MATRILYSIN Chemical Properties

storage temp. 

-70°C

form 

buffered aqueous solution

Specific Activity

5,000units/mg protein

Safety Information

Hazard Codes 

B

WGK Germany 

3

HS Code 

3504009000

MSDS

• Language:English Provider:SigmaAldrich

MATRILYSIN Usage And Synthesis

Uses

Matrix metalloproteinase-7 (MMP7) human has been used in in silico analysis of MMP-7 proteolysis of perlecan.

General Description

Matrix metalloproteinase-7 (MMP7) also referred to as matrilysin is encoded by the gene mapped to human chromosome 11q21-q22. MMP7 is a smallest member of MMP enzyme family and is highly expressed in cancer cells. MMP7 is exclusively released by epithelial cells.

Biochem/physiol Actions

Matrix metalloproteinase-7 (MMP-7) catalyzes the cleavage of extracellular matrix (ECM) proteins such as proteoglycans, fibronectin, entactin, laminin, collagen III/ IV/ V/ IX/ X/ XI, type I/ II/ IV/ V gelatins, and elastin. Matrix metalloproteinase-7 facilitates initial stages of tumor progression. Activated MMP7 plays a vital role in human colorectal cancer (CRC) liver metastases. Overexpression of MMP7 is observed in various human cancers, such as breast, lung, prostate, esophagus, stomach, endometrium, and ovarian carcinomas, as well as esophageal squamous cell carcinomas. Increased expression of MMP7 is also associated with pathogenesis of demyelinating multiple sclerosis (MS) lesions. Both in silico and in vitro studies show that MMP7 degrades glycosylated and basement membrane bound perlecan and plays a vital role in prostate cancer cell invasion.

Description

MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.
MMP7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli

Background

Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

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