BID Antibody #2002
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 15, 22 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:10 - 1:50 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
BID Antibody detects endogenous levels of both the full length (22 kDa) and cleaved large fragment (15 kDa) of human BID.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the cleavage site of human BID. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Bid is a pro-apoptotic “BH3 domain-only” member of the Bcl-2 family originally discovered to interact with both the anti-apoptotic family member Bcl-2 and the pro-apoptotic protein Bax (1). Bid is normally localized in the cytosolic fraction of cells as an inactive precursor and is cleaved at Asp60 by caspase-8 during Fas signaling, leading to translocation of the carboxyl terminal p15 fragment (tBid) to the mitochondrial outer membrane (2-4). Translocation of Bid is associated with release of cytochrome c from the mitochondria, leading to complex formation with Apaf-1 and caspase-9 and resulting in caspase-9 activation (5-7). Thus, Bid relays an apoptotic signal from the cell surface to the mitochondria triggering caspase activation (8,9).
- Wang, K. et al. (1996) Genes Dev 10, 2859-69.
- Luo, X. et al. (1998) Cell 94, 481-90.
- Li, H. et al. (1998) Cell 94, 491-501.
- Gross, A. et al. (1999) J Biol Chem 274, 1156-63.
- Li, P. et al. (1997) Cell 91, 479-89.
- Zou, H. et al. (1999) J Biol Chem 274, 11549-56.
- Saleh, A. et al. (1999) J Biol Chem 274, 17941-5.
- Yin, X.M. et al. (1999) Nature 400, 886-91.
- Korsmeyer, S.J. et al. (2000) Cell Death Differ 7, 1166-73.
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