Peptides

390 MMP FRET Substrate 1 - 1 mg

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  • Cat.Number : AS-27076
  • Availability :
    In stock

Size

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Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptide is a fluorogenic substrate that is best cleaved by MMP-7, 8, 9 and 13. The highly fluorescent Mca moiety is efficiently quenched by energy transfer to the Dnp group. The punctuated metallo proteinase (PUMP, EC 3.4.24.23) cleaves the substrate at the Gly-Leu bond with a 190-fold increase in fluorescence (Abs/Em = 325/393 nm). In human MMP assays, this substrate is about 50 to 100 times more sensitive than the generic MMP substrate, Dnp-PLGLWAr-NH2.


Specifications

Chemistry
Sequence one letter code
  • Mca-PLGL-Dap(Dnp)-AR-NH2
Sequence three letter code
  • Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2
CAS registry number
  • 140430-53-1
Molecular Formula
  • C49H68N14O15
Molecular Mass/ Weight
  • 1093.2
Properties
Absorbance (nm)
  • 325
Emission (nm)
  • 393
Modification
Conjugation type
  • Double dyes
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C Protected from light
Activity
Application
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • Bovine

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References

A novel coumarin‐labelled peptide for sensitive continuous assays of the matrix metalloproteinases

FEBS Lett . 1992 Jan 27 ; 296(3) 263 | DOI : https://doi.org/10.1016/0014-5793(92)80300-6

  • CG. Knight
  • et al

Continuously recording fluorescent assays optimized for five human matrix metalloproteinases

Anal Biochem . 1991 May 15 ; 195(1) 86 | DOI : https://doi.org/10.1016/0003-2697(91)90299-9

  • S. Netzel-Arnett
  • et al