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CRYAB antibody (Crystallin, alpha B)

Details for Product anti-CRYAB Antibody No. ABIN264866, Supplier: Log in to see
Antigen
  • AACRYA
  • CMD1II
  • Crya-2
  • Crya2
  • CRYA2
  • CRYAB
  • CTPP2
  • CTRCT16
  • HspB5
  • HSPB5
  • MFM2
Reactivity
Cow (Bovine), Chicken, Human, Mouse (Murine), Rat (Rattus)
428
192
181
87
27
23
3
2
2
1
1
1
Host
Rabbit
239
179
15
1
Clonality
Polyclonal
Conjugate
This CRYAB antibody is un-conjugated
19
18
16
9
9
9
9
9
6
6
6
6
6
6
6
5
5
5
5
5
5
5
5
5
5
5
4
4
3
3
2
2
Application
Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunofluorescence (IF), Western Blotting (WB)
340
191
139
74
66
52
36
25
19
7
4
2
1
Supplier
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Immunogen Synthetic peptide corresponding to Human Alpha B Crystallin conjugated to KLH
Isotype IgG
Specificity Detects Alpha B Crystallin at ~22 kDa and does not cross-react with Apha A Crystallin.
Purification Serum
Alternative Name alpha-Crystallin B Chain (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 alphacrystallins 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).Synonyms: Alpha(B)-crystallin, CRYA2, CRYAB, Heat shock protein beta-5, HspB5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component
Gene ID 1410
NCBI Accession NP_001876
UniProt P02511
Research Area Neurology, Enzymes
Application Notes Western blot: 1/5000-1/10000 (ECL). Immunohistochemistry on Frozen Sections. Immunflourescence.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer.
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

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

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

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