IMG-EN-AS-27096-01.jpg
Peptides

MMP Colorimetric Substrate - 1 mg

$156.00
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  • Cat.Number : AS-27096
  • Availability :
    In stock

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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 an exceptional MMP-2 (gelatinase A) and MMP-9 (gelatinase B) substrate: this peptide is used for the continuous spectrophotometric assay of MMP-2 and MMP-9 in combination with a color-developing thiol-reactive agent, 4,4’-dithiodipyridine or Ellman’s Reagent (as indicators). This thiol peptide-enzyme reaction has a Km of 0.004 M and a kcat of 103 s-1. Using this substrate, collagenase can be detected at concentrations as low as 2 ng/mL. HPLC and tandem mass spectrometry are also used to analyze MMP-2 and MMP-9 in conjunction with this peptide substrate.

Specifications

Chemistry
Sequence one letter code
  • Ac-PLG-SCH[CH2CH(CH3)2]-CO-LG-OC2H5
Sequence three letter code
  • Ac-Pro-Leu-Gly-SCH[CH2CH(CH3)2]-CO-Leu-Gly-OC2H5
CAS registry number
  • 98992-65-5
Molecular Formula
  • C31H53N5O8S
Molecular Mass/ Weight
  • 655.9
Properties
Absorbance (nm)
  • 412
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Application
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use

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References

Spectrophotometric assay for vertebrate collagenase

Anal Biochem . 1985 Jun 01 ; 147(2) 437 | DOI : 10.1016/0003-2697(85)90294-5

  • H. Weingarten
  • J. Feder

Synthetic substrates of vertebrate collagenase

Biochem . 1985 Nov 01 ; 24(23) 6730 | DOI : https://doi.org/10.1021/bi00344a064

  • H. Weingarten
  • et al