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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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CRYAB antibody targets Alpha-crystallin B chain, a small heat shock protein encoded by the CRYAB gene and widely expressed across many tissues. Alpha-crystallin B chain is a member of the small heat shock protein family and functions primarily as a molecular chaperone that stabilizes unfolded or stress-damaged proteins, preventing their aggregation under conditions such as oxidative stress, heat shock, and mechanical strain. CRYAB antibody is commonly used to study cellular stress responses and protein homeostasis mechanisms.
Alpha-crystallin B chain is localized predominantly in the cytoplasm, with additional presence in the nucleus and cytoskeleton depending on cell type and stress state. It is highly expressed in lens tissue, cardiac and skeletal muscle, and glial cells, where it contributes to structural stability and cellular resilience. In muscle and neural tissues, Alpha-crystallin B chain associates with intermediate filaments, including desmin and GFAP, supporting cytoskeletal integrity during mechanical or metabolic stress. CRYAB antibody detection is therefore relevant for studies examining cytoskeletal dynamics and stress-adaptive remodeling.
Functionally, Alpha-crystallin B chain acts as an ATP-independent chaperone that binds partially unfolded proteins, maintaining them in a refoldable state and limiting toxic aggregation. It participates in multiple signaling pathways related to apoptosis, inflammation, and cellular survival by interacting with key regulatory proteins. Through these interactions, Alpha-crystallin B chain helps modulate cell fate decisions during stress exposure, making CRYAB antibody reagents useful for investigating protective stress-response networks in both normal and diseased tissues.
Dysregulation of Alpha-crystallin B chain expression has been associated with a variety of pathological conditions. Elevated CRYAB expression is frequently observed in neurodegenerative disorders, myopathies, cardiomyopathies, and multiple cancer types, where it may contribute to tumor cell survival and therapy resistance. Conversely, loss-of-function mutations in CRYAB are linked to desmin-related myopathy and certain inherited cataracts. These disease associations highlight the value of recombinant CRYAB antibody tools for research into protein aggregation disorders, muscle disease, neurodegeneration, and cancer biology.
Clone rG2JF is designed to recognize Alpha-crystallin B chain in research applications. CRYAB antibody reagents are suitable for detecting protein expression and localization in tissue sections and cell-based models, supporting studies of stress adaptation, cytoskeletal stability, and disease-associated protein misfolding. CRYAB antibody use is particularly informative in contexts where cellular resistance to stress and apoptosis is under investigation.
1. Optimal dilution of the CRYAB/Alpha-crystallin B chain antibody should be determined by the researcher.
2. This CRYAB/Alpha-crystallin B chain antibody is recombinantly produced by expression in CHO cells.
A synthetic peptide hemocyanin conjugate corresponding to human alpha B crystallin amino acids 1 to 10 was used as the immunogen for the CRYAB/Alpha-crystallin B chain antibody.
CRYAB/Alpha-crystallin B chain antibody with sodium azide - store at 2 to 8oC; antibody without sodium azide - store at -20 to -80oC.
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