Bcl-2 (human, recombinant)

Bcl-2 is an anti-apoptotic protein and the founding member of the Bcl-2 family of proteins. Bcl-2 is composed of a C-terminal helix that acts as a membrane anchor and four highly conserved Bcl-2 homology (BH) domains. The BH1, BH2, and BH3 domains form a hydrophobic cleft that mediates protein-protein interactions with the pro-apoptotic proteins Bax and Bak, resulting in their inhibition, whereas the BH4 domain regulates intracellular calcium levels by interacting with the inositol-1,4,5-triphosphate receptor (IP3R) and ryanodine receptors (RyRs). Bcl-2 is highly expressed during embryogenesis and neuron and lymphocyte development and is primarily localized to the mitochondrial outer membrane. It inhibits the intrinsic apoptotic pathway by inhibiting Bax- or Bak-induced pore formation in the outer mitochondrial membrane, maintaining the mitochondrial membrane potential, and preventing the release of cytochrome c into the cytosol and the induction of apoptosis. Bcl-2 has oncogenic function, promoting tumor progression and angiogenesis, as well as metastasis. The Bcl2 t(14,18)(q32,q21) translocation results in Bcl-2 overexpression and is a hallmark of follicular lymphoma. Bcl-2 is also overexpressed in several other cancers, including chronic lymphocytic leukemia (CLL), diffuse large B cell lymphoma (DLBCL), and prostate cancer. Cayman's Bcl-2 (human, recombinant) protein can be used for binding assays. This protein consists of 221 amino acids and has a calculated molecular weight of 24.7 kDa.Synonyms: BCL2. Purity: >90% estimated by SDS-PAGE. Source: Active recombinant human C-terminal His-tagged Bcl-2 expressed in E. coli. Amino Acids: 1-211. MW: 24.7 kDa. Formulation: (Request formulation change), Lyophilized from sterile 50 mM Tris, 20% glycerol, 100 mM Arg, pH 8.5. UniProt Accession #: P10415.