Recombinant Human BAX Protein (Trx Tag)

BCL2 associated X (BAX) is traditionally thoμght to be regulated by anti-apoptotic BCL-2 family members. BCL-2-associated X protein (BAX) is a critical apoptotic regulator that can be transformed from a cytosolic monomer into a lethal mitochondrial oligomer, The pro-apoptotic BCL-2 protein BAX commits human cells to apoptosis by permeabilizing the outer mitochondrial membrane. BAX activation has been sμggested to require the separation of helix alpha5 from alpha6 - the 'latch' from the 'core' domain - among other conformational changes. BCL-2-associated X (BAX) protein acts as a gatekeeper in regulating mitochondria-dependent apoptosis. Under cellular stress, BAX becomes activated and transforms into a lethal oligomer that causes mitochondrial outer membrane permeabilization (MOMP) .

BCL2L4bcl2-L; Bcl-2-like protein; BCL2L; Bcl2-L; BAX; BCL2L4; apoptosis regulator BAX; Bcl2-L-4; BCL2L4bcl2-L-4; BCL2-associated X protein; Bcl-2-like protein 4; BAXA; Baxdelta2G9; Baxdelta2G9omega; Baxdelta2omega; Bax-protein; BCL2 associated X protein; BCL2 associated X protein omega; BCL2 associated X protein transcript variant delta2; Bcl-2-like protein 4 (Bcl2-L-4) ; membrane isoform alpha

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.