Cell Signaling Technology

Product Pathways - Protein Folding

CRYAB Antibody #8851

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Endogenous 22 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

CRYAB Antibody detects endogeneous levels of total CRYAB protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu165 of human CRYAB protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from SNB75 cells or human, mouse, and rat heart tissue using CRYAB Antibody.

Background

CRYAB (αB-Crystallin) is a member of the small heat shock protein (sHSP also known as HSP20) family (1). This protein was initially found to be overexpressed in the eye lens, and later also detected at high levels in heart and skeletal muscle tissues (2,3). CRYAB functions mainly as a molecular chaperone, responding to stress by binding unfolded target proteins to prevent aggregation (4,5). Research studies have shown that elevated expression of CRYAB in neurological disease and stroke patients protects tissue and cells from damage under extreme stress, leading to the investigation of CRYAB as a potential therapeutic target (6-9). Researchers also found that expression of the missense mutation of CRYAB (R120G) in the mouse model causes cardiomyopathy due to abnormal desmin aggregation (10). At the molecular level, CRYAB is involved in multiple biological processes, such as inhibiting apoptosis by binding and inhibiting caspase and proapoptotic Bax and Bcl-xS protein functions (11,12), promoting angiogenesis by binding and stabilizing VEGF for secretion (13), and regulating cytoskeletal organization through association with actin filament, intermediate filament, and cardiac titin (14-16).

  1. Mehlen, P. et al. (1996) EMBO J 15, 2695-706.
  2. Piatigorsky, J. (1989) FASEB J 3, 1933-40.
  3. Bennardini, F. et al. (1992) Circ Res 71, 288-94.
  4. Benjamin, I.J. and McMillan, D.R. (1998) Circ Res 83, 117-32.
  5. Horwitz, J. (1992) Proc Natl Acad Sci U S A 89, 10449-53.
  6. Ousman, S.S. et al. (2007) Nature 448, 474-9.
  7. Ray, P.S. et al. (2001) FASEB J 15, 393-402.
  8. Arac, A. et al. (2011) Proc Natl Acad Sci U S A 108, 13287-92.
  9. Sanbe, A. (2011) Biol Pharm Bull 34, 1653-8.
  10. Wang, X. et al. (2001) Circ Res 89, 84-91.
  11. Kamradt, M.C. et al. (2001) J Biol Chem 276, 16059-63.
  12. Mao, Y.W. et al. (2004) Cell Death Differ 11, 512-26.
  13. Kase, S. et al. (2010) Blood 115, 3398-406.
  14. Wang, K. and Spector, A. (1996) Eur J Biochem 242, 56-66.
  15. Nicholl, I.D. and Quinlan, R.A. (1994) EMBO J 13, 945-53.
  16. Zhu, Y. et al. (2009) J Biol Chem 284, 13914-23.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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