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Description

Native, human iC3b complement component. iC3b is formed by the cleavage of C3b by Factor I in the presence of Factor H, CR1, or membrane cofactor protein. Factor I cleavage of C3b to iC3b inactivates and prevents C3b from functioning in the C3 or C5 convertase enzymes. The iC3b fragment thus produced is a glycoprotein composed of two C3alpha' polypeptides of M.W. 43 kDa and M.W. 63 kDa which are disulfide bonded to the intact C3 beta-chain (M.W. 75 kDa). iC3b interaction with CR3 (CD11b/CD18) receptors present on a variety of white blood cells greatly enhances phagocytosis of iC3b coated target cells or particles., Native, human iC3b complement component. iC3b is formed by the cleavage of C3b by Factor I in the presence of Factor H, CR1, or membrane cofactor protein. Factor I cleavage of C3b to iC3b inactivates C3b from functioning in the C3 or C5 convertase enzymes. The iC3b fragment thus produced is a glycoprotein composed of two C3alpha' polypeptides of M.W. 43,000 and M.W. 63,000 are disulfide bonded to the intact C3 b-chain (M.W. 75,000). iC3b interaction with CR3 (CD11b/CD18) receptors present on a variety of white blood cells greatly enhances phagocytosis of iC3b coated target cells or particles.