Crystallin, alpha B (CRYAB) antibody

Details for Product No. ABIN361812
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

 
Antigen
Synonyms CMD1II, CRYA2, CTPP2, CTRCT16, HSPB5, MFM2, Crya2, HspB5, Crya-2, AACRYA, CRYAB
Reactivity
Human, Cow (Bovine)
(226), (131), (117), (89), (62), (37), (36), (7), (1), (1)
Host
Mouse
(156), (74), (5)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(8), (8), (6), (6), (6), (6), (6), (6), (6), (6), (6), (2), (2), (2)
Application
Western Blotting (WB), ELISA
(161), (98), (62), (60), (50), (18), (15), (11), (9), (4), (2), (2), (1)
Pubmed 10 references available
Catalog no. ABIN361812
Quantity 50 µg
Price
185.90 $   Plus shipping costs $45.00
Options
Shipping to United States (Change)
Availability Will be delivered in 3 to 4 Business Days

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Native Alpha B Crystallin
Clone 3A10-H4
Isotype IgG1
Specificity Detects a band at approx. 20 kDa (predicted mol.weight is approx. 21 kDa) corresponding to αB-crystallin.
Cross-Reactivity (Details) Does not cross-react with αA-crystallin, βL-crystallin, ΒH-crystallin, γ-crystallin, Hsp25, Hsp27 or Hsp47 proteins.
Sensitivity 0.5 µg/mL of SMC-165 was sufficient for detection of 50 ng purified alpha B crystalline by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name Alpha B Crystallin
Background Synonyms:
AACRYA, Alpha crystallin B chain, CRYA2, CRYAB, CTPP2, HspB5, NY REN 27 antigen
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’ phosphorylatedstate 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.
Gene ID 1410
NCBI Accession NP_001876.1
UniProt P02511
Research Area Cancer, Tyrosine Kinases, Heat Shock Proteins
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
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).

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).

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).

Banduseela, Ochala, Chen et al.: "Gene expression and muscle fiber function in a porcine ICU model." in: Physiological genomics, Vol. 39, Issue 3, pp. 141-59, 2009 (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 (156), (74), (5)
Reactivities (226), (131), (117), (89), (62), (37), (36), (7), (1), (1)
Applications (161), (98), (62), (60), (50), (18), (15), (11), (9), (4), (2), (2), (1)
Conjugates (8), (8), (6), (6), (6), (6), (6), (6), (6), (6), (6), (2), (2), (2)
Epitopes (32), (19), (19), (14), (12), (12), (10), (10), (5), (3), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
back to top