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C3b is the larger of two elements formed by the cleavage of complement component 3, and is considered an important part of the innate immune system. C3b is potent in opsonization: tagging pathogens, immune complexes (antigen-antibody), and apoptotic cells for phagocytosis.
C4b-binding protein inhibits the haemolytic function of cell-bound C4b. C4b-binding protein and C3b inactivator control the C3 convertase of the classical pathway in a similar way to that described for β1H and C3b inactivator in the alternative pathway. [8] C3b has different binding site for C3bINA, β1H, factor B and properdin.
The reference designator usually consists of one or two letters followed by a number, e.g. C3, D1, R4, U15. The number is sometimes followed by a letter, indicating that components are grouped or matched with each other, e.g. R17A, R17B. The IEEE 315 standard contains a list of Class Designation Letters to use for electrical and electronic ...
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The C5-convertase of the alternative pathway consists of (C3b) 2 BbP (sometimes referred to as C3b 2 Bb). After the creation of C5 convertase (either as (C3b) 2 BbP or C4b2a3b from the classical pathway), the complement system follows the same path regardless of the means of activation (alternative, classical, or lectin). C5-convertase cleaves ...
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To prevent this from happening, factor H competes with factor B to bind C3b; if it manages to bind, then the convertase is not formed. Factor H can bind C3b much more easily in the presence of sialic acid, which is a component of most cells in the human body; conversely, in the absence of sialic acid, factor B can bind C3b more easily. This ...
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