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Caspase-6 substrate
ALX-260-064-M001 1 mg 106.00 USD
ALX-260-064-M005 5 mg 183.00 USD
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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)
Sequence:Ac-Val-Glu-Ile-Asp-AMC (AMC=7-Amino-4-methylcoumarin)
Peptide Content:70-90%
Purity:≥95% (HPLC)
Appearance:White to off-white powder.
Solubility:Soluble in DMSO; dilute with distilled water or buffer; also soluble in phosphate buffer, pH 7.5.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Handling:Protect from light. Keep cool and dry.
Technical Info/Product Notes:AMC has an excitation maximum of 340-360nm and an emission maximum of 440-460nm.
Regulatory Status:RUO - Research Use Only

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;

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