Crystallin, alpha A (CRYAA) Antikörper

Antigen: Crystallin, alpha A (CRYAA)

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

Klonalität: Monoklonal (1H3-B8)

Wirt: Maus

Reaktivität: Human, Maus, Rind (Kuh), Ratte (Rattus)

Applikation: Western Blot (WB), ELISA

Produktnummer: ABIN361798

Produktbeschreibung

Produktmerkmale: Detects alpha-crystallin at ~20kDa. Does not cross-react with alphaB-crystallin, betaL-crystallin, BetaH- crystallin, gamma-crystallin, Hsp25, Hsp27 or Hsp47 proteins.

Weitere Bezeichnung: Alpha A Crystallin

Gen-ID: 1409

Swiss-Prot: P02489

Immunogen: Native Alpha Crystallin

Format: Liquid

Isotyp: IgG1  (Passende Sekundärantikörper)

Klon: 1H3-B8

Beschreibung: 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.
Synonyms: Heat shock protein beta4, Acry 1, CRYA1, CRYAA, HspB4

Spezifität: 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.

Sensitivität: 0.5µg/ml was sufficient for detection of 100ng purified alphaA crystalline by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Anwendungen

Applikationshinweise: 1:2000 (WB)

Konzentration: 1 mg/mL

Reinigung: Protein G Purified

Buffer: PBS pH7.2, in 50% glycerol

Lagerung: -20 °C

Storage Shipping Temp Max: Blue Ice or 4 °C

Beschränkungen: Nur für Forschungszwecke einsetzbar

Bilder

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

Publikationen

Publikationen: 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).