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) |
|
Sequence: | Ac-Tyr-Val-Ala-Asp-pNA (pNA=p-Nitroaniline) |
|
Formula: | C29H36N6O10 |
|
MW: | 628.6 |
|
CAS: | 149231-66-3 |
|
Formulation: | Lyophilized. |
|
Peptide Content: | 75-95% |
|
Purity: | ≥97% (HPLC) |
|
Appearance: | White to off-white powder. |
|
Solubility: | Soluble in DMSO. Dilute with buffer pH 7.5. |
|
Shipping: | Ambient |
|
Long Term Storage: | -20°C |
|
Handling: | Protect from light. Keep cool and dry. |
|
Technical Info/Product Notes: | λmax of pNA is 400nm. |
|
Regulatory Status: | RUO - Research Use Only |
|
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;