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. 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. Bfl-1 expression can be induced by cytokines such as IL-1beta and TNF-alpha 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. However, a short splice variant, Bfl-1S, localizes to the nucleus. Bfl-1 is involved in p53-dependent apoptosis and autophagy. Ectopic overexpression of BCL2A1 induces resistance to the Bcl-2 inhibitor venetoclax (ABT-199, Cay-16233) in cancer cells, and Bfl-1 is overexpressed in several cancers. Cayman's Bfl-1 (human, recombinant) protein consists of 170 amino acids and has a calculated molecular weight of 19.7 kDa.Synonyms: Bcl-2A1, Bcl-2-related Protein A1, Hemopoietic-specific Early Response Protein. Purity: >85% estimated by SDS-PAGE. Source: Recombinant human N-terminal His-tagged Bfl-1 expressed in E. coli. Amino Acids: 1-152. MW: 19.7 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4. UniProt Accession No: Q16548.