Crystallin, alpha A (CRYAA) antibody

Details for Product No. ABIN361798
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Antigen
Synonyms CRYA1, CTRCT9, HSPB4, Crya1, lop18, Acry-1, Crya-1, DAcry-1, AI323437, cryaa-A, CRYAA, wu:fc06h04, zgc:92036, alpha-a-crystallin
Reactivity
Human, Cow (Bovine), Rat (Rattus)
(33), (12), (11), (6)
Host
Mouse
(30), (7)
Clonality (Clone)
Monoclonal ()
Application
Western Blotting (WB), ELISA
(30), (20), (3), (1), (1), (1), (1)
Pubmed 8 references available
Catalog no. ABIN361798
Quantity 50 µg
Price
185.90 $   Plus shipping costs $45.00
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Immunogen Native Alpha Crystallin
Clone 1H3-B8
Isotype IgG1
Specificity Detects α-crystallin at approx. 20 kDa.
Cross-Reactivity (Details) Does not cross-react with αB-crystallin, βL-crystallin, ΒH- crystallin, γ-crystallin, Hsp25, Hsp27 or Hsp47 proteins.
Sensitivity 0.5 µg/ml was sufficient for detection of 100 ng purified alphaA crystalline by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
Purification Protein G Purified
Alternative Name Alpha A Crystallin
Background Synonyms:
Heat shock protein beta4, Acry 1, CRYA1, CRYAA, HspB4
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 denaturedproteins, 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.
Gene ID 1409
NCBI Accession NP_000385.1
UniProt P02489
Research Area Chaperones, Transporters
Application Notes Recommended Dilution: 1:2000 (WB)
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.2, in 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Storage -20 °C
Supplier Images
anti-Crystallin, alpha A (CRYAA) antibody Alpha A Crystallin (1H3 B8), alphaA (L) and AlphaB (R) crystallin.
Background 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).

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).

General 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).

Hosts (30), (7)
Reactivities (33), (12), (11), (6)
Applications (30), (20), (3), (1), (1), (1), (1)
Epitopes (2), (2), (1), (1)
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