Recombinant Human Matrilysin (MMP7) Protein (GST)

Name: Recombinant Human Matrilysin (MMP7) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03668P
Price: 418.4 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Matrilysin (MMP7) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P09237
Target Symbol	MMP7
Synonyms	Matrilysin; Matrin; Matrix Metalloproteinase 7; Matrix metalloproteinase-7; MMP 7; MMP-7; MMP7; MMP7_HUMAN; MPSL1; PUMP 1; Pump 1 protease; Pump-1 protease; PUMP1; Uterine matrilysin; Uterine metalloproteinase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	YSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK
Expression Range	95-267aa
Protein Length	Full Length of Mature Protein
Mol. Weight	46.1kDa
Research Area	Developmental Biology
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	Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Peptidase M10A family
Database References	HGNC: 7174 OMIM: 178990 KEGG: hsa:4316 STRING: 9606.ENSP00000260227 UniGene: Hs.2256

Gene Functions References

CTHRC1 serves as a pro-metastatic gene that contributes to NSCLC invasion and metastasis, which are mediated by upregulated MMP7 and MMP9 expression. Targeting CTHRC1 may be beneficial for inhibiting NSCLC metastasis. PMID: 29631554
no difference in the expression of MMP-7 and TIMP-1 in the endometrium in relation to hormone levels and menstrual cycle phases were observed PMID: 30187906
MMP-7 A-181G may play an indirect role in determining personal susceptibility to Colorectal Cancer. PMID: 29695403
Results provide evidence that MMP7 expression is regulated by leptin through ERK and JNK pathways to modulate cell invasion of ovarian neoplasm. PMID: 28885729
Absence of MMP-7 Promoter Polymorphisms is associated with Lung Cancer Susceptibility. PMID: 30275186
MMP-7(-181A/G) polymorphisms associate with obesity risk and its severity. PMID: 29317790
Higher serum MMP-7 levels were independently associated with renal fibrosis and poor prognosis in IgA Nephropathy. PMID: 28922659
The results demonstrate that MMP-7 may play an important role in the defensive mechanism against the aggregation of amyloid beta (1-42), which gives rise to the pathology of Alzheimer's disease. PMID: 28871443
among HPV-positive OPSCC patients, high MMP-7 expression is related to worse 5-year DSS and increased rate of distant recurrences PMID: 29721609
MMP7 promoter genotypes only play an indirect role in determining the personal susceptibility to oral cancer in Taiwan. PMID: 29599326
S1P induces advanced tumor phenotypes of hepatocellular carcinoma via establishing an MMP-7/syndecan-1/TGF-beta1 autocrine loop PMID: 27556509
the anti-tumor activity of oleuropein against hepatocellular carcinoma could be attributed to influencing the pro-NGF/NGF balance via affecting MMP-7 activity without affecting the gene expression of NGF PMID: 29476769
These findings suggest the usefulness of combining MMP-7 with CA 125 and HE4 in the diagnosis of epithelial ovarian cancer as a new tumor marker panel. PMID: 28662671
Our findings suggest that the two MMP-7 polymorphisms A-181G and C-153T do not play a major role in determining personal susceptibility to renal cell cancer in Taiwan PMID: 28652430
results suggest that MMP-7 might be involved in the pathogenesis of H. pylori; peptic ulcer was associated with cag pathogenicity island-dependent MMP-7 upregulation PMID: 28699830
Studies have identified an unexpected tumor-suppressive role for host-derived MMP-7 in myeloma bone disease in vivo, and highlight the importance of elucidating the effect of individual MMPs in a disease-specific context. PMID: 28241871
the crosstalk between ARF and MMP7 in nucleus contributes to ECM network in tumor microenvironments in vivo, implicating a novel therapeutic target for advanced PCa treatment. PMID: 27356744
Data suggest that HAI1, a protease on the surface of colon carcinoma cells, is an MMP7 substrate; proteolysis by MMP7 releases extracellular region as soluble HAI1 (sHAI1); sHAI1 induces cancer cell aggregation; cholesterol sulfate is required for MMP-7--catalyzed generation of sHAI1. (HAI1 = hepatocyte growth factor activator inhibitor type 1; MMP7 = matrix metalloproteinase-7) PMID: 29046355
Results indicate that the matrix metallopeptidase 7 (MMP7)A-181G genotype interacts with age and gender and may serve as an early and predictive biomarker for childhood acute lymphoblastic leukemia (ALL). PMID: 29187444
SLC12A5 promoted the migration and invasion of BUC by enhancing MMP-7 expression. PMID: 28333147
Matrix Metalloproteinase-7 Promoter polymorphism is associated with breast Cancer. PMID: 28870920
Data suggest that the cytoplasmic domain of Sdc2 is involved in regulation of expression of MMP7 in colon carcinoma/adenocarcinoma cells; induction of MMP7 involves protein kinase C gamma-mediated FAK/ERK signaling. (Sdc2 = syndecan-2; MMP7 = matrix metalloproteinase-7; FAK = focal adhesion kinase 1) PMID: 28821612
We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7, MMP-10 and TIMP-1 correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10, MMP-7, TIMP-1, TIMP-2 were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively. PMID: 28510611
plasma concentrations of MMP-7, MMP-8, -9 and TIMP-1 within 96 h from the onset of acute pancreatitis symptoms are elevated in acute pancreatitis patients compared with healthy controls PMID: 27561093
ZnCo-heterobimetallic analog of cdMMP7 with Co(II) bound in the catalytic site was prepared and characterized. This study describes a well-characterized analog of MMP7 that is available for future inhibitor design efforts. PMID: 27755977
data suggest that syndecan-2 induces extracellular shedding of E-cadherin and supports the acquisition of a fibroblast-like morphology by regulating MMP-7 expression in a colon cancer cell line PMID: 27270030
There were no statistically significant differences in the distribution of MMP7 -181 A/G and MMP12 -82 A/G genotype, allele, or haplotype frequencies between IRSA patients and controls, as well as patients' primary and secondary idiopathic recurrent spontaneous abortion PMID: 27987113
No significant differences were found between MMP-7 A-181G, C-115T, and TIMP-2 G-418C polymorphism and coronary artery disease and myocardial infarction in a Turkish population. PMID: 28137415
MMP-7 is a stable neutral hydrophilic secreted protein, and it may play a vital role in the invasion and metastasis of cancer cells. PMID: 27146730
MMP-7 expression is regulated by SOX18 in prostate cancer. PMID: 27922675
Elevated levels of MMP-7 are Associated with Idiopathic Pulmonary Fibrosis. PMID: 27293304
High MMP2 expression is associated with necrosis in Pancreatic Ductal Adenocarcinoma. PMID: 27429508
Together, these data suggest that IDH2 may be a tumor suppressor in that its loss may promote malignant progression of gastric cancer via NF-kappaB-dependent increases in MMP7 activity. PMID: 26553362
Expression of MMP7 was increased in CRC tissues and cell lines, and inversely correlated with miR-143 expression in CRC tissues. Increased expression of miR-143 repressed MMP7 expression in CRC cells both in mRNA and protein levels. Increased expression of MMP7 reversed the potential influence of miR-143 on CRC cell proliferation and invasion ability. PMID: 27827523
In conclusion, individuals with -181GG genotype and G allele had no impact on susceptibility to the development of HIV-associated neurocognitive disorder and its severity. PMID: 27538541
Together, perlecan fragments in sera and MMP-7 in tissues of Prostate cancer patients are measures of invasive Prostate cancer. PMID: 26862737
The prevalence of matrix metallopeptidase 7 G allele was 40% in studied individuals. PMID: 26950446
Data suggest that, in type 2 diabetes complicated by kidney disease, up-regulation of urinary MMP7 is strongly associated with progression to end-stage renal disease/subsequent mortality; study was conducted in public hospitals in Los Angeles County. PMID: 26412030
Data suggest MMP7 (matrix metalloproteinase 7) in follicular fluid cleaves proNGF (pro-nerve growth factor) in ovarian follicle; both MMP7 and proNGF appear to be products of granulosa cells; processing of proNGF to NGF appears to regulate apoptosis. PMID: 26457789
The multivariate stepwise logistic regression identified the following biomarkers as the best gastric cancer predictors: CEA, CA72-4, pepsinogen I, Helicobacter pylori presence and MMP7 PMID: 27069188
The ELM7 assay was specific towards in vitro MMP-7 degraded elastin. PMID: 26164539
Study shows that MiR-543 inhibits translation of MMP7 through binding to the 3'-UTR of MMP7 mRNA in ovarian cancer. PLGF suppresses miR-543, which activates MMP7-mediated cancer invasion. PMID: 26402225
Protein, mRNA, and serum expression levels of MMP-7 and IL-15 in patients with osteoarthritis were all significantly increased in osteoarthritis patients compared with the control group. PMID: 26464654
Data showed that AEG1 and MMP7 levels were both significantly increased and strongly correlated in non-small cell lung cancer (NSCLC) tissues. AEG-1 promotes NSCLC cell invasiveness through MAPK-p42/p44-dependent activation of MMP7. PMID: 26418251
For the MMP7 -181 A/G polymorphism, a decreased bladder cancer risk was found (G-allele vs. A-allele. PMID: 26301605
In a Chinese population, genetic polymorphisms in MMP7 were associated with risk of coal workers pneumoconiosis. PMID: 26330178
Data show that 5-hydroxytryptamine receptor (5-HT1DR) played an important role in cell invasion via Axin1/beta-catenin/matrix metalloproteinase 7 (MMP-7) pathway. PMID: 26214021
Urinary MMP7 improves the overall diagnostic performance of urinary CXCL10 for distinguishing normal histology from subclinical and clinical inflammation/injury, but not subclinical inflammation alone. PMID: 26906940
Our data suggested a potential role of Rab11-FIP2 in tumor progression and provided novel insights into the mechanism of how Rab11-FIP2 positively regulated cell migration and invasion in CRC cells. PMID: 26792722
MMP-7 expression is highly specific, though only of moderate sensitivity, for the diagnosis of carcinoma in the differential diagnosis from both benign and malignant mesothelial cells. PMID: 26520416

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.