Mouse alpha B Crystallin Monoclonal Antibody | anti-CRYAB antibody
Alpha B Crystallin Antibody: PerCP
Western Blot (WB)
(Western Blot analysis of Bovine cell lysates showing detection of Alpha B Crystallin protein using Mouse Anti-Alpha B Crystallin Monoclonal Antibody, Clone 1A7.D5. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Alpha B Crystallin Monoclonal Antibody at 1:50 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.)
Scientific Background: The alpha-crystallins are major water-soluble lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. The alpha-crystallins possess structural and functional similarities with Hsp25 and Hsp27 (1). Mammalian lens cystallins are divided into alpha, beta and gamma families. Alpha and beta families are further divided into acidic and basic groups (Alpha-A and Alpha-B respectively). In the lens, alpha-crystallin primarily functions to maintain proper refractive index, however it can also function as a molecular chaperone that binds to the denatured proteins, keeping them in solution and thereby maintaining the translucency of the lens. When cellular stress occurs, alpha-crystallin enters its' phosphorylated state and may serve a structural control function and play a role in protein maintenance (2). In addition to their interaction with proteins, alpha-crystallins also interact with native molecules such as membrane proteins, Golgi matrix protein, structural proteins, nuclear proteins and DNA (3, 4, 5, 6, and 7). Two other functions are an autokinase activity and participation in the intracellular architecture, and it has also been proven that both alpha-A and B prevent apoptosis by inhibiting caspases (8). Specifically, alpha-B cystallin is found in many cells and organs outside the lens, and alpha B is overexpressed in several neurological disorders and in cell lines under stress conditions (9).
1. Banduseela, V.C. et al. (2009). Gene expression and muscle fiber function in a porcine ICU model. Physiol Genomics. 39 (3), 141-159. doi: 10.1152/physiolgenomics.00026.2009.
2. Aare, S. et al. (2011). Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model. Physiol Genomics. 43 (24), 1334-1350. doi: 10.1152/physiolgenomics.00116.2011.
3. Ochala, J. et al. (2011). Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms. J Physio. 589 (8). 2007-2026. doi: 10.1113/jphysiol.2010.202044.
NCBI and Uniprot Product Information
NCBI Description
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. 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. [provided by RefSeq, Jan 2014]
Uniprot Description
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
Chromosomal Location of Human Ortholog: 11q22.3-q23.1
Cellular Component: microtubule cytoskeleton; Golgi apparatus; cell surface; mitochondrion; cytoplasm; actin filament bundle; plasma membrane; cytosol; Z disc; nucleus
Molecular Function: identical protein binding; protein binding; protein homodimerization activity; metal ion binding; microtubule binding; unfolded protein binding; structural constituent of eye lens
Biological Process: lens development in camera-type eye; muscle development; protein folding; stress-activated MAPK cascade; microtubule polymerization or depolymerization; negative regulation of caspase activity; response to estradiol stimulus; tubulin folding; negative regulation of intracellular transport; response to hydrogen peroxide; muscle contraction; response to hypoxia; negative regulation of cell growth; protein homooligomerization; aging; negative regulation of apoptosis
Disease: Cataract 16, Multiple Types; Myopathy, Myofibrillar, Fatal Infantile Hypertonic, Alpha-b Crystallin-related; Myopathy, Myofibrillar, 2; Cardiomyopathy, Dilated, 1ii
