CRYAB antibody (Crystallin, alpha B)

Details for Product anti-CRYAB Antibody No. ABIN361809, Supplier: Log in to see
Antigen
  • CRYAB
  • CMD1II
  • CRYA2
  • CTPP2
  • CTRCT16
  • HSPB5
  • MFM2
  • Crya-2
  • Crya2
  • HspB5
  • AACRYA
  • crystallin, alpha B
  • hypothetical protein
  • CRYAB
  • alpha-B-crystallin
  • Cryab
Reactivity
Cow (Bovine), Human, Pig (Porcine), Rat (Rattus)
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11
7
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4
1
Host
Mouse
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1
Clonality (Clone)
Monoclonal ()
Conjugate
This CRYAB antibody is un-conjugated
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12
9
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9
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6
6
6
5
5
5
5
5
5
5
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5
5
5
3
3
3
3
2
Application
ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
403
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135
118
78
27
19
5
3
2
1
1
Options
Supplier
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Supplier Product No.
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Immunogen Native Alpha B Crystallin
Clone 1A7-D5
Isotype IgG1
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.
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).
Gene ID 1410
NCBI Accession NP_001876
UniProt P02511
Research Area Cancer, Tyrosine Kinases
Application Notes
  • WB (1:2000)
  • ICC/IF (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

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.

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-Crystallin, alpha B (CRYAB) antibody (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 (PubMed).

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 (PubMed).

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 (PubMed).

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 (PubMed).

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 (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).

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).

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 (PubMed).

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

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).

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 (PubMed).

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).

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