Replaces Prod. #: BML-P408
Sequence is a modification of pro-interleukin-1β Asp-116 cleavage site for caspase-1. Similar to Ac-YVAD-AMC but cleavage is monitored colorimetrically at 405nm.
Product Details
| Alternative Name: | Caspase-1 substrate (chromogenic) |
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| Sequence: | Ac-Tyr-Val-Ala-Asp-pNA (pNA=p-Nitroaniline) |
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| Formula: | C29H36N6O10 |
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| MW: | 628.6 |
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| CAS: | 149231-66-3 |
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| Formulation: | Lyophilized. |
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| Peptide Content: | 75-95% |
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| Purity: | ≥97% (HPLC) |
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| Appearance: | White to off-white powder. |
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| Solubility: | Soluble in DMSO. Dilute with buffer pH 7.5. |
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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: | λmax of pNA is 400nm. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Interleukin-1 β 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;
A novel heterodimeric cysteine protease is required for interleukin-1 β processing in monocytes: N.A. Thornberry, et al.; Nature
356, 768 (1992),
Abstract;
