BackgroundIL-1R1 is an 80 kD transmembrane glycoprotein and a member of the Ig superfamily. IL-1 binds both IL-1R1 and IL-1R2. The ligands IL-1α and IL-1β only commence when binding IL-1R1 because IL-1R2 acts as a decoy receptor and competitively antagonizes the binding of IL-1α and IL-1β, thereby reducing their biological effects. Binding of the ligands to IL-1R1 is enhanced by an accessory protein, IL-1R-AcP. IL-1α can exist as either a 31 kD precursor or an 18 kD mature form. IL-1α is a proinflammatory cell-associated cytokine and IL-1β is a 17.5 kD proinflammatory secreted cytokine. Both IL-1α and IL-1β bind to the same receptor and have similar properties that include stimulation of thymocyte proliferation via IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. Furthermore, IL-1β mediates a variety of immune and inflammatory responses. IL-1β is a major cause of severe inflammation in the mouse model of Crohn’s Disease, which makes IL-1β an important target for this disease. Protein DetailsPurity >97% by SDS-PAGE and analyzed by silver stain. Endotoxin Level <0.1 EU/µg as determined by the LAL method Biological Activity The biological activity of Human IL-1 Beta was determined by a cell proliferation assay using the murine helper T cell line, D10.G4.1 (Symons, J.A. et al., Lymphokines and Interferons, a Practical Approach, 1987, M.J. Clemens, A.G. Morris, and A.J.H. Gearing, eds., IRL Press, p. 272). The expected ED50 for this effect is typically <12 pg/ml. Expression Host E. coli Protein Accession No. Amino Acid Sequence apvr slnctlrdsq qkslvmsgpy elkalhlqgq dmeqqvvfsm sfvqgeesnd kipvalglke knlylscvlk ddkptlqles vdpknypkkk mekrfvfnki einnklefes aqfpnwyist sqaenmpvfl ggtkggqdit dftmqfvss
N-terminal Sequence Analysis Ala117 & Pro118 State of Matter Solution Predicted Molecular Mass The predicted molecular weight of Recombinant Human IL-1 Beta is Mr 17 kDa. Additionally, the actual molecular weight as observed by migration on SDS-PAGE is 17 kDa (reducing conditions). Formulation This recombinant protein solution was 0.2 µm filtered and supplied in modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives present at a concentration of 1.25 mg/ml. Storage and Stability This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions. Country of Origin USA Shipping Dry Ice PubMed NCBI Gene Bank References & Citations1. Gelmann, EP. et al. (2008) Cancer Res. 68(17):6896-901. PubMed 2. Arend, WP. et al. (2003) Cytokine Growth Factor Rev. 13:323 3. Nicklin, MJ. et al. (1994) Genomics 19:382 4. Dunn, E. et al. (2001) Trends Immunol. 22:533 5. Samad, TA. et al. (2001) Nature 410:425 IMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein. |
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