BCL2L10 contains several conserved domains, including the BH4, BH1, and BH2 domains . These domains are critical for its function and interactions with other proteins in the BCL-2 family. BCL2L10 can form hetero- or homodimers with other BCL-2 family members, influencing their pro- or anti-apoptotic activities .
The primary function of BCL2L10 is to suppress apoptosis. It achieves this by preventing the release of cytochrome c from the mitochondria, a key step in the activation of caspase-3, an enzyme that plays a central role in the execution phase of cell apoptosis . By inhibiting this pathway, BCL2L10 helps in promoting cell survival.
Recombinant BCL2L10 is produced using recombinant DNA technology, where the gene encoding BCL2L10 is cloned and expressed in a suitable host, such as E. coli. The recombinant protein is then purified using chromatographic techniques . The recombinant human BCL2L10 typically consists of 195 amino acids and has a molecular mass of approximately 21.8 kDa .
Recombinant BCL2L10 is used in various research applications, including: