Anti-IL1 beta/IL1B Antibody (PE Conjugate)

Interleukin-1β (IL-1β) is a potent stimulator of bone resorption whose gene is mapped to 2q14, and has been implicated in the pathogenesis of high bone turnover and osteoporosis. IL-1β, a prominent microglia-derived cytokine, caused oligodendrocyte death in coculture with astrocytes and microglia, but not in pure culture of oligodendrocytes alone. It also can cause nuclear export of a specific NCOR corepressor complex, resulting in derepression of a specific subset of nuclear factor-kappa-B (NFKB)-regulated genes. Furthermore, Microenvironmental IL-1β and, to a lesser extent, IL-1α are required for in vivo angiogenesis and invasiveness of different tumor cells. Additional, the cooperation of IL-1β and PDGFB induces contractile-to-synthetic phenotype modulation of human aortic smooth muscle cells in culture. Moreover, the association with disease may be explained by the biologic properties of IL-1β, which is an important proinflammatory cytokine and a powerful inhibitor of gastric acid secretion.

A synthetic peptide corresponding to a sequence at the C-terminus of rat IL-1 beta, different from the related human sequence by five amino acids, and from the related mouse sequence by one amino acid.

Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Secreted. The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.