BCL2 Like 2, also known as Bcl-2-like protein 2 or BCL2L2, is a member of the Bcl-2 family of proteins. This family is known for its role in regulating apoptosis, a form of programmed cell death crucial for maintaining cellular homeostasis and development. The recombinant form of BCL2L2, tagged with a His-tag, is widely used in research to study its structure, function, and interactions.
The human BCL2L2 protein consists of 172 amino acids and has a molecular weight of approximately 20 kDa . It is expressed in an E. coli expression system and purified using affinity chromatography, which leverages the His-tag for efficient purification . The His-tag is a sequence of histidine residues added to the C-terminus of the protein, facilitating its detection and purification.
BCL2L2 plays a significant role in the regulation of apoptosis. It is an anti-apoptotic protein, meaning it helps to prevent cell death by inhibiting the activity of pro-apoptotic proteins. This function is critical in various physiological processes, including development, immune response, and tissue homeostasis. Dysregulation of BCL2L2 and other Bcl-2 family members is often associated with cancer and other diseases characterized by abnormal cell survival.
BCL2L2 exerts its anti-apoptotic effects by interacting with other proteins in the Bcl-2 family. It binds to pro-apoptotic proteins such as Bax and Bak, preventing them from inducing mitochondrial outer membrane permeabilization (MOMP), a key step in the apoptotic pathway. By inhibiting MOMP, BCL2L2 prevents the release of cytochrome c and other apoptogenic factors from the mitochondria, thereby blocking the activation of caspases and the execution of apoptosis.
The recombinant form of BCL2L2, tagged with a His-tag, is a valuable tool in research. It is used in various assays to study protein-protein interactions, apoptosis mechanisms, and the effects of potential therapeutic compounds. For example, BCL2L2 can be used in TR-FRET (time-resolved fluorescence resonance energy transfer) assays to measure its interaction with other proteins . Additionally, it is employed in structural studies to elucidate the molecular details of its function and regulation.