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).
Stoccaggio: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Simbolo target: BAX
Ig target: 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
Area di ricerca:Cell Biology;Metabolism;Cancer;Kits;Lysates;Other
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