Replaces Prod. #: BML-P401
Fluorogenic caspase-1 substrate with a Km=14µM. Ex.:340-360nm, Em.:440-460nm.Sequence is based on precursor interleukin-1β Asp116 cleavage site for caspase-1.
Product Details
| Alternative Name: | Caspase-1 substrate (fluorogenic) |
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| Sequence: | Ac-Tyr-Val-Ala-Asp-AMC (AMC = 7-Amino-4-methylcoumarin) |
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| Formula: | C33H39N5O10 |
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| MW: | 665.7 |
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| Peptide Content: | 75-95% |
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| Purity: | ≥98% (HPLC) |
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| Appearance: | White to off-white powder. |
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| Solubility: | Soluble in DMSO. Dilute with distilled water or buffer, pH 7.0-7.5 (e. g. TRIS, HEPES). |
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| Shipping: | Ambient |
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| Long Term Storage: | -20°C |
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| Handling: | Protect from light. Keep cool and dry. |
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| Technical Info/Product Notes: | AMC has an excitation maximum of 340-360nm and an emission maximum of 440-460nm. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Cardioprotective Effects of Oroxylum indicum Extract Against Doxorubicin and Cyclophosphamide-Induced Cardiotoxicity: S.R. Pondugula, et al.; Cardiovasc. Toxicol.
22, 67 (2022),
Abstract;
β-hydroxybutyric acid attenuates oxidative stress and improves markers of mitochondrial function in the HT-22 hippocampal cell line: M. Majrashi, et al.; J. Integr. Neurosci.
20, 321 (2021),
Abstract;
Clearance of intracellular Klebsiella pneumoniae infection using gentamicin-loaded nanoparticles: L. Jiang, et al.; J. Control Release
279, 316 (2018),
Abstract;
Design and application of a fluorogenic assay for monitoring inflammatory caspase activity: R. Ranganathan, et al.; Anal. Biochem.
543, 1 (2017),
Abstract;
Reperfusion therapy with recombinant human relaxin-2 (Serelaxin) attenuates myocardial infarct size and NLRP3 inflammasome following ischemia/reperfusion injury via eNOS-dependent mechanism: J.V. Raleigh, et al.; Cardiovasc Res
113, 609 (2017),
Application(s): Caspase-1 activity in mouse heart homogenates,
Abstract;
Temporal Changes in Caspase-1 and Caspase-8 Activities Following Brain Hypoxia With and Without Src kinase Inhibition in a Piglet Animal Model: D. Angelis, et al.; Neurochem. Res.
40, 2270 (2015),
Abstract;
Crystal structure of the cysteine protease interleukin-1 β-converting enzyme: a (p20/p10)2 homodimer: N.P.C. Walker, et al.; Cell
78, 343 (1994),
Abstract;
Interleukin-1 β converting enzyme: N.A. Thornberry; Meth. Enzymol.
244, 615 (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;
