Anti-Crystallin Alpha B antibody
Description
Application Data
Description
-
An antibody raised against Anti-Crystallin Alpha B antibody (CRYAB). CRYAB is a small heat shock protein (chaperone) with roles in aggregate diseases, cancers, cardiomyopathy, and cataracts.
Application Data
-
Anti-Crystallin Alpha B antibody antibody Molecular weight: ~ 20.1 kDa. Western blot analysis of Bovine Lens Soluble Protein Extract. Lane 1: Bovine Lens Soluble Protein Extract Lane 2: Bovine Lens Soluble Protein Extract Western blot image provided courtesy of Dr. Roy Quinlain, Durham University
| Catalogue number | crb2005274 |
|---|---|
| Antibody | Anti-Crystallin Alpha B antibody |
| Antigen Peptide | Crystallin Alpha B protein |
| Aliases | Heat Shock Protein Beta-5, Crystallin Alpha B, CRYAB, Alpha-crystallin B chain,, CRYA2, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component |
| Cross-Reactivity | Human |
| Host Species | Rabbit |
| Antibody Type | Polyclonal |
| Concentration | serum |
| Target | Crystallin Alpha B |
| Family | Small heat shock protein (HSP20) family. |
| Storage | This material is supplied in PBS containing 0.01% sodium azide and 1% trehalose. The product should be stored at +4°C for short term storage and -20°C for long term storage. Avoid repeated freeze/thaw cycles. |
| References | Berry et al., (2001). Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. The American Journal of Human Genetics, 69(5): 1141. doi: 10.1086/324158. Zhang et al., (2019). Progression of the role of CRYAB in signaling pathways and cancers. Onco Targets Ther., 12: 4129. PMID: 31239701. |
Anti-Crystallin Alpha B antibody (CRYAB) is part of the small heat shock protein (HSP20) family, acting as a chaperone. The holdase activity aims to prevent the aggregation of various proteins in various cellular processes, often to prevent the proteasomal degradation of client proteins. CRYAB aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. CRYAB associates with intermediate filaments as one of the cytoskeletal elements. Not much is known about CRYAB regulation.
CRYAB dysregulation is linked to several aggregate diseases and is a histopathological marker for aggregate-based human disorders. CRYAB is also involved in numerous prostate, lung, and ovarian cancers. In addition, CRYAB is a biomarker for poor prognosis of breast carcinoma progression and metastases to the brain.
Mutations to the CRYAB gene are linked to several myopathies, including cardiomyopathy. Mutated CRYAB results in large granules and aggregates, leading to muscle rigidity, breathing difficulty, congestive heart failure, arrhythmia, and premature death.
CRYAB may contribute to the transparency and refractive index of the lens. In addition, in lens epithelial cells, CRYAB stabilizes the ATP6V1A protein, preventing its degradation by the proteasome. Dysregulation of CRYAB is involved in cataracts.