Anti-Alpha B Crystallin / CRYAB, clone CPTC-CRYAB-1

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta and gamma families, and the beta- and gamma-crystallins also compose a superfamily. Crystallins usually contain seven distinct protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha-crystallins consist of three gene products, alpha-A-, alpha-B- and alpha-C-crystallin, which are members of the small heat shock protein family (HSP 20). Alpha-crystallins act as molecular chaperones by holding denatured proteins in large soluble aggregates. However, unlike other molecular chaperones, alpha-crystallins do not renature these proteins. Expression of alpha-A-crystallin is restricted to the lens and defects of this gene cause the development of autosomal dominant congenital cataracts (ADCC). The human alpha-B-crystallin gene product is expressed in many tissues, including lens, heart and skeletal muscle. Elevated expression of alpha-B-crystallin is associated with many neurological diseases, and a missense mutation in this gene has co-segregated in a family with a Desmin-related myopathy. Protein function: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome. [The UniProt Consortium]