"product_id":"mouse-tgf-1-protein-his-tag-animal-free-bhp13700105","title":"Mouse TGF-?1 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTGF-Β1\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 TGF-beta-1; CED; DPD1; TGFB; TGF-b1; TGFB1; CEDLAP; latency-associated peptide; TGFbeta; TGF-beta 1 protein; transforming growth factor beta-1; TGF-β1; TGF beta1; TGFbeta 1; TGF-beta 1.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse TGF-β1 protein, His tag (Animal-Free), expressed in HEK293 Cells\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\u003eTGF-Β1\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\u003eOncology \u0026amp; Angiogenesis\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 42.7 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human Mouse TGF-β1 protein consists of 91 amino acids and predicts a molecular mass of 42.7 KD. It migrates as an approximately 54, 41 and 15 KD band 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 TGFβ-1 (P04202) (Met1-Ser390) was expressed with a 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 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 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 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 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":52997737546093,"sku":"PRP1017-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997737578861,"sku":"PRP1017-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997737611629,"sku":"PRP1017-100UG","price":229.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997737644397,"sku":"PRP1017-1MG","price":1879.0,"currency_code":"USD","in_stock":true}]},{"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":"rat-tnf-protein-bhp13700113","title":"Rat TNF-α Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTNF-Α\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 TNF; TNFA; TNFSF2; DIF; Tumor Necrosis Factor; Tumor Necrosis Factor Ligand Superfamily Member; Tumor Necrosis Factor (TNF Superfamily, Member 2); Tumor Necrosis Factor Ligand 1F; Tumor Necrosis Factor-Alpha; TNF Superfamily, Member 2; TNLG1F 3; TNF 5.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Rat.\u003c\/p\u003e\u003cp\u003eRat TNF-α 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\u003eTNF-Α\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\u003eImmunology \u0026amp; Inflammation\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 17.2 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Rat TNF-α consists of 156 amino acids and has a predicted molecular mass of 17.2 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Rat TNF-α (P16599)(Leu80-Leu235) 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\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 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":52997738070381,"sku":"PRP1213-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997738103149,"sku":"PRP1213-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738135917,"sku":"PRP1213-100UG","price":379.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997738168685,"sku":"PRP1213-1MG","price":1879.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1213.jpg?v=1770191170"},{"product_id":"human-il-3-protein-his-tag-animal-free-bhp13700124","title":"Human IL-3 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-3\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 Hematopoietic growth factor; IL3; IL-3; IL-3MGC79398; interleukin 3 (colony-stimulating factor, multiple); interleukin-3; Mast cell growth factor; mast-cell growth factor; MCGF; MCGFMGC79399; MULTI-CSF; multilineage-colony-stimulating factor; Multipotential colony-stimulating factor; P-cell stimulating factor; P-cell-stimulating factor.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-3 protein, His tag (Animal-Free), expressed in HEK 293 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\u003eFunctionally, \u003cstrong\u003eIL-3\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\u003eImmunology \u0026amp; Inflammation\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 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human IL-3 protein consists of 140 amino acids and predicts a molecular mass of 16 kD.The apparent molecular mass of the human IL-3 is approximately 17-35 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-3 protein (NP_000579.2, Met1-Phe152) was expressed with a polyhistidine 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 Measured in a cell proliferation assay using TF-1 cells. The ED50 for this effect is 6.87ng\/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 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 HEK 293 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 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":52997738201453,"sku":"PRP2015-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997738234221,"sku":"PRP2015-20UG","price":139.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738266989,"sku":"PRP2015-100UG","price":469.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997738299757,"sku":"PRP2015-1MG","price":3769.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2015.jpg?v=1770191171"},{"product_id":"mouse-il-13-protein-his-tag-animal-free-bhp13700125","title":"Mouse IL-13 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-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 ALRHMGC116789; BHR1interleukin-13; IL13; IL-13; IL-13MGC116788; interleukin 13; MGC116786; NC30; P600.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse IL-13 protein, His tag (Animal-Free), expressed in HEK 293 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\u003eFunctionally, \u003cstrong\u003eIL-13\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\u003eImmunology \u0026amp; Inflammation\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 12.7kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant mouse IL-13 protein consists of 118 amino acids and predicts a molecular mass of 12.7 kD.The apparent molecular mass of the mouse IL-13 is approximately 15-30 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 mouse IL-13 protein (P20109, Met1-Phe131) was expressed with a polyhistidine 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 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 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 HEK 293 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 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":52997738332525,"sku":"PRP2114-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997738365293,"sku":"PRP2114-20UG","price":139.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738398061,"sku":"PRP2114-100UG","price":569.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997738430829,"sku":"PRP2114-1MG","price":3769.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2114.jpg?v=1770191171"},{"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":"recombinant-sars-cov-2-spike-rbd-protein-his-tag-animal-free-bhp13700127","title":"Recombinant SARS-CoV-2 Spike RBD Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSARS-CoV-2 Spike RBD Protein\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 SARS-CoV-2-Spike-RBD，RBD，SARS-CoV-2 Spike RBD，SARS-CoV-2 SP RBD，2019-nCoV SARS-CoV-2 Spike Protein (RBD).\u003c\/p\u003e\u003cp\u003eRecombinant SARS-CoV-2 Spike RBD Protein, His tag (Animal-Free), expressed in HEK 293 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\u003eSARS-CoV-2 Spike RBD Protein\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\u003eInfectious Disease\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 26.5kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant SARS-CoV-2 (COVID-19) Spike RBD protein consists of 229 amino acids and predicts a molecular mass of 26.5 kD.The apparent molecular mass of the human CD33 is approximately 32-35 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 SARS-CoV-2 (COVID-19) Spike RBD protein (YP_009724390.1, Arg319-Phe541) was expressed with a polyhistidine 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 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 HEK 293 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":"5 ug","offer_id":52997738594669,"sku":"PRP2039-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997738627437,"sku":"PRP2039-20UG","price":139.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997738660205,"sku":"PRP2039-100UG","price":499.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997738692973,"sku":"PRP2039-1MG","price":3819.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2039.jpg?v=1770191172"},{"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-il-8-protein-bhp13700130","title":"Human IL-8 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-8\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 IL8; IL 8; IL-8; NAF; GCP1; LECT; LUCT; NAP1; GCP-1; LYNAP; MDNCF; MONAP; NAP-1; CXCL8.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-8 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-8\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\u003eImmunology \u0026amp; Inflammation\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 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-8 consists of 72 amino acids (N-Met) and has a predicted molecular mass of 8 kDa. The apparent molecular mass of the Human IL-8 protein is approximately 8 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 IL-8 isoform (P10145)(Ser28-Ser99) 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 human IL-8 at 200 ng\/mL (100μL\/well) can bind mouse anti-IL-8 antibody, the EC50 of mouse anti-IL-8 antibody is 66.4 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 20 mM Tris, 200 mM 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 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":52997738987885,"sku":"PRP1022-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997739020653,"sku":"PRP1022-50UG","price":249.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997739053421,"sku":"PRP1022-100UG","price":449.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739086189,"sku":"PRP1022-1MG","price":2609.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1022.png?v=1770191174"},{"product_id":"human-il-18-protein-bhp13700131","title":"Human IL-18 Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-18\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-18; IL18; IL 18; IFN gamma inducing factor; Interleukin 18; Interleukin-18; Interleukin 18 (interferon-gamma-inducing factor).\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-18 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-18\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\u003eImmunology \u0026amp; Inflammation\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-18 consists of 158 amino acids (N-Met) and has a predicted molecular mass of 18 kDa. The apparent molecular mass of the Human IL-18 protein is approximately 18 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 IL-18 isoform (Q14116)(Tyr37-Asp193) 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 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 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":52997739118957,"sku":"PRP1023-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997739151725,"sku":"PRP1023-50UG","price":249.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997739184493,"sku":"PRP1023-100UG","price":469.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739217261,"sku":"PRP1023-1MG","price":2609.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1023.png?v=1770191174"},{"product_id":"rat-ifn-protein-bhp13700132","title":"Rat IFN-? Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIFN-Γ\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 IFG; IFI; IFN gamma; IFN Immune; IFNG; Interferon gamma; Interferon Gamma Precursor; Macrophage Activating Factor; MAF; T Cell Interferon; Type II Interferon.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Rat.\u003c\/p\u003e\u003cp\u003eRat IFN-γ 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\u003eIFN-Γ\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\u003eImmunology \u0026amp; Inflammation\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 14.8 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Rat IFN-γ consists of 134 amino acids and has a predicted molecular mass of 14.8 kDa. The apparent molecular mass of the Rat IFN-γ protein is approximately 14.8 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 Rat IFN-γ isoform (P01581)(Glu23-Cys156) 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 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 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 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":"20 ug","offer_id":52997739250029,"sku":"PRP1214-20UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997739282797,"sku":"PRP1214-100UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997739315565,"sku":"PRP1214-500UG","price":589.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739348333,"sku":"PRP1214-1MG","price":889.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1214.png?v=1770191175"},{"product_id":"human-tgf-protein-bhp13700133","title":"Human TGF-α Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTGF-α\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 ETGF; TGF-alpha; TGF type 1; TGFA; TGF-α,TGF α.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman TGF-α 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\u003eTGF-α\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\u003eOncology \u0026amp; Angiogenesis\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 5.5 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant human TGF-α consists of 50 amino acids and has a predicted molecular mass of 5.5 kDa. The apparent molecular mass of the human TGF-α protein is approximately 5.5 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 TGF-α isoform (P01135)(Val40-Ala89) 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 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":"20 ug","offer_id":52997739381101,"sku":"PRP1024-20UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997739413869,"sku":"PRP1024-100UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997739446637,"sku":"PRP1024-500UG","price":589.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739479405,"sku":"PRP1024-1MG","price":889.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1024.png?v=1770191175"},{"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-il-4-protein-bhp13700135","title":"Human IL-4 protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eIL-4\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 IL4; IL-4; IL-4B_cell stimulatory factor 1; B cell growth factor 1; BCGF1; BCGF-1; interleukin 4; binetrakin; BCDF; B-cell stimulatory factor 1; BSF1; BSF-1; IL4E12; interleukin-4; Lymphocyte stimulatory factor 1; MGC79402; pitrakinra; MGC79403.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman IL-4 protein, expressed in HEK293 Cells\u003c\/p\u003e\u003cp\u003eEndotoxin: \u0026lt; 1 EUperµgofthe protein as determined by the LALmethod\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eIL-4\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\u003eImmunology \u0026amp; Inflammation\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 15.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-4 protein consists of 153 amino acids and has a predicted molecular mass of 15.4 kDa. The apparent molecular mass of the Human IL-4 protein is approximately 18 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 IL-4 protein isoform (P05112，Met 1-Ser153) 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. 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 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 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":52997739643245,"sku":"PRP2017-10UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997739676013,"sku":"PRP2017-50UG","price":249.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997739708781,"sku":"PRP2017-100UG","price":429.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739741549,"sku":"PRP2017-1MG","price":3739.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP2017.jpg?v=1770191176"},{"product_id":"human-fgf-21-protein-bhp13700137","title":"Human FGF 21 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 21; FGF-21; FGF21.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eHuman FGF21 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\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\u003eOncology \u0026amp; Angiogenesis\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 19.4 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human FGF21 consists of 181 amino acids and has a predicted molecular mass of 19.4 kDa. The apparent molecular mass of the Human FGF21 protein is approximately 19.4 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 FGF21 isoform(Q9NSA1)(His29-Ser209) 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 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 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":52997739774317,"sku":"PRP1030-5UG","price":89.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997739807085,"sku":"PRP1030-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"500 ug","offer_id":52997739839853,"sku":"PRP1030-500UG","price":909.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997739872621,"sku":"PRP1030-1MG","price":1369.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1030.png?v=1770191177"},{"product_id":"terminal-deoxynucleotidyl-transferase-tdt-bhp13700139","title":"Terminal Deoxynucleotidyl Transferase (TdT)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTDT\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 DNA nucleotidylexotransferase; Terminal addition enzyme; Terminal deoxynucleotidyltransferase; Terminal transferase; TdT.\u003c\/p\u003e\u003cp\u003eTerminal Deoxynucleotidyl Transferase (TdT), expressed in Null\u003c\/p\u003e\u003cp\u003eTerminal deoxynucleotidyl transferase (TdT), also known as terminal transferase, is a specialized DNA polymerase expressed in immature, pre-B, pre-T lymphoid cells, and acute lymphoblastic leukemia\/lymphoma cells. Generally, TdT catalyses the addition of nucleotides to the 3' terminus of a DNA molecule. Unlike most DNA polymerases, it does not require a template. The preferred substrate of this enzyme is a 3'-overhang, but it can also add nucleotides to blunt or recessed 3' ends.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTDT\u003c\/strong\u003e supports biochemical transformations that can be read out as changes in substrate\/product balance, metabolic intermediates, or signaling-relevant small molecules. Defined recombinant enzymes help enable mechanistic dissection and quantitative reconstitution studies. 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 58.3 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant bovine TdT consists of 520 amino acids and migrates with an apparent molecular mass of 58.3 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 Bovine TdT (X04122) (Mer1-Ala520) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 90 % 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 Liquid in sterile 50 mM K2HPO4, 100 mM NaCl, 1 mM DTT, 0.1% Tween20, 1% BSA, 50% Glycerol, 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 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":"40 ug","offer_id":52997740036461,"sku":"PRP3002-40UG","price":99.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740069229,"sku":"PRP3002-100UG","price":189.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP3002.png?v=1770191178"},{"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-il-1-protein-his-tag-animal-free-bhp13700142","title":"Human IL-1à Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eEP\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 Hematopoietin-1, Lymphocyte-Activating Factor (LAF), Endogenous Pyrogen (EP), Leukocyte; IL-1α,IL 1α,Lymphocyte-Activating Factor (LAF),Endogenous Pyrogen (EP),Leukocyte.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eInterleukin-1 alpha (IL1 alpha or IL1α) is a member of the interleukin-1 cytokine family, found constitutively present in epithelial layers of the entire gastrointestinal tract, lung, liver, kidney, endothelial cells, and astrocytes. The synthesized IL-1 alpha is a 31 kDa inactive precursor and can be cleaved by intracellular caspase-1 or extracellular proteases to generate the bioactive 17 kDa form and the 16 kDa N-terminal cleavage product. Both precursor and mature IL-1 alpha protein bind to the IL-1 receptor (IL-1R), initiating a cascade of inflammatory cytokines and chemokines production such as IL-6, IL-8, and TNF, in response to viral and bacterial pathogens conditions. IL-1 alpha plays a central role in immune-surveillance mechanisms, stimulating macrophages, neutrophils, and CD8+ T cells activity.\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\u003eEP\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\u003eImmunology \u0026amp; Inflammation\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 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-1α Protein consists of 159 amino acids and predicts a molecular mass of 19 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IL-1α (Ser113-Ala271)(P01583) 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 D10.G4.1 cells proliferation.The ED₅₀ for this effect is \u0026lt;10 pg\/mL.The specific activity of recombinant human IL-1 alpha is approximately \u0026gt;1 x10⁸ 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. 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":52997740331373,"sku":"PRP1003-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997740364141,"sku":"PRP1003-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740396909,"sku":"PRP1003-100UG","price":549.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997740429677,"sku":"PRP1003-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1003.png?v=1770191179"},{"product_id":"human-tgf-protein-his-tag-animal-free-bhp13700143","title":"Human TGF-α Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTGF-α Protein\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 Sarcoma growth factor, TGF-type I, ETGF, TGFA; TGF-α,TGF α.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eTransforming Growth Factors alpha (TGF-α) is a 5.68 kDa member of the epidermal Growth Factors with 51 amino acid residues. TGF-α is mainly expressed from brain, skin, epithelial cell (pancreatic endocrine cells, urothelial cells, oligodendrocyte precursor cells, etc.). TGF-α is a regulator of cell proliferation and differentiation via bind to the EGFR and to act synergistically with TGF β. TGF-α also associates with myriad forms of cancer.\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\u003eTGF-α Protein\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\u003eOncology \u0026amp; Angiogenesis\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 6.49 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human TGF-α consists of 50 amino acids and predicts a molecular mass of 6.49 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human TGF-α (Val40-ALa89) (P01135) 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 3T3 cells proliferation.The ED₅₀ for this effect is \u0026lt;0.2 ng\/mL.The specific activity of recombinant human TGF alpha is \u0026gt; 5 x 10⁶ 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. 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":52997740462445,"sku":"PRP1004-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997740495213,"sku":"PRP1004-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740527981,"sku":"PRP1004-100UG","price":649.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997740560749,"sku":"PRP1004-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1004.png?v=1770191180"},{"product_id":"human-il-36-protein-his-tag-animal-free-bhp13700144","title":"Human IL-36? Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eEPSILON\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-1F9, IL-1ε (epsilon), IL-1H1, L1RP2, IL-1RP2; IL-36γ,IL 36γ,IL 36gama.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eInterleukin-36 gamma (IL-36γ) consists of 134 amino acids. IL-36γ is a member of the interleukin-1 cytokine family. It plays a significant role in immune responses, particularly in inflammatory reactions, which are essential for binding with interleukin-1 receptor and serves as receptor agonists, enabling cytokine activity and generating pro-inflammatory.\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\u003eEPSILON\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\u003eImmunology \u0026amp; Inflammation\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 17.98 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human IL-36γ consists of 152 amino acids and predicts a molecular mass of 17.98 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human IL-36γ (Ser18-Asp169) (Q9NZH8-1) 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 IL-8 secretion in A431 cells.The ED₅₀ for this effect is \u0026lt;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 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":52997740593517,"sku":"PRP1005-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997740626285,"sku":"PRP1005-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740659053,"sku":"PRP1005-100UG","price":1779.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997740691821,"sku":"PRP1005-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1005.png?v=1770191180"},{"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-tgf-2-protein-his-tag-animal-free-bhp13700146","title":"Human TGF-?2 Protein, His tag (Animal-Free)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTGF-Β2\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 G-TSF, LDS4, TGFB2; G-TSF, LDS4, TGFB2,TGF-β2，TGF β2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eTransforming Growth Factors beta 2 (TGFβ-2) is a 12.85 kDa member of the epidermal Growth Factors with 113 amino acid residues. TGFβ-2 is expressed from throughout the body. TGFβ-2 is a regulator of cell proliferation, differentiation, apoptosis, cell plasticity and migration, etc. TGF-β-2 also associates with various kinds of diseases, such as cancer and tissue fibrosis.\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\u003eTGF-Β2\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\u003eImmunology \u0026amp; Inflammation\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 13.66 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human TGF-β2 consists of 112 amino acids and predicts a molecular mass of 13.66 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human TGF-β2 (Ala 303-Ser 414) (P61812-1) 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 inhibit IL-4-induce proliferation in HT-2 cells.The ED₅₀ for this effect is \u0026lt;0.2 ng\/mL.The specific activity of recombinant human TGF beta 2 is \u0026gt; 5 x 10⁶ 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. 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 solution containing 20 mM 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 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":52997740855661,"sku":"PRP1007-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997740888429,"sku":"PRP1007-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997740921197,"sku":"PRP1007-100UG","price":739.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997740953965,"sku":"PRP1007-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1007.png?v=1770191181"},{"product_id":"human-fgf-1-afgf-protein-his-tag-animal-free-bhp13700147","title":"Human FGF-1\/aFGF Protein, His tag (Animal-Free)","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 HBGF-1, ECGF-beta; FGF-1，FGF1，FGF 1，HBGF-1, ECGF-beta.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eFibroblast Growth Factors-1 (FGF-1) is a Growth Factors of mitogenic peptides which is a 15 kDa protein containing 139 amino acid residues. Fibroblast Growth Factors-1 is secreted by the macrophage which induce endothelial cell proliferation and angiogenesis. During wound injury, fibroblast Growth Factors-1 helps the tissue remodeling. When the fibroblast Growth Factors-1 binds with the FGFR on the cell membrane which is endocytosed by FGFR and induces the cell cycle.\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\u003eOncology \u0026amp; Angiogenesis\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 16.77 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human FGF1 consists of 140 amino acids and predicts a molecular mass of 16.77 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human FGF1 (Phe 16-Asp 155) (P05230-1) 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 3T3 cells proliferation.The ED₅₀ for this effect is \u0026lt;0.3 ng\/mL.The specific activity of recombinant human FGF-1 is \u0026gt; 1 x 10⁶ 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. 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":52997740986733,"sku":"PRP1008-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997741019501,"sku":"PRP1008-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997741052269,"sku":"PRP1008-100UG","price":469.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997741085037,"sku":"PRP1008-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1008.png?v=1770191182"},{"product_id":"human-fgf-5-protein-his-tag-animal-free-bhp13700148","title":"Human FGF-5 Protein, His tag (Animal-Free)","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 HBGF-5, Smag-82; FGF-5，FGF5，FGF 5，HBGF-5,Smag-82.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eFibroblast Growth Factors-5 (FGF-5) is a 29.6 kDa member of the fibroblast Growth Factors with 268 amino acid residues. FGF-5 have an important role in the regulation of cell proliferation and cell differentiation. In physiological function, FGF5 is a crucial regulator of hair growth in humans.\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\u003eOncology \u0026amp; Angiogenesis\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 28.46 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human FGF-5 consists of 251 amino acids and predicts a molecular mass of 28.46 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human FGF-5 (Ala18-Gly268) (P12034-1) 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 3T3 cells proliferation.The ED₅₀ for this effect is \u0026lt;0.7 ng\/mL.The specific activity of recombinant human FGF-5 is \u0026gt; 1.4 x 10⁶ 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. 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":52997741117805,"sku":"PRP1009-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997741150573,"sku":"PRP1009-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997741183341,"sku":"PRP1009-100UG","price":619.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997741216109,"sku":"PRP1009-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1009.png?v=1770191183"},{"product_id":"human-fgf-6-protein-his-tag-animal-free-bhp13700149","title":"Human FGF-6 Protein, His tag (Animal-Free)","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 HBGF-6,HST-2; FGF-6，FGF6，FGF 6，HBGF-6,HST-2.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Human.\u003c\/p\u003e\u003cp\u003eFibroblast Growth Factors-6 (FGF-6) is a 22.9 kDa member of the fibroblast Growth Factors with 208 amino acid residues. FGF-6 is an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis. In physiological function, FGF6 is required for normal muscle regeneration.\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\u003eOncology \u0026amp; Angiogenesis\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 19.66 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant Human FGF-6 consists of 168 amino acids and predicts a molecular mass of 19.66 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Human FGF-6 (Gly41-Ile208) (P10767) 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 3T3 cells proliferation.The ED₅₀ for this effect is \u0026lt;0.1 ng\/mL.The specific activity of recombinant human FGF-6 is \u0026gt; 1 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. 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 solution containing 20 mM 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 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":52997741248877,"sku":"PRP1026-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":52997741281645,"sku":"PRP1026-20UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997741314413,"sku":"PRP1026-100UG","price":549.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997741347181,"sku":"PRP1026-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1026.png?v=1770191183"},{"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"}],"url":"https:\/\/www.ebiohippo.com\/collections\/abbkine-proteins.oembed?page=3","provider":"BioHippo","version":"1.0","type":"link"}