CRYAB (D6S9E) Rabbit mAb #45844

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).