BMF Human

Bcl2 Modifying Factor, Isoform 3, is a human recombinant protein produced in Escherichia coli (E. coli). It is a single, non-glycosylated polypeptide chain consisting of 144 amino acids, with a molecular mass of approximately 15.6 kDa . The recombinant protein is fused to a 15 amino acid His Tag at the N-terminus, which facilitates its purification through proprietary chromatographic techniques .

BMF contains a single Bcl2 homology domain 3 (BH3), which is essential for its interaction with other Bcl2 family proteins. The BH3 domain allows BMF to bind to anti-apoptotic Bcl2 proteins, thereby promoting apoptosis . This interaction is critical for the regulation of cell death processes in response to various stimuli.

As an apoptotic activator, BMF plays a significant role in the intrinsic pathway of apoptosis. It supports the pro-apoptotic protein Bim in regulating cell death processes. BMF and Bim work synergistically in an apoptotic pathway that leads to the clearance of infected cells, such as those infected by Neisseria gonorrhoeae .

BMF is particularly important in cancer research due to its role in apoptosis. Histone deacetylase (HDAC) inhibitors, which are used in cancer therapy, can alter the balance between acetylation and deacetylation, significantly increasing histone acetylation and strongly inducing apoptosis in various cancer cell types . BMF is a key player in this process, making it a valuable target for therapeutic interventions.

The recombinant BMF protein is stable at 4°C for up to four weeks. For long-term storage, it is recommended to store the protein desiccated below -18°C, with the addition of a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) to prevent freeze-thaw cycles .