Alpha Crystallin A (CRYAA) Antibody – Mouse Monoclonal

Mammalian lens crystallins are divided into alpha, beta, and gamma families. 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 (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC). [provided by RefSeq, Jan 2014]

CRYA1: a major structural protein of the eye lens. A member of the small heat shock protein (sHSP, also known as the HSP20) family. Alpha-A is preferentially restricted to the lens.

Protein type: Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 21q22.3

Cellular Component: cytoplasm; nucleus

Molecular Function: identical protein binding; protein binding; metal ion binding; unfolded protein binding; structural constituent of eye lens

Biological Process: negative regulation of intracellular transport; visual perception; response to stimulus; protein refolding; protein homooligomerization; negative regulation of apoptosis

Disease: Cataract 9, Multiple Types