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To make this Recombinant Human MMP14 protein, the MMP14 gene was isolated at first and cloned into an expression vector. CUSABIO has built a mature recombinant protein platform. This Recombinant Human MMP14 protein was developed in the platform. It was expressed in E.coli at the region of 112-582aa of the Human MMP14 protein. N-terminal 6xHis-SUMO tag was fused with the expression vector for affinity and purification purposes. The purity is 90%+ determined by SDS-PAGE. MMP14 was first described by Sato et al. as a transmembrane protein which activates pro-MMP2 to induce tumor cell invasion. Most MMPs are secreted as inactive pro-proteinases that are activated by proteolytic cleavage. Active MMP14 binds to the metallopeptidase inhibitor, tissue inhibitor of metalloproteinases 2 (TIMP2), to form a receptor for proMMP2 activation. MMP14 knockout mice exhibit defects in skeletal development and angiogenesis, fibrosis of soft tissues, and premature death. This phenotype has been attributed largely to the importance of MMP14 in collagen turnover and bone remodeling. MMP14 is up-regulated in several types of cancer, promoting angiogenesis, inflammation, cancer cell invasion, and metastasis. In genetically-modified mouse models, MMP14 overexpression induces mammary gland adenocarcinoma formation and pancreatic cancer development. Other mouse models of epithelial cancers have also identified MMP14 expression, particularly in tumor-associated cells of the TME, to be involved in cancer progression. An MMP14-deficient breast cancer mouse model showed reduced metastasis; an effect attributed to the reduced collagen I degradation by stromal fibroblasts. Yet, the MMP14 gene expression across a variety of cancer types is highest in sarcomas, with the childhood rhabdomyosarcomas and Ewing sarcoma representing intriguing exceptions, suggesting that it may be a particularly important player in sarcoma biology.
To make this Recombinant Human MMP14 protein, the MMP14 gene was isolated at first and cloned into an expression vector. CUSABIO has built a mature recombinant protein platform. This Recombinant Human MMP14 protein was developed in the platform. It was expressed in E.coli at the region of 112-582aa of the Human MMP14 protein. N-terminal 6xHis-SUMO tag was fused with the expression vector for affinity and purification purposes. The purity is 90%+ determined by SDS-PAGE. MMP14 was first described by Sato et al. as a transmembrane protein which activates pro-MMP2 to induce tumor cell invasion. Most MMPs are secreted as inactive pro-proteinases that are activated by proteolytic cleavage. Active MMP14 binds to the metallopeptidase inhibitor, tissue inhibitor of metalloproteinases 2 (TIMP2), to form a receptor for proMMP2 activation. MMP14 knockout mice exhibit defects in skeletal development and angiogenesis, fibrosis of soft tissues, and premature death. This phenotype has been attributed largely to the importance of MMP14 in collagen turnover and bone remodeling. MMP14 is up-regulated in several types of cancer, promoting angiogenesis, inflammation, cancer cell invasion, and metastasis. In genetically-modified mouse models, MMP14 overexpression induces mammary gland adenocarcinoma formation and pancreatic cancer development. Other mouse models of epithelial cancers have also identified MMP14 expression, particularly in tumor-associated cells of the TME, to be involved in cancer progression. An MMP14-deficient breast cancer mouse model showed reduced metastasis; an effect attributed to the reduced collagen I degradation by stromal fibroblasts. Yet, the MMP14 gene expression across a variety of cancer types is highest in sarcomas, with the childhood rhabdomyosarcomas and Ewing sarcoma representing intriguing exceptions, suggesting that it may be a particularly important player in sarcoma biology.
| Cat.No | ACP02763 | Target Name | MMP14 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 112-582aa | Mol Weight | 69.9kDa |
| Protein Length | Full Length of Mature Protein | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P50281 |
|---|
Uniprot Id
P50281
Target Species
Human
Target Name
MMP14
Target Full Name
Matrix metalloproteinase-14
Target Function
Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.
Target Involvement
Winchester syndrome (WNCHRS)
Target Subcellular Location
Membrane; Single-pass type I membrane protein. Melanosome. Cytoplasm. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm.
Target Protein Families
Peptidase M10A family
Target Tissue Specificity
Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.
Target Research Area
Cancer
Target Synonyms
Matrix metallopeptidase 14 (membrane inserted); Matrix metalloproteinase 14 ; Matrix metalloproteinase-14; Membrane type 1 matrix metalloproteinase ; Membrane type 1 metalloprotease; Membrane type matrix metalloproteinase 1; Membrane-type matrix metalloproteinase 1; Membrane-type-1 matrix metalloproteinase; MMP 14; MMP X1; MMP-14; MMP-X1; Mmp14; MMP14_HUMAN; MMPX1; MT MMP 1; MT-MMP 1; MT1 MMP; MT1-MMP; MT1MMP; MTMMP 1; MTMMP1
Target Background
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. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion.
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