Crystallin Alpha B (mCRYAB) Mouse Recombinant Protein

This gene encodes a member of the small heat-shock protein (HSP20) family. The encoded protein is a molecular chaperone that protects proteins against thermal denaturation and other stresses. This protein is a component of the eye lens, regulates lens differentiation and functions as a refractive element in the lens. This protein is a negative regulator of inflammation, has anti-apoptotic properties and also plays a role in the formation of muscular tissue. Mice lacking this gene exhibit worse experimental autoimmune encephalomyelitis and inflammation of the central nervous system compared to the wild type. In mouse models, this gene has a critical role in alleviating the pathology of the neurodegenerative Alexander disease. Mutations in the human gene are associated with myofibrillar myopathy 2, fatal infantile hypertonic myofibrillar myopathy, multiple types of cataract and dilated cardiomyopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]

CRYAB: a major structural protein of the eye lens. A member of the small heat shock protein (sHSP also known as the HSP20) family. Alpha-B is expressed in the lens as well as other tissues. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

Protein type: Heat shock protein; Chaperone

Cellular Component: Golgi apparatus; I band; cell surface; contractile fiber; mitochondrion; actin filament bundle; Z disc; cytosol; microtubule cytoskeleton; cytoplasm; plasma membrane; nucleus; myelin sheath

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; microtubule binding; metal ion binding; cytoskeletal protein binding; unfolded protein binding; structural constituent of eye lens

Biological Process: lens development in camera-type eye; muscle development; camera-type eye development; protein folding; stress-activated MAPK cascade; microtubule polymerization or depolymerization; negative regulation of caspase activity; tubulin folding; negative regulation of intracellular transport; response to hydrogen peroxide; response to hypoxia; negative regulation of cell growth; protein homooligomerization; negative regulation of apoptosis