IMG-EN-AS-27109-01.jpg
Peptides

390 MMP FRET Substrate XI - 5 mg

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  • Cat.Number : AS-27109
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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 substrate is readily hydrolyzed by MMP-8, 9 and collagenase-3 (MMP-13), Abs/Em = 325/393 nm. The hydrolysis is inhibited in a 1:1 stoichiometric fashion by the tissue inhibitors of metalloproteinases, TIMP-1, TIMP-2, and TIMP-3.

Specifications

Chemistry
Sequence one letter code
  • Mca-P-Cha-G-Nva-HA-Dap(Dnp)-NH2
Sequence three letter code
  • Mca-Pro-Cha-Gly-Nva-His-Ala-Dap(Dnp)-NH2
Molecular Formula
  • C51H65N13O15
Molecular Mass/ Weight
  • 1100.2
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

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References

Kinetic Analysis of Matrix Metalloproteinase Activity Using Fluorogenic Triple-Helical Substrates

Biochem . 2001 Apr 18 ; 40(19) 5795 | DOI : https://doi.org/10.1021/bi0101190

  • JL. Lauer-Fields
  • et al

Biochemical characterization of human collagenase-3

J Biol Chem . 1996 Jan 19 ; 271(3) 1544 | DOI : 10.1074/jbc.271.3.1544.

  • V. Knauper
  • et al

Triple-helical peptide analysis of collagenolytic protease activity

Biol Chem . 2002 Jul 08 ; 383(7-8) 1095 | DOI : 10.1515/BC.2002.118.

  • JL. Lauer-Fields
  • GB. Fields