Recombinant Human Matrix Metalloproteinase-14 (MMP14) Protein (His-SUMO)

Name: Recombinant Human Matrix Metalloproteinase-14 (MMP14) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03636P
Price: 418.4 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) MMP14.

Collections: Enzymes, Featured enzyme molecules, Protease, Recombinant proteins

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Product Overview

Description	Recombinant Human Matrix Metalloproteinase-14 (MMP14) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P50281
Target Symbol	MMP14
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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	YAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV
Expression Range	112-582aa
Protein Length	Full Length of Mature Protein
Mol. Weight	69.9kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

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.
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
Database References	HGNC: 7160 OMIM: 277950 KEGG: hsa:4323 STRING: 9606.ENSP00000308208 UniGene: Hs.2399
Associated Diseases	Winchester syndrome (WNCHRS)
Tissue Specificity	Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.

Gene Functions References

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
The results suggest that MMP-14 is involved in proliferative diabetic retinopathy angiogenesis. PMID: 29853773
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
High expression of mmp14 is associated with preeclampsia. PMID: 29363569
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
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
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
MMP14 rs1042703 was associated with nominally shorter time to progression in malignant mesothelioma patients. PMID: 29138529
analysis of MT1-MMP structure and proteolytic activity PMID: 27405411
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
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
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
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
CCN3 (Nov) and CCN5 (WISP2) are novel substrates of MMP14. PMID: 27471094
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
Endoplasmic reticulum (ER) glycosylation of MMP14 is required for ECM degradation and tumor growth. PMID: 29136507
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
developed a GNP-based, near-infrared fluorescent contrast agent that is highly specific for MMP-14 detection in breast tumor cell lines. PMID: 27526171
ERO1alpha plays a crucial role in HSC proliferation via posttranslational modification of collagen and MT1-MMP PMID: 28774960
MT1-MMP-expressing cells induced co-cultured non-MT1-MMP-expressing cells. PMID: 26881932
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
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
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
High expression of MMP14 and CDK7 was independent prognostic factors for overall survival in patients with gastric cancer. PMID: 27562173
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
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
DDR2 mediates collagen-induced activation of MT1-MMP in human fibroblasts PMID: 28270508
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
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
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
The results suggest a regulatory role of miRNA-410 in modulating levels of MMP-14 in endometrial cancer PMID: 26842619
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
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
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
possible involvement of membrane-type 1 matrix metalloproteinase processing of erythropoietin-producing hepatocellular receptor-2in invasiveness of cutaneous cutaneous squamous cell carcinoma PMID: 27056569
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
The results suggest that MT1-MMP promotes esophageal squamous cell carcinoma invasion and metastasis. PMID: 26916665
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
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
These results suggest that KLF6 regulates MMP14 transcription and is a critical player of the gene expression network triggered during endothelial repair. PMID: 26850053
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
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
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
Increased MMP14 expression is associated with malignant phenotype of cervical cancer. PMID: 26825836
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
Independent prognostic value of MMP-14 expression in ovarian cancer is limited to a role in PFS for stromal MMP-14. PMID: 27038607
Data indicate that miR-337-3p directly binds the MMP-14 promoter to repress its transcription, thus suppressing the progression of NB. PMID: 26084291
Results identify the tumor suppressor SPRY4 as a novel molecular effector of MT1-MMP affecting melanoma cell motility. PMID: 26392417
Pressure and Temperature Effects on the Activity and Structure of the Catalytic Domain of Human MT1-MMP PMID: 26636948
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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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