IL-6 ELISA/人白细胞介素6 ELISA检测试剂盒

Interleukin-6 (IL-6), also known as B-cell stimulatory factor 2 (BSF-2), CTL differentiation factor (CDF), Hybridoma growth factor or Interferon beta-2 (IFN-beta-2), was successfully cloned by Hirano et al. in 1986 (Hirano T et al.) . The gene is mapped at chromosome 7p21. IL-6 protein is built up by 183 amino acids and has a calculated molecular weight of 23.7 kDa. It is a pleiotropic, alpha helical protein that is composed of a four-helix bundle (Somers W et al.). It shares 39% sequence identity with mouse and 40% with rat IL-6. IL-6 is phosphorylated at amino acid 81 and it is variably glycosylated by N-linked glycosylation. IL-6 belongs to the IL-6/GCSF/MGF protein family (Rose-John S et al.) whose members share a common use of the gp130 receptor subunit. IL-6 isoforms, with internal deletions, are generated by alternative splicing. The principal cell sources for IL-6 are mononuclear phagocytes, vascular endothelial cells, fibroblasts or other cells. IL-6 is the ligand for the Interleukin-6 receptor α (IL-6Rα) (Schwantner A et al.) that occurs membrane-bound, but that may also circulate as soluble form generated by alternative splicing or proteolytic cleavage. To induce signaling, IL-6 first forms a complex with the non-signaling IL-6Rα. Subsequent binding to the signal transducing subunit gp130 leads to dimerization of gp130 and finally to the formation of the hexameric signaling complex (Boulanger MJ et al.). Complexes of IL-6 and soluble IL-6Rα may elicit responses in cells lacking the membrane-bound IL-6Rα but expressing the ubiquitous gp130 coreceptor. This process is known as trans-signaling, it enlarges the spectrum of target cells responding to IL-6 (Mihara M et al.).