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Alpha B Crystallin Antibody
Alpha B Crystallin Antibody, Clone 1A7.D5
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E, ICC |
|---|---|
| Primary Accession | P02511 |
| Other Accession | NP_001876.1 |
| Host | Mouse |
| Isotype | IgG1 |
| Reactivity | Human, Rat, Pig, Bovine |
| Clonality | Monoclonal |
| Description | Mouse Anti-Human Alpha B Crystallin Monoclonal IgG1 |
| Target/Specificity | Detects ~20kDa (Predicted mol. weight is ~21kDa). Does not cross-react with αA-crystallin, βL-crystallin, βH-crystallin, γ-crystallin, HSP25, HSP27 or HSP47 proteins. |
| Other Names | AACRYA Antibody, CRYA2 Antibody, CRYAB Antibody, CTPP2 Antibody, HSPB5 Antibody, NY Ren 27 antigen Antibody, alpha crystallin BAntibody |
| Clone Names | 1A7.D5 |
| Immunogen | Native Alpha B Crystallin |
| Purification | Protein G Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.2, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 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. |
| Cellular Localization | Cytoplasm | Nucleus |
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Provided below are standard protocols that you may find useful for product applications.
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).
References
1. Merck K.B. et al. (1993) J Biol Chem. 268: 1046-1052.
2. Horwitz J. (1992) Proc Natl Acad Sci USA. 89(21): 10449-10453.
3. Cobb B.A. and Petrash J.M. (2002) Biochemistry. 41: 483-490
4. Horwitz J. (2003) Exp Eye Res. 76: 145-153.
5. Bullard B. et al. (2004) J Biol Chem. 279: 7917-7924.
6. Gangalum R.K., Schibler M.J. and Bhat S.P. (2004) J Biol Chem. 279: 43374.43377.
7. Maddala R. and Rao V.P. (2005) Exp Cell Res. 306: 203-215.
8. Yaung J., et al. (2007) Molecular Vision 13: 566-577.
9. Head M.W. et al. (2000) Neuropathol Appl Neurobiol. 26: 304-312.
10. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.
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