Vitronectin Antibody (Monoclonal)

A murine monoclonal antibody to human Vitronectin.

100 µl

Purified human protein.

IgG1k

≥ 95% by SDS PAGE

This monoclonal antibody was raised against purified human S Protein (Vitronectin).

Short term (30 days) 4˚C. Long term at or below –20˚C.

In contract to membrane-formed C5b-9 complexes, C5b-9 complexes formed in the fluid phase contain an additional protein, the S protein. Subsequently, it was found that isolated S protein inhibited C5b-9 attachment. S protein functions like a “membrane analogue” in that it binds to the binding site generated on assembly of C5b-9 and is required for insertion of the complex into the membrane. As a result, SC5b-7, SC5b-8 or SC5b-9 complexes are formed which have lost their membrane-binding capacity. When the S protein was cloned and sequenced, it was found to be identical to Vitronectin. Within the complement cascade, Vitronectin not only inhibits attachment of C5b-9 to target cells, but also prevents C9 polymerization. The biological function of Vitronectin is to minimize complement-mediated attack of cells in the vicinity of an ongoing complement attack. This may be relevant, not only during the generation of bactericidal activity in the case of infection, but also in autoimmune disease, immune complex disease, or inflammatory lesions, where complement is readily activated by dead or dying cells, exposed basement membranes or matrix proteins. S protein is present in human plasma at an approximate concentration of 150 µg/mL.