Replaces Prod. #: ALX-260-152
Colorimetric granzyme B substrate. Combinatorial and kinetic studies have found the IEPD sequence to be optimal for cleavage of a tetrapeptide substrate by recombinant granzyme B, with a Km for Ac-IEPD-pNA of 57 µM. Cleavage of the substrate by granzyme B releases pNA, which can be detected by its absorbance at 405 nm.
Product Details
Alternative Name: | Caspase-8 substrate (chromogenic), Granzyme B substrate (chromogenic) |
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Sequence: | N-acetyl-Ile-Glu-Pro-Asp-pNA (p-nitroanilide) |
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Formula: | C28H38N6O11 |
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MW: | 634.7 |
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Purity: | ≥95% |
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Appearance: | Lyophilized solid. |
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Solubility: | Soluble to at least 100mM in DMSO. |
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Shipping: | Shipped on Blue Ice |
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Long Term Storage: | -20°C |
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Use/Stability: | Stock solution in DMSO (e.g. 0.1M) is highly stable at -20°C or -70°C. |
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Handling: | Keep cool and dry. |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Reduced serpinB9-mediated caspase-1 inhibition can contribute to autoinflammatory disease: R. van der Burgh, et al.; Oncotarget
7, 19265 (2016),
Abstract;
Full Text
Approaches to design non-covalent inhibitors for human granzyme B (hGrB): M. Kim, et al.; Org. Biomol. Chem.
12, 8952 (2014),
Abstract;
Definition and redesign of the extended substrate specificity of granzyme B: J.L. Harris, et al.; J. Biol. Chem.
273, 27364 (1998),
Abstract;
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis: N.A. Thornberry, et al.; J. Biol. Chem.
272, 17907 (1997),
Abstract;