Anti-Alpha B Crystallin/CRYAB Antibody Picoband® Fluoro647 Conjugated

Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene. 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. 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. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. Alternative splicing results in multiple transcript variants.

Calpain-2 catalytic subunit;3.4.22.53; Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain; M-calpain; CAPN2; CANPL2

Calcium Signaling, Cancer, Cancer Metabolism, Cell Biology, Metabolism, Metabolism Processes, Pathways and Processes, Proteolysis/Ubiquitin, Proteolytic Enzymes, Response To Hypoxia, Signal Transduction, Signaling Pathway

Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508) . .

1. Berry, V., Francis, P., Reddy, M. A., Collyer, D., Vithana, E., MacKay, I., Dawson, G., Carey, A. H., Moore, A., Bhattacharya, S. S., Quinlan, R. A. Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. Am. J. Hum. Genet. 69: 1141-1145, 2001. 2. Brakenhoff, R. H., Geurts van Kessel, A. H. M., Oldenburg, M., Wijnen, J. T., Bloemendal, H., Meera Khan, P., Schoenmakers, J. G. G. Human alpha-B-crystallin (CRYA2) gene mapped to chromosome 11q12-q23. Hum. Genet. 85: 237-240, 1990. 3. Chavez Zobel, A. T., Loranger, A., Marceau, N., Theriault, J. R., Lambert, H., Landry, J. Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alpha-B-crystallin mutant. Hum. Molec. Genet. 12: 1609-1620, 2003.