Cleaved Caspase-1 (Asp297) (D57A2) Rabbit mAb #4199
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 20, 22 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Protocol
Specificity / Sensitivity
Cleaved Caspase-1 (Asp297) (D57A2) Rabbit mAb detects endogenous levels of the p20 subunit of human caspase-1 only upon cleavage at Asp297.
Species Reactivity:
Human
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues adjacent to Asp297 of human caspase-1.
Background
Caspase-1, or interleukin-1ß converting enzyme (ICE/ICEα), is a class I cysteine protease, which also includes caspases -4, -5, -11, and -12. Caspase-1 cleaves inflammatory cytokines such as pro-IL-1ß and interferon-γ inducing factor (IL-18) into their mature forms (1,2). Like other caspases, caspase-1 is proteolytically activated from a proenzyme to produce a tetramer of its two active subunits, p20 and p10. Caspase-1 has a large amino-terminal pro-domain that contains a caspase recruitment domain (CARD). Overexpression of caspase-1 can induce apoptosis (3). Mice deficient in caspase-1, however, have no overt defects in apoptosis but do have defects in the maturation of pro-IL-1β and are resistant to endotoxic shock (4,5). At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε, and ζ (6). Most caspase-1 isoforms (α, β, γ, and δ) produce products between 30-48 kDa and induce apoptosis upon overexpression. Caspase-1 ε typically contains only the p10 subunit, does not induce apoptosis, and may act as a dominant negative. The widely expressed ζ isoform of caspase-1 induces apoptosis and lacks 39 amino-terminal residues found in the α isoform (6). Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1 (7).
- Thornberry, N.A. et al. (1992) Nature 356, 768-74.
- Martinon, F. and Tschopp, J. (2004) Cell 117, 561-74.
- Miura, M. et al. (1993) Cell 75, 653-60.
- Kuida, K. et al. (1995) Science 267, 2000-3.
- Li, P. et al. (1995) Cell 80, 401-11.
- Feng, Q. et al. (2004) Genomics 84, 587-91.
- Martinon, F. et al. (2002) Mol Cell 10, 417-26.
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