Recombinant Human MMP-2 Protein, CF | R&D Systems 902-MP product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

R&D Systems

product type :

protein

product name :

Recombinant Human MMP-2 Protein, CF

catalog :

902-MP

quantity :

10 ug

price :

369 USD

citations: 24

Reference
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 Î±-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
KlÃ¸verpris 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
Zhao Z, McCloud B, Fleming R, Klempner M. Borrelia burgdorferi-induced monocyte chemoattractant protein-1 production in vivo and in vitro. Biochem Biophys Res Commun. 2007;358:528-33 pubmed
Borrelli V, di Marzo L, Sapienza P, Colasanti M, Moroni E, Cavallaro A. Role of platelet-derived growth factor and transforming growth factor beta1 the in the regulation of metalloproteinase expressions. Surgery. 2006;140:454-63 pubmed
Zhou B, Peyton M, He B, Liu C, Girard L, Caudler E, et al. Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell. 2006;10:39-50 pubmed
Haug C, Lenz C, Diaz F, Bachem M. Oxidized low-density lipoproteins stimulate extracellular matrix metalloproteinase Inducer (EMMPRIN) release by coronary smooth muscle cells. Arterioscler Thromb Vasc Biol. 2004;24:1823-9 pubmed

product information

brand :

R&D Systems

master code :

902-MP

SKU :

902-MP-010

product name :

Recombinant Human MMP-2 Protein, CF

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

unit size :

10 ug

buffer :

Supplied as a 0.2 µm 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/µg, as measured under the described conditions.

endotoxin note :

<1.0 EU per 1 µg of the protein by the LAL method.

catalog number base :

902-MP

accessionNumbers :

P08253

applications :

Enzyme Activity

source :

Chinese Hamster Ovary cell line, CHO-derived human MMP-2 protein Ile34-Cys660

2020 USD :

369

2021 USD :

369 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.