Recombinant Human BID Protein (Active)
SKU: PKSH031587-100
Recombinant Human BID Protein (Active)
SKU # | PKSH031587 |
Expression Host | E.coli |
Description
Synonyms | BH3-Interacting Domain Death Agonist, BID, p22 BID |
Species | Human |
Expression Host | E.coli |
Sequence | Met 1-Asp 195 |
Accession | P55957-1 |
Calculated Molecular Weight | 22 kDa |
Observed Molecular Weight | 22 kDa |
Tag | None |
Bio-activity | 1. Immobilized human BID at 10 μg/mL (100 μl/well) can bind biotinylated human BCL2L1, The EC50 of biotinylated human BCL2L1 is 7.1 ng/mL. 2. Immobilized human BID at 10 μg/mL (100 μl/well) can bind biotinylated mouse BCL2L1, The EC50 of biotinylated mouse BCL2L1 is 5. 6 ng/mL. |
Properties
Purity | > 90 % as determined by reducing SDS-PAGE. |
Endotoxin | Please contact us for more information. |
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 sterile 40mM Tris, 150mM NaCl, pH 8.0 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
Reconstitution | Please refer to the printed manual for detailed information. |
Background
The BH3 interacting domain death agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family; which contains only the BH3 domain; and is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals. Recent studies further indicate that Bid may be more than just a killer molecule; it could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint. BID is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. BID is activated by Caspase 8 in response to Fas/TNF-R1 death receptor activation. Activated BID is translocated to mitochondria and induces cytochrome c release; which in turn activates downstream caspases. BID action has been proposed to involve the mitochondrial re-location of its truncated form; tBid; to facilitate the release of apoptogenic proteins like cytochrome c.