Recombinant Human BID (Caspase-8-cleaved) Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 882-B8
Key Product Details
Product Specifications
Source
E. coli-derived human BID protein
Met1-Asp195, protein was purified, cleaved by Caspase-8 and further purified
Met1-Asp195, protein was purified, cleaved by Caspase-8 and further purified
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
N-terminal Sequence Analysis
Met1 (N-terminal fragment) & Gly61 (C-terminal fragment)
Predicted Molecular Mass
7 kDa (N-terminal fragment) & 15 kDa (C-terminal fragment)
SDS-PAGE
9 kDa &14 kDa, reducing conditions
Activity
Measured by its ability to induce cytochrome c release from isolated mouse liver mitochondria using the Rat/Mouse Cytochrome c Quantikine ELISA (Catalog # MCTC0) to quantify cytochrome c.
The typical EC50 for cytochrome c releasing activity is <50 nM.
The EC50 for the desired application should be determined.
Uncleaved Recombinant Human BID (Catalog # 846-BD) is available.
The typical EC50 for cytochrome c releasing activity is <50 nM.
The EC50 for the desired application should be determined.
Uncleaved Recombinant Human BID (Catalog # 846-BD) is available.
Formulation, Preparation and Storage
882-B8
| Formulation | Supplied as a 0.2 μm filtered solution in HEPES-KOH and KCl. |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: BID
BID is a 195 amino acid member of the Bcl-2 family of proteins that regulates outer mitochondrial membrane permeability (1). BID is a pro‑apoptotic member that causes cytochrome c to be released from the mitochondria intermembrane space into the cytosol. In healthy cells BID is cytosolic. In response to Fas ligand or TNF, BID is cleaved by caspase-8 and it then relocates to the mitochondria outer membrane (2, 3). Cleavage of BID by caspase-8 generates a new N-terminus that contains a terminal glycine. It appears that the glycine is myristoylated and myristoylation serves to target BID to the mitochondria (4). BID may then interact with another pro‑apoptotic Bcl-2 family member Bak (5). Interaction of BID with Bak causes altered mitochondrial membrane permeability. A 9-13 amino acid stretch called the BH3 region (Bcl-2 homology region) appears to mediate the BID interaction with other Bcl-2 family members. BID is neutralized by binding to the anti-apoptotic member Bcl‑xL.
References
- Gross, A. et al. (1999) Genes and Develop. 13:1899.
- Luo, X. et al. (1998) Cell 94:481.
- Li, H. et al. (1998) Cell 94:491.
- Zha, J. et al. (2000) Science 290:1761.
- Wei, M.C. et al. (2000) Genes Dev. 14:2060.
Long Name
BH3 Interacting Domain Death Agonist
Alternate Names
apoptic death agonist, BH3 interacting domain death agonist, BH3-interacting domain death agonist, BID isoform ES(1b), BID isoform L(2), BID isoform Si6, desmocollin type 4, FP497, Human BID coding sequence, MGC15319, MGC42355, p22 BID, tbid
Gene Symbol
BID
UniProt
Additional BID Products
Product Documents for Recombinant Human BID (Caspase-8-cleaved) Protein, CF
Product Specific Notices for Recombinant Human BID (Caspase-8-cleaved) Protein, CF
For research use only
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