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CRYAB antibody (Crystallin, alpha B)

Details for Product anti-CRYAB Antibody No. ABIN361809, Supplier: Log in to see
Antigen
  • AACRYA
  • CMD1II
  • Crya-2
  • Crya2
  • CRYA2
  • CRYAB
  • CTPP2
  • CTRCT16
  • HspB5
  • HSPB5
  • MFM2
Reactivity
Cow (Bovine), Human, Pig (Porcine), Rat (Rattus)
400
184
166
80
23
23
3
2
2
1
1
1
Host
Mouse
220
170
15
1
Clonality (Clone)
Monoclonal ()
Conjugate
This CRYAB antibody is un-conjugated
18
17
16
9
9
9
6
6
6
6
6
6
6
6
6
5
5
5
5
5
5
5
5
5
5
5
2
2
2
Application
ELISA, Western Blotting (WB)
314
188
129
66
65
42
25
24
18
7
4
2
1
Supplier
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Immunogen Native Alpha B Crystallin
Clone 1A7-D5
Specificity Detects ~20 kDa (Predicted mol. weight is ~21 kDa). 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-159 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 (CRYAB Antibody Abstract)
Background 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' phosphorylated state and may serve a structural control function and play a role in protein maintenance (2). 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 (3, 4, 5, 6, and 7). 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 (8). 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 (9).
Cellular Localization: Cytoplasm | Nucleus
Gene ID 1410
NCBI Accession NP_001876
UniProt P02511
Research Area Cancer, Tyrosine Kinases
Application Notes Recommended Dilution: WB (1:2000), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-CRYAB antibody (Crystallin, alpha B) (ABIN361809) Alpha B Crystallin (1A7 D5), AlphaA (L), AlphaB (R).
Product cited in: Akkad, Corpeno, Larsson: "Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model." in: PLoS ONE, Vol. 9, Issue 4, pp. e92622, 2014

Ochala, Gustafson, Diez, Renaud, Li, Aare, Qaisar, Banduseela, Hedström, Tang, Dworkin, Ford, Nair, Perera, Gautel, Larsson: "Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms." in: The Journal of physiology, Vol. 589, Issue Pt 8, pp. 2007-26, 2011

Aare, Ochala, Norman, Radell, Eriksson, Göransson, Chen, Hoffman, Larsson: "Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model." in: Physiological genomics, Vol. 43, Issue 24, pp. 1334-50, 2011

Banduseela, Ochala, Chen, Göransson, Norman, Radell, Eriksson, Hoffman, Larsson: "Gene expression and muscle fiber function in a porcine ICU model." in: Physiological genomics, Vol. 39, Issue 3, pp. 141-59, 2009

Background publications Yaung, Jin, Barron, Spee, Wawrousek, Kannan, Hinton: "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

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

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

Bullard, Ferguson, Minajeva, Leake, Gautel, Labeit, Ding, Labeit, Horwitz, Leonard, Linke: "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

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

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

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

Merck, Groenen, Voorter, de Haard-Hoekman, Horwitz, Bloemendal, de Jong: "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

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