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| | Cleaved Caspase-1 (Asp297) (D57A2) Rabbit mAb Chemical Properties |
| | Cleaved Caspase-1 (Asp297) (D57A2) Rabbit mAb Usage And Synthesis |
| Source | Rabbit | | Reactivity | Human | | Background | Caspase-1, or interleukin-1ß converting enzyme, 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 into their mature forms. 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. Overexpression of caspase-1 can induce apoptosis. 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. At least six caspase-1 isoforms have been identified, including caspase-1 α, β, γ, δ, ε, and ζ. Most caspase-1 isoforms 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. Activation of caspase-1 occurs through an oligomerization molecular platform designated the "inflammasome" that includes caspase-5, Pycard/Asc, and NALP1. | | References | [1] Thornberry, N.A. et al. (1992) Nature 356, 768-74.
[2] Martinon, F. and Tschopp, J. (2004) Cell 117, 561-74.
[3] Miura, M. et al. (1993) Cell 75, 653-60.
[4] Kuida, K. et al. (1995) Science 267, 2000-3.
[5] Li, P. et al. (1995) Cell 80, 401-11.
[6] Feng, Q. et al. (2004) Genomics 84, 587-91.
[7] Martinon, F. et al. (2002) Mol Cell 10, 417-26. |
| | Cleaved Caspase-1 (Asp297) (D57A2) Rabbit mAb Preparation Products And Raw materials |
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