MMP3 recombinant protein

Recombinant Human MMP3 protein

Cat. Num. AAA1561104

• Gene Names: MMP3; SL-1; STMY; STR1; CHDS6; MMP-3; STMY1
• Purity: >90% as determined by SDS-PAGE
• Synonyms: MMP3; Recombinant Human MMP3 protein; Stromelysin-1; SL-1; Matrix metalloproteinase-3; MMP-3; Transin-1; MMP3 recombinant protein

• Host: E Coli
• Purity/Purification: >90% as determined by SDS-PAGE
• Form/Format: Lyophilized. Lyophilized from PBS pH 7.4, 0.2% NLS, 5% Trehalose, 5% Mannose, 1mM EDTA.

• Species: Homo sapiens (Human)
• Protein Construction: A DNA sequence encoding the human MMP3 (Phe100-Cys477) was fused with His tag
• Reconstitution: Reconstitute in sterile water for a stock solution.
• Preparation and Storage: Store at 2 to 8 degree C for one week. Store at -20 to -80 degree C for twelve months from the date of receipt. Use a manual defrost freezer and avoid repeated freeze thaw cycles.; In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.

SDS-Page

Related Product Information for MMP3 recombinant protein

Matrix metallopeptidase 3 (abbreviated as MMP3) is also known as stromelysin 1 and progelatinase. MMP3 is a member of the matrix metalloproteinase (MMP) family whose members are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, tissue remodeling, and disease processes including arthritis and metastasis. As a secreted zinc-dependent endopeptidase, MMP3 exerts its functions mainly in extracellular matrix. This protein is activated by two major endogenous inhibitors: alpha2-macroglobulin and tissue inhibitors of metalloproteases (TIMPs). MMP3 plays a central role in degrading collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP3 can also active other MMPs such as MMP1, MMP7, and MMP9, rendering MMP3 crucial in connective tissue remodeling. Dysregulatoin of MMPs has been implicated in many diseases including arthritis, chronic ulcers, encephalomyelitis and cancer. Synthetic or natural inhibitors of MMPs result in inhibition of metastasis, while up-regulation of MMPs led to enhanced cancer cell invasion.

Product Categories/Family for MMP3 recombinant protein

Protein

NCBI and Uniprot Product Information

• NCBI GI #: 4505217
• NCBI GeneID: 4314
• NCBI Accession #: NP_002413.1
• NCBI GenBank Nucleotide #: NM_002422.3
• UniProt Accession #: P08254; Q3B7S0; Q6GRF8; B2R8B8
• Molecular Weight: 53,977 Da
• NCBI Official Full Name: stromelysin-1 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 3 (stromelysin 1, progelatinase)
• NCBI Official Symbol: MMP3
• NCBI Official Synonym Symbols: SL-1; STMY; STR1; CHDS6; MMP-3; STMY1
• NCBI Protein Information: stromelysin-1; transin-1; proteoglycanase; matrix metalloproteinase-3; matrix metalloproteinase 3 (stromelysin 1, progelatinase)
• UniProt Protein Name: Stromelysin-1
• Protein Family: Stromelysin
• UniProt Gene Name: MMP3
• UniProt Synonym Gene Names: STMY1; SL-1; MMP-3
• UniProt Entry Name: MMP3_HUMAN

NCBI Description

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

Catalytic activity: Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

Cofactor: Binds 4 calcium ions per subunit.Binds 2 zinc ions per subunit.

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. Ref.13

Involvement in disease: Coronary heart disease 6 (CHDS6) [MIM:614466]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries.Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions. Ref.11 Ref.12

Sequence similarities: Belongs to the peptidase M10A family.Contains 4 hemopexin-like domains.