Bfl-1 (human, recombinant)

Bfl-1, also known as Bcl-2-related protein A1 (Bcl-2A1), is an anti-apoptotic member of the Bcl-2 family of proteins.¹ It is composed of two Bcl-2 homology (BH) domains (BH1 and BH2), which facilitate binding to Bim, Bid, PUMA, and Noxa, putative BH3 and BH4 domains, and a C-terminal region that regulates localization and function.^1,2 Bfl-1 expression can be induced by cytokines such as IL-1β and TNF-α and is primarily expressed in leukocytes, the spleen, and the lungs but is also expressed in the small intestine, testis, and thymus and localizes to the mitochondria.^3,4 However, a short splice variant, Bfl-1S, localizes to the nucleus.⁵ Bfl-1 is involved in p53-dependent apoptosis and autophagy.^2,6 Ectopic overexpression of BCL2A1 induces resistance to the Bcl-2 inhibitor venetoclax (ABT-199; Item No. 16233) in cancer cells, and Bfl-1 is overexpressed in several cancers.^7,8 Cayman’s Bfl-1 (human, recombinant) protein consists of 170 amino acids and has a calculated molecular weight of 19.7 kDa.

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1. Opfeman, J.T. Attacking cancer’s Achilles heel: Antagonism of anti-apoptotic BCL-2 family members. FEBS J. 283(14), 2661-2675 (2016).

2. Klener, P., Sovilj, D., Renesova, N., et al. BH₃ mimetics in hematologic malignancies. Int. J. Mol. Sci. 22(18), 10157 (2021).

3. Karsan, A., Yee, E., Kaushansky, K., et al. Cloning of human Bcl-2 homologue: Inflammatory cytokines induce human A₁ in cultured endothelial cells. Blood 87(8), 3089-3096 (1996).

4. Brien, G., Debaud, A.L., Robert, X., et al. C-terminal residues regulate localization and function of the antiapoptotic protein Bfl-1. The Journal of Biological Chemisty 284(44), 30257-30263 (2009).

5. Ko, J.-K., Lee, M.-J., Cho, S.-H., et al. Bfl-1S, a novel alternative splice variant of Bfl-1, localizes in the nucleus via its C-terminus and prevents cell death. Oncogene 22(16), 2457-2465 (2003).

6. Wang, G., Diepstraten, S.T., and Herold, M.J. Last but not least: BFL-1 as an emerging target for anti-cancer therapies. Biochem. Soc. Trans. 50(4), 1119-1128 (2022).

7. Lou, J., Zhou, Q., Lyu, X., et al. Discovery of a covalent inhibitor that overcame resistance to venetoclax in AML cells overexpressing BFL-1. J. Med. Chem. 67(13), 10795-10830 (2024).

8. Vogler, M. BCL2A1: The underdog in the BCL2 family. Cell Death Differ. 19(1), 67-74 (2012).