CRYAB Human

Crystallin Alpha B is composed of 175 amino acids and has a molecular weight of approximately 20.1 kDa . It is expressed in various tissues, including the lens of the eye, heart, skeletal muscles, and kidneys . The protein is encoded by the CRYAB gene located on chromosome 11 in humans .

The primary function of Crystallin Alpha B is to act as a molecular chaperone. It prevents the aggregation of denatured proteins under stress conditions, thereby protecting cells from damage . Additionally, it has been shown to inhibit apoptosis (programmed cell death) and contribute to the intracellular architecture . These properties make it a vital protein in maintaining cellular integrity and function.

Mutations in the CRYAB gene can lead to various diseases, including cardiomyopathies, skeletal myopathies (mainly myofibrillar myopathy), and cataracts . The protein’s chaperone activity is also affected by post-translational modifications, which can decrease its ability to prevent protein aggregation .

Recombinant Human Alpha B Crystallin is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically purified to a high degree (>95% purity) and is used in various research applications, including Western blotting (WB), functional studies (FuncS), and SDS-PAGE . The recombinant form retains the chaperone-like activity of the native protein, making it a valuable tool for studying protein aggregation and related diseases .

Recombinant Crystallin Alpha B is used in various research applications to study its role in protein aggregation, stress response, and disease mechanisms. It is also utilized in the development of therapeutic strategies for diseases associated with protein misfolding and aggregation .