MMP 7 Human, Active

Matrix Metalloproteinase-7 Human Recombinant, Active
Cat. No.
BT8353
Source
Escherichia Coli.
Synonyms
Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.
Appearance
Sterile clear liquid solution.
Purity
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Matrix Metalloproteinase-7 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 19.13 kDa.
The MMP-7 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Matrix metalloproteinase-7 (MMP-7), alternatively known as matrilysin or PUMP (EC 3.4.24.23), plays a crucial role in the breakdown of extracellular matrix components. This enzyme exhibits catalytic activity against various substrates, including collagen types IV and X, elastin, fibronectin, gelatin, laminin, and proteoglycans. Although closely related to the stromelysin family, MMP-7 is encoded by a distinct gene. Structurally, MMP-7 is the smallest among all MMPs, comprising a pro-peptide domain and a catalytic domain, lacking the hemopexin-like domain found in other MMP members. Synthesized as a 28 kDa proenzyme, MMP-7 can be activated in vitro by organomercurials and trypsin, while in vivo activation is mediated by MMP-3, resulting in an 18 kDa active enzyme. Upon activation, MMP-7 exhibits the ability to activate pro-MMP-1 and pro-MMP-9, but not pro-MMP-2. Notably, MMP-7 demonstrates widespread expression, with elevated levels observed in cycling endometrium, colorectal cancers, adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately half of all gliomas.
Description

Recombinant Matrix Metalloproteinase-7, expressed in E. coli, is produced as a single, non-glycosylated polypeptide chain with a molecular weight of 19.13 kDa. The purification of MMP-7 is achieved through proprietary chromatographic methods.

Physical Appearance
A clear, sterile liquid solution.
Formulation
This protein solution is formulated with the following additives: 10mM HEPES (pH 7.4), 5mM CaCl2, and 150mM NaCl.
Stability
Matrilysin exhibits stability at 4°C for a period of 3 weeks. However, for long-term storage, it is recommended to store the protein below -18°C. It is crucial to avoid repeated freeze-thaw cycles.
Biological Activity

The specific activity of this product has been determined to be 9,100 U/mg.

Unit Definition
One unit of activity is defined as the amount of enzyme required to digest 1 µg of Azocoll per minute at a temperature of 37°C.
Synonyms
Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.
Source
Escherichia Coli.

Product Science Overview

Gene and Expression

MMP-7 is encoded by the MMP7 gene, which is located on human chromosome 11q21-q22 . Unlike other MMPs, MMP-7 is primarily expressed by epithelial cells . It is the smallest member of the MMP family, with a molecular weight of approximately 20 kDa .

Structure and Activation

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 an 18 kDa active enzyme . Once activated, MMP-7 can further activate other MMPs, such as pro-MMP-1 and pro-MMP-9, but not pro-MMP-2 .

Functions and Mechanisms

MMP-7 plays a vital role in the cleavage of ECM proteins such as proteoglycans, fibronectin, entactin, laminin, and various types of collagen (III, IV, V, IX, X, XI), as well as elastin . This enzyme is involved in the initial stages of tumor progression by facilitating the invasion and metastasis of cancer cells .

Clinical Significance

Overexpression of MMP-7 has been observed in various human cancers, including colorectal, breast, lung, prostate, esophageal, stomach, endometrial, and ovarian carcinomas . It is also associated with the pathogenesis of demyelinating multiple sclerosis (MS) lesions . In colorectal cancer (CRC), activated MMP-7 plays a crucial role in liver metastases .

Applications

Recombinant human MMP-7 is widely used in in silico and in vitro studies to analyze its proteolytic activity and its role in cancer cell invasion . It is typically expressed in E. coli and is available in buffered aqueous solutions for research purposes .

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MMP 7 Human
Matrix Metalloproteinase-7 Human Recombinant
Cat. No.
BT8275
Source
Escherichia Coli.
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