ProMatrilysin
ProMatrix Metalloproteinase-7 Recombinant
Cat. No.
BT9805
Source
Escherichia Coli.
Synonyms
Appearance
Sterile clear liquid solution.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(b) Analysis by SDS-PAGE.
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 (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.
Product Specs
Description
Matrix metalloproteinase-7 (MMP-7), also called matrilysin or PUMP (EC 3.4.24.23), is an enzyme that breaks down various substrates. These include collagen types IV and X, elastin, fibronectin, gelatin, laminin, and proteoglycans. MMP-7 shares similarities with the stromelysin family but originates from a different gene. As the smallest MMP, it comprises a pro-peptide domain and a catalytic domain, lacking the hemopexin-like domain found in other MMPs. MMP-7 is secreted as a 28 kDa proenzyme. Its activation to an 18 kDa active MMP-7 enzyme occurs in vitro via organomercurials and trypsin, and in vivo by MMP-3. Activated MMP-7 can activate pro-MMP-1 and pro-MMP-9, but not pro-MMP-2. MMP-7 exhibits widespread expression, with elevated levels observed in the cycling endometrium, colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately half of all gliomas.
Physical Appearance
A clear, sterile liquid solution.
Formulation
This protein solution contains the following additives: 25mM Tris-HCl (pH 7.5), 150mM NaCl, 5mM CaCl2, 0.01% Brij-35, and 0.02% NaN3.
Stability
For optimal storage:
- Keep at 4°C if the entire vial will be used within 2-4 weeks.
- For longer storage, freeze at -20°C.
- For long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended.
- Avoid repeated freezing and thawing.
Purity
Purity exceeds 95.0% as determined by:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Unit Definition
One unit is defined as the amount of enzyme that can digest 1 microgram of Azocoll per minute at a temperature of 37 degrees Celsius.
Biological Activity
The specific activity of this enzyme was determined to be 1400 international units per milligram (IU/mg).
Source
Escherichia Coli.
Product Science Overview
Structure and Activation
MMP-7 is the smallest member of the matrix metalloproteinase family. It consists of a pro-peptide domain and a catalytic domain but lacks the hemopexin-like domain that is common to other 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 form an 18 kDa active enzyme .
Substrate Specificity
Biological Functions
MMP-7 plays a significant role in:
- Tissue remodeling: By degrading extracellular matrix components, MMP-7 facilitates tissue repair and remodeling.
- Cancer progression: Elevated levels of MMP-7 have been reported in various cancers, including colorectal cancers, hepatocellular carcinomas, and gliomas .
- Activation of other MMPs: Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2 .
Expression Patterns and Tissue Distribution
Recombinant Production
Recombinant ProMatrix Metalloproteinase-7 is typically produced in Escherichia coli. The recombinant protein is often purified to a high degree, with a purity greater than 95% as determined by RP-HPLC and SDS-PAGE . The protein is formulated in a solution containing additives such as Tris-HCl, NaCl, CaCl2, Brij-35, and NaN3 to maintain its stability and activity .
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