Replaces Prod. #: BML-P406
Fluorogenic substrate for caspase-1. AFC has an excitation maximum of 400nm and an emission maximum of 505nm. This product is similar to Ac-YVAD-AMC, Prod. No. ALX-260-024, but the AFC fluorophore has a greater Stokes' shift upon cleavage and the N-terminal is blocked by a benzyloxycarbonyl moiety, which increases cell permeability.
Product Details
| Alternative Name: | Caspase-1 substrate (fluorogenic) |
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| Sequence: | Z-Tyr-Val-Ala-Asp-AFC (AFC = 7-Amido-4-trifluoromethylcoumarin) |
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| Formula: | C39H40N5O11F3 |
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| MW: | 811.8 |
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| CAS: | 201608-13-1 |
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| Purity: | ≥95% (HPLC).
Single spot (TLC) |
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| Appearance: | White to off-white powder. |
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| Solubility: | Soluble in DMSO, DMF or methanol; insoluble in water. |
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| Shipping: | Ambient |
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| Long Term Storage: | -20°C |
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| Use/Stability: | DMF or DMSO stock solution highly stable at -20°C. |
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| Handling: | Protect from light. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Laquinimod decreases Bax expression and reduces caspase-6 activation in neurons: D. Ehrnhoefer, et al.; Exp. Neurol.
283A, 121 (2016),
Application(s): Western blot,
Abstract;
Activity-Based Proteomic Profiling of Deubiquitinating Enzymes in Salmonella-Infected Macrophages Leads to Identification of Putative Function of UCH-L5 in Inflammasome Regulation: E. Kummari, et al.; PLoS One
10, e0135531 (2015),
Application(s): Measurement of caspase-1,
Abstract;
Full Text
Activation of multiple interleukin-1beta converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis: L.M. Martins, et al.; J. Biol. Chem.
272, 7421 (1997),
Abstract;
Full Text
BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases: J. Xiang, et al.; PNAS
93, 14559 (1996),
Abstract;
Crystal structure of the cysteine protease interleukin-1 beta- converting enzyme: a (p20/p10)2 homodimer: N.P. Walker, et al.; Cell
78, 343 (1994),
Abstract;
Interleukin-1 beta converting enzyme: N.A. Thornberry; Meth. Enzymol.
244, 615 (1994),
Abstract;
Peptidic p-nitroanilide substrates of interleukin-1 β-converting enzyme: L.A. Reiter; Int. J. Pept. Protein Res.
43, 87 (1994),
Abstract;
Interleukin 1 beta (IL-1 beta) processing in murine macrophages requires a structurally conserved homologue of human IL-1 beta converting enzyme: S.M. Molineaux, et al.; PNAS
90, 1809 (1993),
Abstract;
A novel heterodimeric cysteine protease is required for interleukin-1 β processing in monocytes: N.A. Thornberry, et al.; Nature
356, 768 (1992),
Abstract;
Molecular cloning of the interleukin-1 beta converting enzyme: D.P. Cerretti, et al.; Science
256, 97 (1992),
Abstract;
IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha: A.D. Howard, et al.; J. Immunol.
147, 2964 (1991),
Abstract;
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