Recombinant Human Matrix metalloproteinase-14 (MMP14)

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Code CSB-EP014661HU
MSDS
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP014661HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP14.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP014661HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP14.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
MMP14
Uniprot No.
Research Area
Cancer
Alternative Names
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
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
112-582aa
Target Protein Sequence
YAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
69.9kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

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.

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Applications : Cell culture

Review: In certain experiments, CD8+ T cells were stimulated with recombinant human MMP-14 for 48 hours.

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Target Background

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.
Gene References into Functions
  1. Melatonin disturbs SUMOylation-mediated crosstalk between c-Myc and nestin via MT1 activation and promotes the sensitivity of paclitaxel in brain cancer stem cells PMID: 29654697
  2. The results suggest that MMP-14 is involved in proliferative diabetic retinopathy angiogenesis. PMID: 29853773
  3. MMP14 down-regulated the expression of TNF-alpha to inhibit extracellular matrix and MMP14 down-regulation was found to impair the proliferation and invasion ability of cervical cancer cells. PMID: 30355924
  4. High expression of mmp14 is associated with preeclampsia. PMID: 29363569
  5. Study suggest that the downregulation of miR1505p and the overexpression of MMP14 may be deeply involved in the pathogenesis of lung squamous cell carcinoma. PMID: 29286099
  6. the expression of three cytokines for the pathogenesis of osteoarthritis (OA). which include IL-1beta, MMP14 and GRP78 was decreased by the various concentrations of icariin. These preliminary results imply that icariin might be an effective compound for the treatment of OA disease. PMID: 29292760
  7. Overexpression of MMP-14 in familial amyloidotic polyneuropathy might be associated with the inflammatory process and can also contribute to further remodeling of the ECM. PMID: 28993312
  8. MMP14 rs1042703 was associated with nominally shorter time to progression in malignant mesothelioma patients. PMID: 29138529
  9. analysis of MT1-MMP structure and proteolytic activity PMID: 27405411
  10. In squamous cell carcinoma of the cervix (SCCC), higher levels of MMP-14 expression were established in tumor cells, as evidenced by IHC (+3) and RT-PCR.Furin activity in the tumor was much higher than that in normal tissues. The expression of TIMP-2 mRNA was sufficiently obvious in both the tumor and normal tissues to the bottom of the uterine cavity. PMID: 29265076
  11. MMP-14 is regulated by a cascade of IL-6 and p53, demonstrating that the tumor microenvironment directly stimulates molecular changes in cancer cells to drive an invasive phenotype PMID: 27531896
  12. MMP-14 levels decrease in lungs from endotoxemic mice and serum from septic patients. * Mmp14 (-/-) mice show increased lung injury and mortality following endotoxemia. * Absence of Mmp14 decreases activated MMP-2 and increases S100A9 levels in lung tissue. * MMP-14 ameliorates inflammation by promoting S100A9 cleavage by activated MMP-2. PMID: 28120021
  13. miR-337-3p directly binds to the MMP-14 promoter to repress MZF1-facilitatd MMP-14 expression, thus suppressing the progression of gastric cancer PMID: 27259238
  14. CCN3 (Nov) and CCN5 (WISP2) are novel substrates of MMP14. PMID: 27471094
  15. The current data support MT1-MMP as an additional ILK substrate and show that modulation of ILK expression and activity inhibit MT1-MMP-related pro-metastatic behaviors of ovarian cancer cells. PMID: 26959113
  16. Endoplasmic reticulum (ER) glycosylation of MMP14 is required for ECM degradation and tumor growth. PMID: 29136507
  17. Authors demonstrate that CAIX associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity. PMID: 28692057
  18. developed a GNP-based, near-infrared fluorescent contrast agent that is highly specific for MMP-14 detection in breast tumor cell lines. PMID: 27526171
  19. ERO1alpha plays a crucial role in HSC proliferation via posttranslational modification of collagen and MT1-MMP PMID: 28774960
  20. MT1-MMP-expressing cells induced co-cultured non-MT1-MMP-expressing cells. PMID: 26881932
  21. The mechanism of transition from nondifferentiated to differentiated states in HepaRG cells was studied by proteomics. Two key factors (MMP-14 and OCLN) were validated by qRT-PCR and Western blot. Blockade of MMP-14 further demonstrated its important function during tumor cell migration. PMID: 27790907
  22. Data suggest that phosphorylation of Thr567 in cytoplasmic tail of MT1-MMP (MMP14) influences behavior of both individual ovarian cancer cells and multicellular aggregates; tumor cells expressing MT1-MMP-T567E phosphomimetic mutant exhibit enhanced cell migration and enhanced cell adhesion to peritoneum and other biological surfaces. PMID: 28655772
  23. MMP-14 Is a novel substrate for matriptase, which regulates the levels of MMP-14 on the cell surface. High levels of matriptase in alpha-1 antitrypsin deficiency may contribute to increased extracellular matrix degradation by alveolar macrophages both directly and through MMP-14 activation. PMID: 28362108
  24. High expression of MMP14 and CDK7 was independent prognostic factors for overall survival in patients with gastric cancer. PMID: 27562173
  25. only collagen-IV elicits the formation of proteolytically active podosomes through a mechanism involving increased Src phosphorylation, p190RhoGAP-B (also known as ARHGAP5) relocalisation and MT1-MMP (also known as MMP14) cell surface exposure at podosome sites. PMID: 27231093
  26. This study demonstrates that excessive ECM degradation mediated by high levels of MT1-MMP is not associated with cell migration and tumourigenesis, while low levels of MT1-MMP promote invasion and vascularization in vivo. PMID: 27756325
  27. DDR2 mediates collagen-induced activation of MT1-MMP in human fibroblasts PMID: 28270508
  28. results suggest that the cytoplasmic domain regulates MT1-MMP function in a manner required for cell survival, but is dispensable for cell migration PMID: 27889376
  29. MMP14 plays an important mechanistic role in NSCLC progression, by supporting cancer invasiveness, promoting collagen degradation, and releasing HB-EGF, which accelerates lung tumor progression. PMID: 28013056
  30. We conclude that ADAM12 and MMP-14 are associated with cavernous sinus invasion in pituitary adenomas, which qualifies these proteins in diagnosis and therapy. PMID: 27144841
  31. The results suggest a regulatory role of miRNA-410 in modulating levels of MMP-14 in endometrial cancer PMID: 26842619
  32. Studies demonstrate that the interaction Bst-2 and MT1-MMP, actually happens and the cytoplasmic tails, both the N-terminal domain of Bst-2 and the C-terminal domain of MT1-MMP, play crucial roles in the interaction. The interaction between Bst-2 and MT1-MMP is important in MT1-MMP regulating the tetherin activity of Bst-2 and also in Bst-2 regulating the activity of the MT1-MP/proMMP2/MMP2 pathway. PMID: 27240342
  33. The subgroup of patients with double expression of MMP-14 and CD44 had a poor prognosis despite complete debulking. Serous subtype in advanced-stage patients and CD44 expression were found to be correlated with vimentin expression, and CD44 expression was found to be significantly correlated with complete debulking PMID: 27590006
  34. Akt level was reduced in preeclamptic placentas relative to preterm control. Inhibition of PI3K/Akt resulted in significantly elevated soluble endoglin release from endothelial cells, had no effect on MMP14 mRNA expression but resulted in significantly reduced TIMP3. In contrast inhibiting PI3K/Akt in placental explants or primary trophoblast did not change soluble endoglin release. PMID: 27155335
  35. possible involvement of membrane-type 1 matrix metalloproteinase processing of erythropoietin-producing hepatocellular receptor-2in invasiveness of cutaneous cutaneous squamous cell carcinoma PMID: 27056569
  36. Findings suggest that regulation of cellular trafficking and microtubule-mediated localization of MT1-MMP by mDia1 is likely important in breast cancer invasion through the expression of cancer stem cell genes. PMID: 26893363
  37. The results suggest that MT1-MMP promotes esophageal squamous cell carcinoma invasion and metastasis. PMID: 26916665
  38. Report design of PEGylated peptide probes conjugated with (18)F-labeled BODIPY to be used as a hybrid PET/optical imaging agent and for non-invasive monitoring of MT1-MMP activity in cancers. PMID: 26578437
  39. Downregulation of miR-193a-3p promoted loss of type II collagen by directly targeting MMP14 in IDD. miR-193a-3p inhibited IDD in vitro and in vivo. miR-193a-3p may be a promising candidate for prevention of degenerative disc disease. PMID: 26620678
  40. These results suggest that KLF6 regulates MMP14 transcription and is a critical player of the gene expression network triggered during endothelial repair. PMID: 26850053
  41. In summary, clinical and cell-based experiments suggested that physical interaction between MT1-MMP and ADI1 led to suppression of hepatitis C virus infection. This inhibitory effect could be reversed by ADI1 overexpression. PMID: 26537061
  42. Matrix metalloproteinase 14 was highly expressed in uterine leiomyoma and correlated with myostatin and activin A mRNA expression. Moreover, MMP14 and myostatin mRNA expression correlated significantly and directly with the intensity of dysmenorrhea. PMID: 26138721
  43. Hic-5 appears to enhance complex formation between MT1-MMP and FAK in activated endothelial cells, which likely coordinates matrix proteolysis and cell motility. PMID: 26769900
  44. Increased MMP14 expression is associated with malignant phenotype of cervical cancer. PMID: 26825836
  45. Silencing KIF1B inhibited expression of membranal MT1-MMP in glioma cells; however, the amount of MT1-MMP in the whole cell lysate was not affected. PMID: 26576027
  46. Independent prognostic value of MMP-14 expression in ovarian cancer is limited to a role in PFS for stromal MMP-14. PMID: 27038607
  47. Data indicate that miR-337-3p directly binds the MMP-14 promoter to repress its transcription, thus suppressing the progression of NB. PMID: 26084291
  48. Results identify the tumor suppressor SPRY4 as a novel molecular effector of MT1-MMP affecting melanoma cell motility. PMID: 26392417
  49. Pressure and Temperature Effects on the Activity and Structure of the Catalytic Domain of Human MT1-MMP PMID: 26636948
  50. MiR-22 downregulation promotes GC invasion and metastasis by upregulating MMP14 and Snail, and then inducing ECM remodeling and EMT. PMID: 26610210

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Involvement in disease
Winchester syndrome (WNCHRS)
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.
Protein Families
Peptidase M10A family
Tissue Specificity
Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.
Database Links

HGNC: 7160

OMIM: 277950

KEGG: hsa:4323

STRING: 9606.ENSP00000308208

UniGene: Hs.2399

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