Peptides

490 MMP FRET Substrate 10 - 1 mg

$238.00
Check your price
  • Cat.Number : AS-27104
  • Availability :
    In stock

Quantity

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 has an optimized sequence for MMP-7, with the cleavage occuring at the Ala-Leu bond. The substrate is used for high throughput screening of MMP-7 inhibitors. Abs/Em = 340/490 nm.

Specifications

Chemistry
Sequence one letter code
  • DABCYL-RPLALWRS-EDANS
Sequence three letter code
  • DABCYL-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser-EDANS
Molecular Formula
  • C73H100N20O13S
Molecular Mass/ Weight
  • 1497.8
Properties
Absorbance (nm)
  • 340
Emission (nm)
  • 490
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

You may also be interested in the following product(s)

IMG-EN-AS-55576-1-01.jpg

MMP-9 (Catalytic Domain), human recombinant

Cat.Number : AS-55576-1
$103.00 Excl. Tax
IMG-EN-AS-71158-01.jpg

SensoLyte® 520 Generic MMP Activity Kit Fluorimetric - 1 kit

Cat.Number : AS-71158
$504.00 Excl. Tax

References

Flow injection analysis for measurement of activity of matrix metalloproteinase-7 (MMP-7)

J Pharm Biomed Anal . 1997 Jun 01 ; 15(9-10) 1417 | DOI : https://doi.org/10.1016/S0731-7085(97)00035-6

  • M. Itoh
  • et al

Purification of Human Matrilysin Produced inEscherichia coliand Characterization Using a New Optimized Fluorogenic Peptide Substrate

Arch Biochem Biophys . 1995 Dec 01 ; 324(1) 59 | DOI : https://doi.org/10.1006/abbi.1995.9929

  • AR. Welch
  • et al