Replaces Prod. #: BML-P438
Fluorogenic substrate for caspase-6 (Km=30µML, Kcat/Km=168000M-1sec-1) and related cysteine proteases. Sequence is based on lamin A site of cleavage. Ex.:340-360nM, Em.:440-460nm.
Product Details
| Alternative Name: | Caspase-6 substrate (fluorogenic) |
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| Sequence: | Ac-Val-Glu-Ile-Asp-AMC (AMC=7-Amino-4-methylcoumarin) |
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| Formula: | C32H43N5O11 |
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| MW: | 673.7 |
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| CAS: | 219137-97-0 |
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| Peptide Content: | 70-90% |
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| Purity: | ≥95% (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; also soluble in phosphate buffer, pH 7.5. |
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| Shipping: | Ambient Temperature |
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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
Chemoproteomics Using Nucleotide Acyl Phosphates Reveals an ATP Binding Site at the Dimer Interface of Procaspase-6: E.S. Okerberg, et al.; Biochemistry
58, 5320 (2019),
Abstract;
Tri-arginine exosite patch of caspase-6 recruits substrates for hydrolysis: D.J. MacPherson, et al.; J. Biol. Chem.
294, 71 (2018),
Abstract;
Caspase-6 Undergoes a Distinct Helix-Strand Interconversion upon Substrate Binding: K.B. Dagbay, et al.; J. Biol. Chem.
292, 4885 (2017),
Abstract;
Full Text
Purification and catalytic properties of human caspase family members: M. Garcia-Calvo, et al.; Cell Death Differ.
6, 362 (1999),
Abstract;
A combinatorial approach defines specificities of members of the caspase family and granzyme B: N.A. Thornberry, et al.; J. Biol. Chem.
272, 17907 (1997),
Abstract;
Full Text
Activation of multiple interleukin-1β 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
Apoptosis by death factor: S. Nagata; Cell
88, 355 (1997),
Abstract;
Substrate specificities of caspase family proteases: R.V. Talanian, et al.; J. Biol. Chem.
272, 9677 (1997),
Abstract;
Full Text
Cleavage of lamin A by Mch2alpha but not CPP32: multiple interleukin 1beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis: A. Takahashi, et al.; PNAS
93, 8395 (1996),
Abstract;
The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32: S.M. Srinivasula et al.; J. Biol. Chem.
271, 27099 (1996),
Abstract;
