Recombinant Human Stromelysin-2 (MMP10) Protein (His)

Name: Recombinant Human Stromelysin-2 (MMP10) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02364P
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 Stromelysin-2 (MMP10) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P09238
Target Symbol	MMP10
Synonyms	Matrix metallopeptidase 10 (stromelysin 2); Matrix metalloprotease 10; Matrix metalloproteinase 10 (stromelysin 2); Matrix metalloproteinase 10; Matrix metalloproteinase-10; MMP 10; MMP-10; Mmp10; MMP10_HUMAN; SL 2; SL-2; SL2; STMY 2; STMY2; Stromelysin 2; Stromelysin II; Stromelysin-2; Stromelysin2; StromelysinII; Transin 2; Transin-2; Transin2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	FSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVPTKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLHC
Expression Range	99-476aa
Protein Length	Full Length of Mature Protein
Mol. Weight	47.0kDa
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	Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Peptidase M10A family
Database References	HGNC: 7156 OMIM: 185260 KEGG: hsa:4319 STRING: 9606.ENSP00000279441 UniGene: Hs.2258

Gene Functions References

increased abundance of Snail and Axin2 is highly correlated to malignant transformation of OL, making them novel biomarker(s) predicting oral cancer development PMID: 28939077
MMP10, either alone or in combination with tPA, might represent a new strategy for thrombolysis in ischemic stroke, providing higher protection against cerebrovascular damage. PMID: 28379489
There is a significant association in the expression of P-Rex1 and MMP10 in human luminal breast cancer, and their co-expression is indicative of poor prognosis. PMID: 27351228
MMP10 is a novel marker for cancer stem-like cells (CSCs)/cancer-initiating cells in epithelial ovarian cancer PMID: 27072580
Data show that AJUBA upregulated MMP10 and MMP13 expression in esophageal squamous cell carcinoma (ESCC). PMID: 27172796
MMP10 is overexpressed in the serum and pulmonary arteries of patients with systemic sclerosis-associated pulmonary hypertension. PMID: 28805015
Using a quantum chemical approach method, it has been established that mutations in MMP-10 and FGA proteins led to substantial energetic modifications suggesting an impact on their functions and/or stability in the recurrent pregnancy loss patients. PMID: 29016666
These results indicate that MMP10 serves a beneficial role in response to acute infection by moderating the proinflammatory response of resident and infiltrating macrophages. PMID: 27316687
Mycobacterium tuberculosis activates inflammatory and stromal cells to secrete MMP-10, and this is partly driven by the virulence factor early secretory antigenic 6. PMID: 27654284
MMP10 expression is significantly upregulated in human masticatory mucosa during wound healing. PMID: 28005267
Our results suggest that the level of the MMP-10 expression in tumor epithelium of cutaneous squamous cell carcinoma and basal cell carcinoma may contribute to the different invasive patterns observed in these tumors PMID: 27567711
these results suggest that TGF-beta1 stimulates HSC-4 cell invasion through the Slug/Wnt-5b/MMP-10 signalling axis. PMID: 26861993
the rs17435959 polymorphism of the MMP-10 gene may be associated with an increased risk of pelvic organ prolapse (POP). PMID: 26419737
According to this study, the expression of ST-2 is associated with histopathological grade and tumor differentiation in head and neck squamous cell carcinomas. PMID: 26625808
MMP-10 may be a novel biomarker reflecting both disease severity and prognosis in patients with idiopathic pulmonary fibrosis. PMID: 26415518
Noncomplicated PVVs are associated with systemic, prothrombotic activation of hemostasis and increased concentration of MMP-10, suggesting a prothrombotic and proinflammatory state. PMID: 24413984
Up-regulation of matrix metalloproteinase 10 is associated with colitis-associated cancer. PMID: 25742789
hepatocellular carcinoma cells stably expressing MMP10 had increased CXCR4 expression and migratory capacity PMID: 25808184
No association was found between MMP10 C/T rs486055 variants and anterior cruciate ligament rupture. PMID: 21410539
Suggest that MMP-10 is associated with severity and poor outcome in peripheral arterial disease. PMID: 25441671
Taken together, our findings show that MMP-10 can play a significant role in tumor growth and progression, and that MMP-10 perturbation may represent a rational strategy for cancer treatment. PMID: 24885595
YY1 suppresses invasion and metastasis of pancreatic ductal adenocarcinoma by downregulating MMP10 in a MUC4/ErbB2/p38/MEF2C-dependent mechanism. PMID: 24884523
Preliminary evidence suggests that MMP-10 may be a mediator of the number of depressive phases during bipolar disorder PMID: 24576976
Chrysin downregulates matrix metalloproteinase-10 in triple-negative breast cancer cells. PMID: 24122885
Data suggest that MMP10 promotes differentiation of myoblasts into osteoblasts by up-regulating BMP2/Smad6/Smad7 (bone morphogenetic protein 2) signaling pathway and gene expression of proteins found in bone (collagen, type I; osterix; osteocalcin). PMID: 24077220
MMP-10 is involved in the development of microvascular complications in type 1 diabetes and emerges as a potential therapeutic target for slowing down the evolution of diabetic nephropathy and retinopathy. PMID: 24078057
Marked induction of matrix metalloproteinase-10 by respiratory syncytial virus infection in human nasal epithelial cells. PMID: 24009192
rs17435959 of the MMP-10 gene is associated with carotid vulnerable plaque. PMID: 24327153
serum proMMP-10 after acute ischemic stroke is associated with TNFalpha and may have a role in brain damage and poor outcome PMID: 23742289
Small hairpin RNA silencing of proteinases overexpressed in diabetic corneas enhanced corneal epithelial and stem cell marker staining and accelerated wound healing. PMID: 24255036
COOH truncation of the hepatitis B virus X protein, plays a role in enhancing cell invasiveness and metastasis in hepatocellular carcinoma by activating MMP10 through C-Jun. PMID: 22821423
Findings suggest that MMP10 plays an important role in esophageal squamous cell carcinoma progression in the early stage, and overexpression of MMP10 in tumor tissues could be used as a potential prognostic marker in the early clinical stage of ESCC. PMID: 22121946
High MMP-10 is associated with malignant pleural effusion. PMID: 22524815
Analysis of gene expression data from human cancers reveals a strong positive correlation between tumor Mmp10 expression and metastatic behavior in many human tumor types. PMID: 22545096
Data show that TIMP-1 inhibits the MMP-10 with a K(i) of 1.1 x 10(-9) M, and TIMP-2 inhibits the MMP-10 with a K(i) of 5.8 x 10(-9) M. PMID: 22427646
Thrombin/CD40L elicited a strong synergistic effect on endothelial MMP-10 expression and microparticles containing MMP-10 in vitro and in vivo, which may represent a new link between inflammation/thrombosis with prognostic implications. PMID: 22492089
MMP-10 was capable of enhancing tissue plasminogen activator-induced fibrinolysis via a thrombin-activatable fibrinolysis inhibitor inactivation-mediated mechanism. PMID: 22104553
the roles of MMP-10 in the invasion of head and neck squamous cell carcinoma cells in vitro PMID: 21998657
Mmp10 is overexpressed in lung tumors induced by either the smoke carcinogen urethane or oncogenic Kras. PMID: 22022614
Enhanced expression of MMP-10 is associated with progression from non-dysplastic Barrett's oesophagus to adenocarcinoma. PMID: 20584750
Data demonstrate induction of MMP-10 by VEGF in HUVEC and support an angiogenic role for MMP-10 in response to VEGF stimulation in vitro and in vivo. PMID: 20432469
Results suggest that MMP-10 may be important in the initial stages of squamous cell cancer progression and induced in the stroma relating to the general host-response reaction to skin cancer. PMID: 19601983
MMP-10 and MMP-26, in particular, may associate with aggressive Merkel cell carcinoma. PMID: 19921252
The catalytic domain of human matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 angstroms resolution. PMID: 15095982
Beta-carotene suppresses UVA-induction of MMP-10. PMID: 15288123
a tightly regulated expression level of stromelysin-2 is required for limited matrix degradation at the wound site PMID: 15371548
Overexpression of MMP-10 is associated with non-small cell lung cancer PMID: 15375490
identified significant interactions between MMP10 (nt+180) polymorphisms and gender in abdominal aortic aneurysm PMID: 15944607
zinc finger protein 267 as a negative transcriptional regulator of MMP-10 might promote liver fibrogenesis PMID: 16054593
Increased levels of MMP-10 is associated with gastric cancer PMID: 16331256

FAQs

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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.