Anti-Bcl-2 (Clone: BC1)

Bcl-2 (B-cell lymphoma 2), is a member of Bcl-2 family of regulator proteins. These proteins contain a hydrophobic cleft that binds to BH3-only proteins and to the pro-apoptotic Bcl-2 family members Bad, Bak, and Bax to inhibit apoptosis. In the absence of this binding, the proapoptotic Bcl-2 members are recruited to the OMM (Outer Mitochondrial Membrane) at which they oligomerize and cause OMM permeabilization, releasing proapoptotic effectors such as SMAC or cytochrome-c. Bcl-2 also neutralize a group of 'sensor' proteins (such as BIM), which are triggered by cytotoxic stimuli such as chemotherapy. BCL-2 proteins therefore have a central role as guardians against apoptosis, helping cancer cells to evade cell death. Protein function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785). [The UniProt Consortium]