Render Target: SSR
Render Timestamp: 2025-03-16T02:17:04.243Z
Commit: a619ae74f66dae0f27639e88da12bcf600e46428
XML generation date: 2025-03-07 13:11:59.130
Product last modified at: 2024-05-30T07:13:33.814Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

CRYAB Antibody #8851

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Inquiry Info. # 8851

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    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 22
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    CRYAB Antibody detects endogeneous levels of total CRYAB protein.

    Species Reactivity:

    Human, Mouse, Rat

    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.

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