BCL2 is an integral outer mitochondrial membrane protein that inhibits apoptosis by blocking the release of cytochrome c from the mitochondria. This action prevents the activation of caspases, which are the enzymes responsible for the execution of apoptosis. The protein consists of several conserved domains, including the BH1, BH2, and BH3 domains, which are essential for its anti-apoptotic function.
The recombinant form of BCL2, specifically the Human Recombinant BCL2 with a His Tag, is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. This recombinant protein contains amino acids 1-211 and has a molecular mass of approximately 25.4 kDa . The His Tag, which is a sequence of histidine residues, is fused to the N-terminus of the protein to facilitate purification using affinity chromatography techniques.
The recombinant BCL2 protein is widely used in laboratory research to study its role in apoptosis and its implications in various diseases, including cancer. By using the recombinant form, researchers can investigate the protein’s structure, function, and interactions with other molecules in a controlled environment. This helps in understanding the mechanisms underlying its anti-apoptotic activity and its potential as a therapeutic target.
The BCL2 protein solution is typically stored in a buffer containing 20 mM Tris-HCl (pH 8.0), 2 mM dithiothreitol (DTT), and 20% glycerol . For short-term storage, the solution can be kept at 4°C if it will be used within 2-4 weeks. For long-term storage, it is recommended to freeze the solution at -20°C and add a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), to prevent degradation .