Fluorogenic substrate cleaved by dipeptidyl peptidase IV (DPIV, DPPIV, CD26) (Km=28µM, kcat/Km=3.7 x 103M-1s-1), DPPII/VII (Km=1.12mM, kcat/Km=40.0 M-1s-1), and likely DPP8 and other prolyl peptidases. Can be used in vitro, for inhibitor screening, and in biological fluids. Ex = 380 nm, Em = 460 nm.
Product Details
| Alternative Name: | Asp-Pro-AMC |
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| Sequence: | H-Asp-Pro-AMC |
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| MW: | 387.4 |
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| Formulation: | Lyophilized. |
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| Purity: | ≥95% (HPLC) |
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| Appearance: | Off-white solid. |
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| Solubility: | Soluble in water or DMSO. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Handling: | Protect from light. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Isoaspartate residues dramatically influence substrate recognition and turnover by proteases: L. Böhme, et al.; Biol. Chem.
389, 1043 (2008),
Abstract;
Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8: H.-J. Lee, et al.; J. Biol. Chem.
281, 38653 (2006),
Abstract;
Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity: C.Y. Edosada, et al.; J. Biol. Chem.
281, 7437 (2006),
Abstract;
Full Text
Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7): M.B. Maes, et al.; Biochem. J.
386, 315 (2005),
Abstract;
Full Text
