Tumor Necrosis Factor Receptor-IgG1, Fc Active Protein

Tumor Necrosis Factor Receptor-IgG1, Fc (Fusion Protein), Recombinant, Human (TNFR)

Cat. Num. AAA637920

• Purity: Highly Purified; 98% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.
• Synonyms: Tumor Necrosis Factor Receptor-IgG1; Fc; Fc (Fusion Protein); Recombinant; Human (TNFR); Fc active protein

• Host: CHO cells
• Purity/Purification: Highly Purified; 98% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.
• Form/Format: Supplied as a lyophilized powder. Each mg of protein contains 1.6mg mannitol, 0.4mg sucrose, 48ug tromethamine.

• Biological Activity: Recombinant Human TNF-alpha is fully biologically active when compared to standard. Potency is determined by its ability to neutralize TNF-alpha mediated growth inhibition of A375 cells, corresponding to a Specific Activity of 1.7x10e7 IU/mg.
• Reconstitution: Reconstitute in sterile ddH2O, 0.1% BSA or HSA to a concentration of >0.1mg/ml
• Preparation and Storage: Lyophilized powder may be stored at -20 degree C. Reconstitute with sterileddH2O, 0.1% BSA or HSA. Aliquot and store at -20 degree C. Reconstituted product is stable for 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for Tumor Necrosis Factor Receptor-IgG1, Fc active protein

TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR. Recombinant Human TNFR is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules. It inhibits the activity of TNF in vitro and has been shown to affect several animal models of inflammation, including murine collagen-induced arthritis. TNFR inhibits binding of both TNF and TNF (lymphotoxin alpha [LT ]) to cell surface TNFRs, rendering TNF biologically inactive. Cells expressing transmembrane TNF that bind to TNFR are not lysed in vitro in the presence or absence of complement. rTNFR can also modulate biological responses that are induced or regulated by TNF, including expression of adhesion molecules responsible for leukocyte migration (i.e., E-selectin and to a lesser extent intercellular adhesion molecule-1 [ICAM-1]), serum levels of cytokines (e.g., IL-6), and serum levels of matrix metalloproteinase-3 (MMP-3 or stromelysin).

Recombinant Human TNFR produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of the extracellular ligand-binding portion of the human 75 kilodalton (p75) tumor necrosis factor receptor (TNFR) linked to the Fc portion of human IgG1. The Fc component of TNFR contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. It consists of 934 amino acids and has an apparent molecular weight of approximately 150 kilodaltons. Recombinant TNF Receptor is purified by standard chromatographic techniques.

Product Categories/Family for Tumor Necrosis Factor Receptor-IgG1, Fc active protein

Molecular Biology; MB-Receptors