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Species cross reactivity not tested 

2°C to 8°C  (≤ 30 days)

For long-term storage (> 30 days), aliquot and store at ≤ –20°C. Avoid repeated freeze-thaw.

For Research Use Only. Not for use in diagnostic procedures

Highly purified human Victronectin was isolated and used to immunize rabbits. The Anti-Human Vitronectin polyclonal antisera was tested by immunodiffusion methods and determined to be monospecific for the Vitronectin protein

In contrast 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 near an ongoing complement attack 

Applications of the Anti-Human Vitronectin antisera have been evalsuated, and include immunodiffusion, Western Blot and ELISA