ChemicalBook--->CAS DataBase List--->141256-52-2

141256-52-2

141256-52-2 Structure

141256-52-2 Structure
IdentificationBack Directory
[Name]

MATRILYSIN
[CAS]

141256-52-2
[Synonyms]

MMP-7
PUMP-1
RHMMP-7
MMP7 HUMAN
MATRILYSIN
HUMAN MMP-7
MATRILYSIN-1
EC 3.4.24.23
RHMMP-7, ACTIVE
Pump-1 protease
MATRILYSIN HUMAN
MMP-7 ENZYME, HUMAN
Matrilysin-1, MMP-7
Uterine metalloproteinase
MATRIX METALLOPROTEINASE-7
Human MMP7 Protein, Fc Tag
MATRIX METALLOPROTEINASE-7 HUMAN
HUMAN MATRIX METALLOPROTEINASE 7
MMP-7, HUMAN, RECOMBINANT, E COLI
MMP-7, ACTIVE, HUMAN, RECOMBINANT
PUMP-1, ACTIVE, HUMAN, RECOMBINANT
MATRILYSIN, ACTIVE, HUMAN, RECOMBINANT
Recombinant Human Matrix Metalloproteinase-7
Matrix Metalloproteinase-7 from human, Recombinant
Anti-MMP-7, C-Terminal antibody produced in rabbit
[MDL Number]

MFCD01633460
Chemical PropertiesBack Directory
[storage temp. ]

-70°C
[form ]

buffered aqueous solution
Safety DataBack Directory
[Hazard Codes ]

B
[WGK Germany ]

3
[HS Code ]

3504009000
Hazard InformationBack Directory
[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.
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