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Overview
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Recombinant Human CRYAA produced in E. Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids and having a molecular mass of 19,909 Dalton. CRYAA is purified by proprietary chromatographic techniques. Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein(sHSP also known as the HSP20). They act as molecular chaperones and hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. The expression of alpha-A is preferentially restricted to the lens cell.
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- Properties
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Overview