CRYAB Mouse

CRYAB is composed of 175 amino acids and has a molecular weight of approximately 20 kDa . It is widely expressed in various tissues and organs, including the heart, skeletal muscle, and lens of the eye . The protein can be induced by stress conditions such as heat shock, ischemia, and oxidative stress .

CRYAB functions primarily as a molecular chaperone. It binds to misfolded proteins, preventing their aggregation and assisting in their proper folding . This chaperone activity is crucial for protecting cells from stress-induced damage. Additionally, CRYAB has autokinase activity and participates in maintaining intracellular architecture .

Recombinant Mouse CRYAB is produced using Escherichia coli (E. coli) expression systems. The recombinant protein is typically purified using conventional chromatography techniques to achieve high purity levels (>95% by SDS-PAGE) . The recombinant form is often used in research to study the protein’s function and its role in various diseases.

CRYAB is implicated in several diseases, including cataracts, neurodegenerative diseases, and various cancers . Its overexpression has been observed in a wide range of cancers, suggesting a potential role as an oncogene . Additionally, CRYAB is a target for adaptive immune responses and can trigger innate immune responses .

Recombinant CRYAB is used in various research applications, including:

• Studying protein aggregation: Understanding the mechanisms of protein aggregation and developing potential therapeutic interventions.
• Disease models: Investigating the role of CRYAB in diseases such as cataracts, neurodegenerative disorders, and cancer.
• Drug development: Screening for compounds that can modulate CRYAB activity and potentially serve as therapeutic agents.