Insulysin FRET substrate [Mca]/[Dnp]
Insulysin FRET substrate [Mca]/[Dnp] is a synthetic insulysin peptide substrate containing the FRET pair Mca and Dnp.
Catalogue number crb1100406 Molecular Weight 1422.6 Sequence (one letter code)
Sequence (three letter code)
[Mca]-Gly-Gly-Phe-Leu-Arg-Lys-His-Gly-Gln-[Dnp], Where Mca is 7-methoxycoumarin-4-acetyl and Dnp is ethylene diamine-N-2,4-dinitrophenyl
Purity >95% References
Song et al., (2003). Substrate activation of insulin-degrading enzyme (insulysin). A potential target for drug development. J Biol Chem. 278(50): 49789-94. PMID:14527953
Yfanti et al., (2013). Expression of metalloprotease insulin-degrading enzyme (insulysin) in normal and malignant human tissues. Int J Mol Med. 22(4): 421. PMID: 18813847
Manufactured in: United Kingdom
The Insulysin FRET substrate [Mca]/[Dnp] is a synthetic insulysin peptide substrate that contains an N-terminal fluorescent 7-methoxycoumarin (Mca) group and a C-terminal 2, 4-dinitrophenyl (Dnp) quencher. This FRET peptide exhibits internal fluorescence quenching when intact, however hydrolysis of the peptide between the donor/acceptor pair generates fluorescence, enabling the quantitative measure of enzymatic activity.
Insulysin, also known as insulin-degrading enzyme (IDE), is a highly conserved zinc metallopeptidase that contains an inverted zincin motif (HXXEH), characteristic of the inverzincin family of proteases. Insulysin functions as a dimer and exhibits allosteric kinetics, whereby small substrate peptides and polyphosphates such as ATP can act as enzyme activators. The endopeptidase cleaves a wide variety of substrates that are diverse in length, structure and sequence and exhibits a preference for basic or bulky hydrophobic residues.
Insulysin is ubiquitously expressed and is responsible for insulin catabolism and the degradation of many bioactive peptide substrates including glucagon, TGF-α, β-endorphin, dynorphins and atrial natriuretic peptide. Insulysin also selectively degrades amylin and β-amyloid amyloidogenic peptides at multiple sites.
Fluorescence Resonance Energy Transfer (FRET) peptides are convenient tools for the study of peptidase specificity and enzymatic activity.
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