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Description
The monoclonal antibody bH6 recognizes a neo-epitope expressed on the cleavage fragments of C3b, iC3b, and C3c. The complement system is an important factor in innate immunity. The third complement component, C3, is central to the classical, alternative and lectin pathways of complement activation. Activation products of the complement cascade contain neo-epitopes that are not present in the individual native components. Monoclonal antibodies detecting neo-epitopes have been used for direct quantification of activation at different steps in the complement cascade. The synthesis of C3 is tissue-specific and is modulated in response to a variety of stimulatory agents. C3 is the most abundant protein of the complement system with serum protein levels of about 1.3 mg/ml. An inherited deficiency of C3 predisposes the person to frequent assaults of bacterial infections. In ulcerative colitis, and idiopathic chronic inflammatory bowel disease, the deposition of C3 in the diseased mucosa has been reported. Proteolysis by certain enzymes results in the cleavage of C3 into C3a and C3b. C3b becomes attached to immune complexes and is further cleaved into iC3b, C3c, C3dg and C3f. The monoclonal antibody bH6 is specific for a C3 neo-epitope expressed on the cleavage fragments of C3b, iC3b, and C3c, but not C3dg and C3f.