Alpha B Crystallin Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC, ICC |
---|---|
Primary Accession | P02511 |
Other Accession | NP_001876.1 |
Host | Rabbit |
Reactivity | Human, Mouse, Rat, Chicken, Bovine |
Clonality | Polyclonal |
Description | Rabbit Anti-Human alpha B Crystallin Polyclonal |
Target/Specificity | Detects ~22kDa. Does not cross-react with αA-crystallin. |
Other Names | AACRYA Antibody, Alpha crystallin B chain Antibody, CRYA2 Antibody, CRYAB Antibody, CTPP2 Antibody, HSPB5 Antibody, NY REN 27 antigen Antibody |
Immunogen | Synthetic peptide corresponding to human alpha B crystallin conjugated to KLH |
Purification | Rabbit Antiserum |
Storage | -20ºC |
Storage Buffer | Rabbit Antiserum |
Shipping Temperature | Blue Ice or 4ºC |
Certificate of Analysis | A 1:5000 dilution of SPC-126 was sufficient for detection of alpha B crystallin in 20 µg of HeLa cell lysate by ECL immunoblot analysis. |
Cellular Localization | Cytoplasm | Nucleus |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
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.
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.