Crystallin, alpha B (CRYAB) antibody

Antigen: Crystallin, alpha B (CRYAB)

Synonyms: CRYA2, CTPP2, HSPB5, Crya2, HspB5, Crya-2, AACRYA, CRYAB, DKFZp468D2015, Cryab

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human, Mouse (Murine), Rat (Rattus), Cow (Bovine), Chicken

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC)

Catalog no.: ABIN361836

Additional Information

Alternative name: Crystallin Alpha B

Gene ID: 1410

UniProt: P02511

Immunogen: Synthetic peptide corresponding to human alpha B crystallin conjugated to KLH.

Description: 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. 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. 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. 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. 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.
Synonyms: AACRYA, Alpha crystallin B chain, CRYA2, CRYAB, CTPP2, HspB5, NY REN 27 antigen

Characteristics: Accession Number: NP_001876.1

Specificity: Detects ~22kDa. Does not cross-react with alphaA-crystallin.

Application Details

Application Notes: 1:5000-10000 (ECL) (WB)

Purification: Rabbit antiserum

Storage: Store at -20° C. Shipping Temperature: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins

Restrictions: For Research Use only

Publications

Horwitz: "Alpha-crystallin can function as a molecular chaperone." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 21, pp. 10449-53, 1992 (PubMed).

Merck, Groenen, Voorter et al.: "Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones." in: The Journal of biological chemistry, Vol. 268, Issue 2, pp. 1046-52, 1993 (PubMed).

Head, Goldman: "Small heat shock proteins, the cytoskeleton, and inclusion body formation." in: Neuropathology and applied neurobiology, Vol. 26, Issue 4, pp. 304-12, 2000 (PubMed).

Cobb, Petrash: "alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts." in: Biochemistry, Vol. 41, Issue 2, pp. 483-90, 2002 (PubMed).

Horwitz: "Alpha-crystallin." in: Experimental eye research, Vol. 76, Issue 2, pp. 145-53, 2003 (PubMed).

Bullard, Ferguson, Minajeva et al.: "Association of the chaperone alphaB-crystallin with titin in heart muscle." in: The Journal of biological chemistry, Vol. 279, Issue 9, pp. 7917-24, 2004 (PubMed).

Gangalum, Schibler, Bhat: "Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization." in: The Journal of biological chemistry, Vol. 279, Issue 42, pp. 43374-7, 2004 (PubMed).

Maddala, Rao: "alpha-Crystallin localizes to the leading edges of migrating lens epithelial cells." in: Experimental cell research, Vol. 306, Issue 1, pp. 203-15, 2005 (PubMed).

Yaung, Jin, Barron et al.: "alpha-Crystallin distribution in retinal pigment epithelium and effect of gene knockouts on sensitivity to oxidative stress." in: Molecular vision, Vol. 13, pp. 566-77, 2007 (PubMed).