Human MMP2 Recombinant Protein (RPPB1956)
- SKU:
- RPPB1956
- Product Type:
- Recombinant Protein
- Species:
- Human
- Uniprot:
- P08253
- Research Area:
- Enzymes
Description
| Product Name: | Human MMP2 Recombinant Protein |
| Product Code: | RPPB1956 |
| Size: | 10µg |
| Species: | Human |
| Target: | MMP2 |
| Synonyms: | kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II. |
| Source: | Escherichia Coli |
| Physical Appearance: | Sterile Filtered colorless solution. |
| Formulation: | The MMP2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol. |
| Stability: | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. |
| Purity: | Greater than 95% as determined by SDS-PAGE. |
| Amino Acid Sequence: | MGSSHHHHHH SSGLVPRGSH MGSEFYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARAFQVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGKEY NSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NAEGQPCKFP FRFQGTSYDS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRSDGKMW CATTANYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS QDDIKGIQEL YGASPDIDLG TGPTPTLGPV TPEICKQDIV FDGIAQIRGE IFFFKDRFIW RTVTPRDKPM GPLLVATFWP ELPEKIDAVY EAPQEEKAVF FAGNEYWIYS ASTLERGYPK PLTSLGLPPD VQRVDAAFNW SKNKKTYIFA GDKFWRYNEV KKKMDPGFPK LIADAWNAIP DNLDAVVDLQ GGGHSYFFKG AYYLKLENQS LKSVKFGSIK SDWLGC |
Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).
MMP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 576 amino acids (110-660a.a) and having a molecular mass of 64.7kDa. MMP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
| UniProt Protein Function: | MMP2: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Interacts (via the C-terminal hemopexin-like domains- containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B. Aspirin appears to inhibit expression. Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. Inhibited by histatin-3 1/24 (histatin-5). Belongs to the peptidase M10A family. |
| UniProt Protein Details: | Protein type:Secreted; Motility/polarity/chemotaxis; Cell development/differentiation; Protease; Apoptosis; EC 3.4.24.24; Secreted, signal peptide Chromosomal Location of Human Ortholog: 16q12.2 Cellular Component: extracellular space; proteinaceous extracellular matrix; sarcomere; mitochondrion; extracellular region; plasma membrane; nucleus Molecular Function:protein binding; zinc ion binding; serine-type endopeptidase activity; metalloendopeptidase activity Biological Process: extracellular matrix disassembly; collagen catabolic process; axon guidance; extracellular matrix organization and biogenesis; intramembranous ossification; cellular protein metabolic process; positive regulation of innate immune response; ephrin receptor signaling pathway; response to hypoxia; angiogenesis; proteolysis; blood vessel maturation; embryo implantation Disease: Multicentric Osteolysis, Nodulosis, And Arthropathy |
| NCBI Summary: | This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. This enzyme can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. This protein is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2014] |
| UniProt Code: | P08253 |
| NCBI GenInfo Identifier: | 116856 |
| NCBI Gene ID: | 4313 |
| NCBI Accession: | P08253.2 |
| UniProt Secondary Accession: | P08253,Q9UCJ8, B2R6U1, B4DWH3, E9PE45, |
| UniProt Related Accession: | P08253 |
| Molecular Weight: | 68,831 Da |
| NCBI Full Name: | 72 kDa type IV collagenase |
| NCBI Synonym Full Names: | matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) |
| NCBI Official Symbol: | MMP2�� |
| NCBI Official Synonym Symbols: | CLG4; MONA; CLG4A; MMP-2; TBE-1; MMP-II�� |
| NCBI Protein Information: | 72 kDa type IV collagenase; gelatinase A; 72 kDa gelatinase; collagenase type IV-A; neutrophil gelatinase; matrix metalloproteinase-2; matrix metalloproteinase-II |
| UniProt Protein Name: | 72 kDa type IV collagenase |
| UniProt Synonym Protein Names: | 72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; MMP-2; TBE-1Cleaved into the following chain:PEX |
| Protein Family: | Matrix metalloproteinase |
| UniProt Gene Name: | MMP2�� |
| UniProt Entry Name: | MMP2_HUMAN |
