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- Tel: 858.663.9055
- Email: info@nsjbio.com
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Alpha B crystallin (CRYAB), also known as heat shock protein beta-5 (HSPB5), is a member of the small heat shock protein family that functions as a molecular chaperone, preventing protein aggregation and maintaining cellular protein stability. Crystallin Alpha B Antibody / Molecular Chaperone Protein (clone CRYAB/4665) is optimized for studies examining CRYABâs role in protein folding and stabilization under both normal and stress conditions. CRYAB antibody, also referred to as Alpha B crystallin antibody in the literature, is widely used in research focused on proteostasis and chaperone-mediated cellular protection.
CRYAB acts by binding partially unfolded or misfolded proteins, preventing their aggregation and facilitating proper folding or degradation. This chaperone activity is essential for maintaining cellular homeostasis, particularly in environments where proteins are prone to denaturation due to stress or high metabolic demand. Unlike ATP-dependent chaperones, CRYAB functions in an ATP-independent manner, forming oligomeric complexes that interact with substrate proteins.
In addition to preventing aggregation, CRYAB interacts with cytoskeletal elements such as intermediate filaments, contributing to structural stability within the cell. These interactions are particularly important in tissues exposed to mechanical stress, where maintenance of cytoskeletal integrity is critical.
CRYAB is expressed in a wide range of tissues, including muscle, neural, and epithelial tissues, reflecting its fundamental role in protein quality control. In immunohistochemistry, it is typically observed as cytoplasmic staining consistent with its intracellular chaperone function.
Western blot analysis of CRYAB reveals a band at approximately 20 kDa, corresponding to its predicted molecular weight, supporting its detection in biochemical assays. Microarray validation confirms selective binding to CRYAB, supporting the specificity of this antibody in complex protein environments.
The mouse monoclonal clone CRYAB/4665 antibody provides reliable detection of CRYAB in research applications focused on molecular chaperone function, protein folding, and cellular proteostasis.
For a microarray-validated reference CRYAB antibody with confirmed specificity, see clone CRYAB/4657.
Optimal dilution of the Crystallin Alpha B Antibody / Molecular Chaperone Protein should be determined by the researcher.
Recombinant human full-length CRYAB protein was used as the immunogen for the Crystallin Alpha B antibody.
Aliquot the Crystallin Alpha B antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Alpha B crystallin antibody, CRYAB antibody, HSPB5 antibody, Heat shock protein beta 5 antibody, Molecular chaperone antibody
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