Recombinant Human BAX Protein(Trx Tag) (PDEH100644)

For research use only.
Synonyms | 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 |
Species | Human |
Expression Host | E.coli |
Sequence | Met1-Trp158 |
Accession | Q07812 |
Calculated Molecular Weight | 37.4 kDa |
Observed Molecular Weight | 35 kDa |
Tag | N-Trx |
Bio-activity | Not validated for activity |
Purity | > 95% as determined by reducing SDS-PAGE. |
Endotoxin | < 10 EU/mg of the protein as determined by the LAL method |
Storage | 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. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol. |
Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis |
Background | 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). |
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