MMP7 Protein Overview: Sequence, Structure, Function and Protein Interaction

MMP7 Protein Overview

MMP7 reagents

The putative metalloproteinase I (PUMP1) gene was identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. Muller et al. (1988) found that the PUMP I protein has 267 amino acids and is significantly shorter than stromelysin (e.g., 185250) or collagenase (e.g., 120353) (477 and 469 amino acids, respectively). Putative metalloproteinase I was later called matrilysin (EC 3.4.24.23) or matrix metalloproteinase-7 (MMP7). Matrix metalloproteinases are enzymes implicated in normal and pathologic tissue remodeling processes. Gaire et al. (1994) compared the structure and expression of matrilysin with those of other members of the matrix metalloproteinase family. At least 11 members of the MMP family are known (see Mignon et al., 1995 for tabulation).

MMP7 protein family

Belongs to the peptidase M10A family.

MMP7 protein name

Recommended name
Matrilysin
Short name
MMP-7
Aliases
matrilysin, PUMP-1
Alternative name
Matrin Matrix metalloproteinase-7 Pump-1 protease Uterine metalloproteinase

MMP7 Protein Sequence

Species Human MMP7 protein
Length 267
Mass (Da) 29677
Sequence Human MMP7 protein sequence
Species Mouse MMP7 protein
Length 264
Mass (Da) 29755
Sequence Mouse MMP7 protein sequence
Species Rat MMP7 protein
Length 267
Mass (Da) 29885
Sequence Rat MMP7 protein sequence

MMP7 Protein Molecular Weight & PI

Matrilysin precursor (EC 3.4.24.23) (Matrin) (Matrix metalloproteinase-7) (MMP-7) (Pump-1 protease) (Uterine metalloproteinase) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 95-267 Matrilysin.

Molecular weight (Da)

19130.47

Theoretical pI

8.77

MMP7 Protein Structure

MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR
Deposited
1995-03-22   Released:  1996-04-03
Deposition Author(s)
Browner, M.F., Smith, W.W., Castelhano, A.L.
Organism(s)
Homo sapiens
Expression System
Cricetulus griseus
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
2.3000 Å
R-Value Work
0.180
1MMP From PDB

Human MMP7 protein Secondary structure

MMP7 Protein Interaction

Recombinant MMP7 Protein Feature

MMP7 Protein, Human, Recombinant (hFc Tag)

High Purity
> 95 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method

Recombinant MMP7 protein citations

Title
DNA Enzyme-Decorated DNA Nanoladders as Enhancer for Peptide Cleavage-Based Electrochemical Biosensor
Year
2016
Author
Kou, BB;Zhang, L;Xie, H;Wang, D;Yuan, YL;Chai, YQ;Yuan, R;
Journal
ACS Appl Mater Interfaces
Title
A Peptide Cleavage-Based Ultrasensitive Electrochemical Biosensor with an Ingenious Two-Stage DNA Template for Highly Efficient DNA Exponential Amplification
Year
2017
Author
Wang, D;Chai, Y;Yuan, Y;Yuan, R;
Journal
Anal. Chem.
Title
PtNPs as Scaffolds to Regulate Interenzyme Distance for Construction of Efficient Enzyme Cascade Amplification for Ultrasensitive Electrochemical Detection of MMP-2
Year
2017
Author
Kou, B;Chai, Y;Yuan, Y;Yuan, R;
Journal
Anal. Chem.
Title
Dual-reaction triggered sensitivity amplification for ultrasensitive peptide-cleavage based electrochemical detection of matrix metalloproteinase-7
Year
2018
Author
Zheng, Y;Ma, Z;
Journal
Biosensors and Bioelectronics
Title
Amperometric Biosensor of Matrix Metalloproteinase-7 Enhanced by Pd-Functionalized Carbon Nanocomposites
Year
2018
Author
Wei, Z;Wang, H;Ma, Z;Han, H;
Journal
Nanoscale Res Lett

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