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  • 產(chǎn)品名稱：Caspase-1/ICEFluorogenicSubstrate2

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  • 產(chǎn)品廠商：KamiyaBiomedical
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Caspase-1/ICEFluorogenicSubstrate2
詳情介紹：
Purpose Fluorometer calibration: The fluorometer is calibrated using known concentrations of free AFC (Excitation = 400 nm, Emission = 505 nm) to generate a standard curve of fluorescence versus μ-moles AFC. Samples: Can be either purified or partially purified caspase preparations. Application to crude cell lysates has not been confirmed. If crude cell lysates are to be assayed, the non- specific protease background must be determined using our specific Caspase-1/ICE Inhibitor 2.
Sequence Ac-Tyr-Val-Ala-Asp-AFC, Ac-YVAD-AFC
Specificity Serves as a substrate for Caspase-1 and as a weak substrate for Caspase-4. Not cleaved by Caspases-2, -3, -6, or -7.
Background Peptide substrate labeled at the carboxy end with AFC (7-amino-4-trifluoromethyl coumarin). Designed to measure Caspase-1 or Caspase-4 activity in vitro. Interleukin-1beta Converting Enzyme (ICE), now termed Caspase-1, is a cytoplasmic cysteine protease that cleaves inactive 31 kDa pro-IL-1beta to generate the active 17.5 kDa proinflammatory cytokine IL-1beta, the predominant form of IL-1 produced by human monocytes. This cytokine has been implicated in the pathogenesis of several diseases such as rheumatoid arthritis, inflammatory bowel disease, and septic shock. Caspase-1/ICE mRNA is found in a variety of cells such as peripheral blood monocytes, peripheral blood lymphocytes, peripheral blood neutrophils, and resting and activated peripheral blood T lymphocytes. The tissue distribution of Caspase-1/ICE suggests that the enzyme may have other substrates in addition to IL-1beta. Current hypotheses suggest that Caspase-1/ICE is able to cause apoptosis as well as activate inflammation in animal cells. Experiments have shown that Caspase-1/ICE has sequence homology with other mammalian apoptosis genes and that activation of Caspase-1/ICE or other ICE-related proteases (caspases)is required for anti-Fas mAb-induced apoptosis.
Molecular Weight 720 Da
Application Notes For in vitro assays of Caspase-1 and Caspase-4 activities. Can be used with purified or partially purified enzymes, or possibly with crude cell lysates (if the Caspase-1/ICE Inhibitor 2 is included to determine background protease activity).
Restrictions For Research Use only
Storage RT
Background publications Hughes, Bortner, Purdy, Cidlowski: "Intracellular K+ suppresses the activation of apoptosis in lymphocytes." in: The Journal of biological chemistry, Vol. 272, Issue 48, pp. 30567-76, 1997 (PubMed).

Talanian, Quinlan, Trautz, Hackett, Mankovich, Banach, Ghayur, Brady, Wong: "Substrate specificities of caspase family proteases." in: The Journal of biological chemistry, Vol. 272, Issue 15, pp. 9677-82, 1997 (PubMed).

Alnemri, Fernandes-Alnemri, Litwack: "Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities." in: The Journal of biological chemistry, Vol. 270, Issue 9, pp. 4312-7, 1995 (PubMed).

Griffiths, Stam, Downs, Otterness: "ATP induces the release of IL-1 from LPS-primed cells in vivo." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 154, Issue 6, pp. 2821-8, 1995 (PubMed).

Kuida, Lippke, Ku, Harding, Livingston, Su, Flavell: "Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme." in: Science (New York, N.Y.), Vol. 267, Issue 5206, pp. 2000-3, 1995 (PubMed).

Kronheim, Mumma, Greenstreet, Glackin, Van Ness, March, Black: "Purification of interleukin-1 beta converting enzyme, the protease that cleaves the interleukin-1 beta precursor." in: Archives of biochemistry and biophysics, Vol. 296, Issue 2, pp. 698-703, 1992 (PubMed).

Buttle, Saklatvala, Tamai, Barrett: "Inhibition of interleukin 1-stimulated cartilage proteoglycan degradation by a lipophilic inactivator of cysteine endopeptidases." in: The Biochemical journal, Vol. 281 ( Pt 1), pp. 175-7, 1992 (PubMed).

Cerretti, Kozlosky, Mosley, Nelson, Van Ness, Greenstreet, March, Kronheim, Druck, Cannizzaro: "Molecular cloning of the interleukin-1 beta converting enzyme." in: Science (New York, N.Y.), Vol. 256, Issue 5053, pp. 97-100, 1992 (PubMed).

Thornberry, Bull, Calaycay, Chapman, Howard, Kostura, Miller, Molineaux, Weidner, Aunins: "A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes." in: Nature, Vol. 356, Issue 6372, pp. 768-74, 1992 (PubMed).