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company name :
R&D Systems
product type :
protein
product name :
Recombinant Human MMP-2 Protein, CF
catalog :
902-MP-010
quantity :
10 ug
price :
444 USD
more info or order :
citations: 31
Reference
Welter A, Wu W, Maurer R, O Quinn T, Chao M, Boyle D, et al. An Investigation of the Altered Textural Property in Woody Breast Myopathy Using an Integrative Omics Approach. Front Physiol. 2022;13:860868 pubmed publisher
Spiller S, Wippold T, Bellmann Sickert K, Franz S, Saalbach A, Anderegg U, et al. Protease-Triggered Release of Stabilized CXCL12 from Coated Scaffolds in an Ex Vivo Wound Model. Pharmaceutics. 2021;13: pubmed publisher
Howng B, Winter M, LePage C, Popova I, Krimm M, Vasiljeva O. Novel Ex Vivo Zymography Approach for Assessment of Protease Activity in Tissues with Activatable Antibodies. Pharmaceutics. 2021;13: pubmed publisher
Uliana F, Vizovišek M, Acquasaliente L, Ciuffa R, Fossati A, Frommelt F, et al. Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen. Nat Commun. 2021;12:1693 pubmed publisher
Kareskoski M, Vakkamäki J, Laukkanen K, Palviainen M, Johannisson A, Katila T. Matrix metalloproteinase (MMP)-2, MMP-9, semen quality and sperm longevity in fractionated stallion semen. Theriogenology. 2021;164:93-99 pubmed publisher
Amaral A, Fernandes C, Rebordão M, Szóstek Mioduchowska A, Lukasik K, Pinto Bravo P, et al. Myeloperoxidase Inhibition Decreases the Expression of Collagen and Metallopeptidase in Mare Endometria under In Vitro Conditions. Animals (Basel). 2021;11: pubmed publisher
Falkowski K, Bielecka E, Thøgersen I, Bocheńska O, Płaza K, Kalińska M, et al. Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)-A CleavEx Based Analysis. Int J Mol Sci. 2020;21: pubmed publisher
Amaral A, Fernandes C, Rebordão M, Szóstek Mioduchowska A, Lukasik K, Gawronska Kozak B, et al. The In Vitro Inhibitory Effect of Sivelestat on Elastase Induced Collagen and Metallopeptidase Expression in Equine Endometrium. Animals (Basel). 2020;10: pubmed publisher
Devel L, Almer G, Cabella C, Beau F, Bernes M, Oliva P, et al. Biodistribution of Nanostructured Lipid Carriers in Mice Atherosclerotic Model. Molecules. 2019;24: pubmed publisher
Huo D, Zhu J, Chen G, Chen Q, Zhang C, Luo X, et al. Eradication of unresectable liver metastasis through induction of tumour specific energy depletion. Nat Commun. 2019;10:3051 pubmed publisher
Ruiz Gómez G, Vogel S, Moller S, Pisabarro M, Hempel U. Glycosaminoglycans influence enzyme activity of MMP2 and MMP2/TIMP3 complex formation - Insights at cellular and molecular level. Sci Rep. 2019;9:4905 pubmed publisher
Pintus G, Giordo R, Wang Y, Zhu W, Kim S, Zhang L, et al. Reduced vasorin enhances angiotensin II signaling within the aging arterial wall. Oncotarget. 2018;9:27117-27132 pubmed publisher
Gioia M, Fasciglione G, Sbardella D, Sciandra F, Casella M, Camerini S, et al. The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site. PLoS ONE. 2018;13:e0192651 pubmed publisher
Sasidhar M, Chevooru S, Eickelberg O, Hartung H, Neuhaus O. Downregulation of monocytic differentiation via modulation of CD147 by 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors. PLoS ONE. 2017;12:e0189701 pubmed publisher
Gopcevic K, Rovcanin B, Kekic D, Milasinovic D, Kocic G, Stojanovic I. Gelatinases A and B and Antioxidant Enzyme Activity in the Early Phase of Acute Myocardial Infarction. Folia Biol (Praha). 2017;63:20-26 pubmed
Pei S, Yang X, Wang H, Zhang H, Zhou B, Zhang D, et al. Plantamajoside, a potential anti-tumor herbal medicine inhibits breast cancer growth and pulmonary metastasis by decreasing the activity of matrix metalloproteinase-9 and -2. BMC Cancer. 2015;15:965 pubmed publisher
Kløverpris S, Mikkelsen J, Pedersen J, Jepsen M, Laursen L, Petersen S, et al. Stanniocalcin-1 Potently Inhibits the Proteolytic Activity of the Metalloproteinase Pregnancy-associated Plasma Protein-A. J Biol Chem. 2015;290:21915-24 pubmed publisher
Wade R, Bassin E, Rodell C, Burdick J. Protease-degradable electrospun fibrous hydrogels. Nat Commun. 2015;6:6639 pubmed publisher
Schlomann U, Koller G, Conrad C, Ferdous T, Golfi P, Garcia A, et al. ADAM8 as a drug target in pancreatic cancer. Nat Commun. 2015;6:6175 pubmed publisher
Temma T, Hanaoka H, Yonezawa A, Kondo N, Sano K, Sakamoto T, et al. Investigation of a MMP-2 activity-dependent anchoring probe for nuclear imaging of cancer. PLoS ONE. 2014;9:e102180 pubmed publisher
Gu Z, Liu F, Tonkova E, Lee S, Tschumperlin D, Brenner M. Soft matrix is a natural stimulator for cellular invasiveness. Mol Biol Cell. 2014;25:457-69 pubmed publisher
Wang L, Cossette S, Rarick K, Gershan J, Dwinell M, Harder D, et al. Astrocytes directly influence tumor cell invasion and metastasis in vivo. PLoS ONE. 2013;8:e80933 pubmed publisher
Djokic J, Fagotto Kaufmann C, Bartels R, Nelea V, Reinhardt D. Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers. J Biol Chem. 2013;288:22821-35 pubmed publisher
Zhang Y, Mao X, Schwend T, Littlechild S, Conrad G. Resistance of corneal RFUVA–cross-linked collagens and small leucine-rich proteoglycans to degradation by matrix metalloproteinases. Invest Ophthalmol Vis Sci. 2013;54:1014-25 pubmed publisher
Devel L, Beau F, Amoura M, Vera L, Cassar Lajeunesse E, Garcia S, et al. Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins. J Biol Chem. 2012;287:26647-56 pubmed publisher
Tsuchiya S, Simmer J, Hu J, Richardson A, Yamakoshi F, Yamakoshi Y. Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp). J Bone Miner Res. 2011;26:220-8 pubmed publisher
Gonzalez R, Seurynck Servoss S, Crowley S, Brown M, Omenn G, Hayes D, et al. Development and validation of sandwich ELISA microarrays with minimal assay interference. J Proteome Res. 2008;7:2406-14 pubmed publisher
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product information
master code :
902-MP
SKU :
902-MP-010
product name :
Recombinant Human MMP-2 Protein, CF
unit size :
10 ug
description :
The Recombinant Human MMP-2 Protein, CF from R&D Systems is derived from CHO. The Recombinant Human MMP-2 Protein, CF has been validated for the following applications: Enzyme Activity.
target :
MMP-2
category :
Proteins and Enzymes
buffer :
Supplied as a 0.2 ╡m filtered solution in Tris, CaCl2, NaCl and Brij-35.
conjugate :
Unconjugated
purity :
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
species :
Human
observed molecular weight :
71 kDa, reducing conditions
theoretical molecular weight :
71 kDa
gene symbol :
MMP2
details of functionality :
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001 ). The specific activity is 1,000 pmol/min/╡g, as measured under the described conditions.
endotoxin note :
<1.0 EU per 1 ╡g of the protein by the LAL method.
accessionNumbers :
P08253
applications :
Enzyme Activity
source long :
Chinese Hamster Ovary cell line, CHO-derived human MMP-2 protein Ile34-Cys660
source short :
CHO
USD :
444 USD
alt names :
72 kDa gelatinase, CLG4, CLG4A72 kDa type IV collagenase, collagenase type IV-A, EC 3.4.24, EC 3.4.24.24, Gelatinase A, matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase), matrix metalloproteinase 2 (gelatinase A, 72kD gelatinase, 72kD type IVcollagenase), Matrix metalloproteinase-2, matrix metalloproteinase-II, MMP2, MMP-2, MMP-II, MONA, neutrophil gelatinase, TBE-1matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IVcollagenase)
storage :
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 6 months from date of receipt, -20 to -70 ░C as supplied. 3 months, -20 to -70 ░C under sterile conditions after opening.
more info or order :
company information
R&D Systems
614 McKinley Place N.E.
Minneapolis, MN 55413
info@RnDSystems.com
https://www.rndsystems.com
800 343-7475
headquarters: USA
R&D Systems develops and manufactures high-quality proteins and serves as a world leader in immunoassays. R&D Systems also produces quality antibodies, antibody arrays, stem cell and cell culture products, and cell selection and detection products, serving the life science and diagnostics industry.