Crystallin, alpha A (CRYAA) antibody

Antigen: Crystallin, alpha A (CRYAA)

Synonyms: CRYA1, HSPB4, Crya1, lop18, Acry-1, Crya-1, DAcry-1, AI323437, cryaa-A, CRYAA, fc06h04, MGC92036, zgc:92036, wu:fc06h04, alpha-a-crystallin

Clonality: Monoclonal (1H3-B8)

Host: Mouse

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

Application: Western Blotting (WB), ELISA

Catalog no.: ABIN361798

Additional Information

Alternative name: Alpha A Crystallin

Immunogen: Native Alpha Crystallin

Format: Protein G purified

Isotype: IgG1  (Matching secondary antibodies)

Clone: 1H3-B8

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 (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

Specificity: Detects alpha crystallin at ~20kDa. Species cross-reactivity: Human, Mouse, Cow, Rat. Other species not tested. Detects alpha crystallin complex (containing alpha A and alpha B subunits). Does not cross react with alpha B crystallin, beta-L crystallin, Beta-H crystallin, gamma crystallin, Hsp25, Hsp27 or Hsp47 proteins.

Application Details

Application Notes: WB 1/2000

Concentration: 1mg/mL

Buffer: PBS pH 7.2, 50% glycerol, 0.09% azide. Protein G affinity purified.

Storage: -20°C, 1 year+, shipped on cold packs or ambient

Restrictions: For Research Use only

Images

Alpha A Crystallin (1H3.B8), alphaA (L) and AlphaB (R) crystallin

Publications

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).

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).