The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Complement component 4-binding protein (C4BP) is a plasma glycoprotein that inhibits the classical pathway of complement activation, which is mediated through antibody targeting of foreign antigen. Structurally, C4BP is a disulfide linked, multimeric protein that is composed of seven α chains and one β chain. C4BP functions as a cofactor for C3β inactivator in the cleavage of C3β, and accelerates the decay of C4βC2α (C3 convertase) by acting as a cofactor in the cleavage of C4β by factor I. Streptococcal strains that express Ig-binding cell surface molecules, which are members of the M protein family,can bind to overlapping C4β binding sites in C4BP and therefore, interfere with the classical pathway of complement activation. Bacteria-bound C4BP may be an evolved mechanism that downregulates complement activation in the bacterial host microenvironment, thereby reducing the occurances of bacterial opsonization and phagocytosis.
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Protein Aliases: C4b-binding protein beta chain; C4BPB
Gene Aliases: C4BP; C4BPB
UniProt ID: (Human) P20851
Entrez Gene ID: (Human) 725