Matrix Metalloproteinase 7, Pro Active Protein | Mmp7 active protein

Matrix Metalloproteinase 7, Pro, Recombinant (ProMMP-7, Promatrilysin)

Cat. Num. AAA636691

• Gene Names: Mmp7; MPMM
• Purity: Highly Purified; 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.
• Synonyms: Matrix Metalloproteinase 7; Pro; Recombinant (ProMMP-7; Promatrilysin); Mmp7 active protein

• Host: E Coli
• Purity/Purification: Highly Purified; 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.
• Form/Format: Supplied as a liquid in 25mM Tris-HCl, pH 7.5, 150mM sodium chloride, 5mM calcium chloride, 0.01% Brij-35, 0.02% sodium azide.

• Biological Activity: The specific activity was found to be ~1400IU/mg.
• Dimers and Aggregates: 1% as determined by silver-stained SDS-PAGE gel analysis.
• Endotoxin Level: 0.1ng/ug (IEU/ug) of Recombinant ProMMP-7
• Unit Definition: One unit is defined as the digestion of 1ug Azocoll/min at 37 degree C.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for Mmp7 active protein

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 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD 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 Categories/Family for Mmp7 active protein

Molecular Biology; MB-Matrix Metalloproteinases

NCBI and Uniprot Product Information

• NCBI GI #: 6981214
• NCBI GeneID: 25335
• NCBI Accession #: NP_036996.1
• NCBI GenBank Nucleotide #: NM_012864.2
• UniProt Accession #: P50280
• Molecular Weight: 29,885 Da
• NCBI Official Full Name: matrilysin
• NCBI Official Synonym Full Names: matrix metallopeptidase 7
• NCBI Official Symbol: Mmp7
• NCBI Official Synonym Symbols: MPMM
• NCBI Protein Information: matrilysin; MMP-7; matrin; pump-1 protease; uterine metalloproteinase; matrix metalloproteinase-7; Matrix metalloproteinase 7 (matrilysin)
• UniProt Protein Name: Matrilysin
• Protein Family: Matrilysin
• UniProt Gene Name: Mmp7
• UniProt Synonym Gene Names: Mmp-7; MMP-7
• UniProt Entry Name: MMP7_RAT

NCBI Description

enzyme that cleaves the alpha 2(I) chain of rat gelatin [RGD, Feb 2006]

Uniprot Description

Function: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase

By similarity.

Catalytic activity: Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).

Cofactor: Binds 2 calcium ions per subunit

By similarity.Binds 2 zinc ions per subunit

By similarity.

Subcellular location: Secreted › extracellular space › extracellular matrix

Probable.

Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities: Belongs to the peptidase M10A family.