Mmp 2

Manufactured by Merck Group

Sourced in United States, United Kingdom, Canada, Germany

MMP-2 is a laboratory product manufactured by Merck Group. It is a recombinant human Matrix Metalloproteinase-2 (MMP-2) protein. MMP-2 is an enzyme that belongs to the matrix metalloproteinase family and plays a role in the degradation of the extracellular matrix.

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Lab products found in correlation

Mmp 9, by Merck Group (28 mentions) Mmp 13, by Merck Group (6 mentions) β actin, by Merck Group (6 mentions) Mmp 8, by Merck Group (5 mentions) Mmp 3, by Merck Group (4 mentions) Gapdh, by Merck Group (3 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (3 mentions) Igf 1, by Merck Group (2 mentions) Bovine serum albumin (bsa), by Merck Group (2 mentions) P akt, by Cell Signaling Technology (2 mentions) Interleukin 6 (il 6), by Merck Group (2 mentions) Mmp 1, by Merck Group (2 mentions) Adam10, by R&D Systems (2 mentions) P aminophenylmercuric acetate, by Merck Group (2 mentions) Mmp 2, by R&D Systems (2 mentions) Mmp 2, by Thermo Fisher Scientific (2 mentions) Vimentin, by Merck Group (2 mentions) Gradient sds page gel, by Bio-Rad (2 mentions) Scion image software, by Techcomp Instruments (2 mentions) Mmp 9, by Abcam (2 mentions)

Close spelling variants of this product

Human MMP-2 (2 citations) Anti-MMP-2 (15 citations) MMP Inhibitor II (3 citations) Active MMP-2 (2 citations) MMP-2/MMP-9 inhibitor III (2 citations) Human MMP Panel 2 Magnetic Bead Kit (2 citations) MMP panel 2 HMMP2MAG-55K kit (2 citations) Recombinant human MMP-2 (6 citations) MMP-2 Inhibitor I (5 citations) Human MMP Panel 2 Magnetic Bead HMMP2MAG-55 K (2 citations)

63 protocols using mmp 2

Inhibition of Collagen Degradation by CG-Renuin and CG-Noverin

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Example 5

Human dermal fibroblast (HDF) cells (3×10⁴) were seeded in a 24-well plate. The next day, the cells were incubated in 5% serum medium for 42 hours, treated with MMP2 (20 ng/ml, SIGMA/USA) and CG-Noverin or CG-Renuin, respectively, and incubated for 6 hours. The supernatant obtained from centrifugation at 14,000×g for 10 minutes was analyzed using the pro-collagen type I kit (RnD system/USA).

Human dermal fibroblast (HDF) cells (3×10⁴) were seeded in a 24-well plate, and then the next day, the medium was exchanged with a 5% serum medium. The cells were treated with IGF-1 (100 ng/ml, Sigma/USA), followed by incubation for 44 hours, and then the cells were treated with MMP2 (20 ng/ml) and CG-Noverin or CG-Renuin, respectively, followed by incubation for 4 hours. The supernatant obtained from centrifugation at 14,000×g for 10 minutes was analyzed using the pro-collagen type I kit.

As a result of testing whether CG-Renuin and CG-Noverin have functions of inhibiting the collagen degradation induced by MMP2, it was verified that the MMP2 treatment increased the intracellular degradation of collagen when compared with a control group, and inhibited the induction of collagen degradation by co-treatment with CG-Renuin or CG-Noverin (FIGS. 6a-6b and 7a-7b).

US10487113B2. Peptide having activity to improve skin condition and use thereof (2019-11-26). CAREGEN CO., LTD. [KR]. Inventors: Yong Ji Chung [KR], Eun Mi Kim [KR].

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Inhibition of MMP and ADAM Proteases

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KP‐457 and GM‐6001 were tested for their ability to inhibit MMP‐ and ADAM‐catalyzed cleavage of substrates in a fluorescence‐based assay. Human ADAM17, ADAM10, and MMP17 were from R&D Systems (Minneapolis, MN, http://www.rndsystems.com), and human MMP1, MMP2, MMP3, MMP8, MMP9, MMP13, and MMP14 were from EMD Millipore. MMP1, MMP2, MMP8, MMP9, MMP13, and MMP17 were activated using p‐aminophenylmercuric acetate (Sigma‐Aldrich) before testing. Fluorogenic substrates for measuring activity of ADAM10 and ADAM17 [Nma‐LAQAVRSSK(Dnp)r‐NH₂, based on the cleavage site of TNF‐α]; MMP1, MMP9, MMP13, and MMP14 [Dnp‐P‐Cha‐GC(Me)HAK(N‐Me‐Abz)‐NH₂]; MMP3 [MOCAc‐RPKPVE‐Nva‐WRK(Dnp)‐NH₂]; and MMP2, MMP8, and MMP17 [MOCAc‐PLGL‐A₂pr(Dnp)‐AR‐NH₂] were all provided by Peptide Institute (Osaka, Japan, https://www.peptide.co.jp/en) and used as substrates. In addition, inhibitory activities were measured using LC/MS/MS with a GPIbα‐based substrate peptide (KKTIPELDQPPKLRGVLQGHLESSRNDPFLHPDF), a C terminal‐based standard peptide (VLQGHLESSRNDPFLHPDF), and an internal standard peptide (VTTGKGQDHSPFWGF). These peptides were synthetized by Scrum (Tokyo, Japan, http://www.scrum‐net.co.jp/english/top_en.htm).

Hirata S., Murata T., Suzuki D., Nakamura S., Jono‐Ohnishi R., Hirose H., Sawaguchi A., Nishimura S., Sugimoto N, & Eto K. (2016). Selective Inhibition of ADAM17 Efficiently Mediates Glycoprotein Ibα Retention During Ex Vivo Generation of Human Induced Pluripotent Stem Cell‐Derived Platelets. Stem Cells Translational Medicine, 6(3), 720-730.

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Fibroblast Collagen Degradation Inhibition

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Example 5

US10047125B2. Peptide having activity to improve skin condition and use thereof (2018-08-14). CAREGEN CO., LTD. [KR]. Inventors: Yong Ji Chung [KR], Eun Mi Kim [KR].

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Quantifying MMP-2 and MMP-9 in Cell Media

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MMP-2 (Life Technologies, UK) and MMP-9 (Invitrogen, UK) ELISAs were carried out as per the manufacturers instruction. For each ELISA, samples of DMEM were included as controls and cell supernatant was diluted 1/10 with standard diluent. For MMP-2 ELISA, an additional positive control was also included of 0.1 mg/mL MMP-2 spiked (Sigma Aldrich, USA) serum free media (complete DMEM without FBS addition). ELISA plates were read at 450 nm using Clariostar microplate reader (BMG Labtech, Germany).

Anderson H.J., Sahoo J.K., Wells J., van Nuffel S., Dhowre H.S., Oreffo R.O., Zelzer M., Ulijn R.V, & Dalby M.J. (2022). Cell-controlled dynamic surfaces for skeletal stem cell growth and differentiation. Scientific Reports, 12, 8165.

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Nanoparticle Synthesis and Characterization

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1-Octadecene, MTT reagent, 4′-6-diamidino-2-phenylindole (DAPI, Thermo Fisher Scientific), acetone (≥99.9%) and acetonitrile (ACN; 99.8%), hexane (95%), iron pentacarbonyl (Fe(CO)₅), oleic acid (90%), PTX (Scinopharm), LST (Fluka), PBS (UniRegion Bio-tech), oleylamine (>70%), pluronic F-127 (Sigma-Aldrich Co., St Louis, MO, USA), sodium dodecyl sulfate gel, acrylamide/bis-acrylamide (40% solution, 29:1), N,N,N′,N′-tetramethylethylenediamine (~99%), trimethylamine N-oxide and ammonium persulfate (≥98%) were purchased from Sigma-Aldrich Co. Benzyl ether (99%), gelatin type A (from porcine skin), MMP-2 (≥98%), chloroform, N-hydroxysuccinimide (NHS) and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) were purchased from Sigma-Aldrich Co. Formaldehyde was purchased from Riedel de Haen and Tri-ton X-100 from J.T. Baker. CdSe/ZnS core/shell QDs were obtained from Ocean Nanotech (Springdale, AR, USA). All chemicals and solvents were of analytical reagent grade.

Lai Y.H., Chiang C.S., Kao T.H, & Chen S.Y. (2018). Dual-drug nanomedicine with hydrophilic F127-modified magnetic nanocarriers assembled in amphiphilic gelatin for enhanced penetration and drug delivery in deep tumor tissue. International Journal of Nanomedicine, 13, 3011-3026.

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Enzymatic Digestion of Antibodies by MMP-2

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The pro-antibody or antibody samples were incubated with 5 μg/ml MMP-2 (type IV collagenase, Sigma-Aldrich, St. Louis, MO, USA) or buffer only (DMEM) for different incubation times (1, 5, 10, 30, 60, 90 and 120 minutes). In our experiments, we opted to use a higher concentration of MMP-2 (1 μg/200 μL, 2700 μU/μg solid enzymes; μU, Furylacryloyl-Leu-Gly-Pro-Ala (FALGPA) peptide hydrolysis activity in microunits) and a shorter digestion time (1 h) as compared to prolonged digestion by lower concentrations of MMP-2 in the colorectal cancer tumor tissues (4762.5 μU/mg protein)^{45 (link)}. After MMP-2 digestion, samples were mixed with 6× sodium dodecyl sulfate (SDS) reducing loading dye for gel electrophoresis and western blotting analyses, or mixed with 10% cosmic calf serum for ELISA experiments.

Chen I.J., Chuang C.H., Hsieh Y.C., Lu Y.C., Lin W.W., Huang C.C., Cheng T.C., Cheng Y.A., Cheng K.W., Wang Y.T., Chen F.M., Cheng T.L, & Tzou S.C. (2017). Selective antibody activation through protease-activated pro-antibodies that mask binding sites with inhibitory domains. Scientific Reports, 7, 11587.

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Quantifying Anti-Elastin and Anti-Collagen V Antibodies

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Human elastin fragments (ELNf) were generated by in vitro digestion with MMP-2 and MMP-9 (Sigma) per manufacturer’s instructions. Relative antibody concentrations specific to human collagen V (COLV) and ELNf were assayed via a previous described modified ELISA protocol.¹⁵ In short, respective antigenic peptides were dissolved in phosphate-buffered saline (PBS) to a stock working solution of 25 ug/mL. This stock solution was used to coat a high protein binding 96-well polystyrene plate (Sigma) for two hours at 37 °C or overnight at 4 °C. Copious washings were performed between all steps with PBS-T (Tween 20, Sigma). The 96-well plate was blocked with 1% bovine serum albumin (BSA, Sigma) for two hours at 37 °C or overnight at 4 °C. Plasma samples were then sequentially diluted up to 1:1000 to determine optimal concentrations and incubated for two hours at 37 °C or overnight at 4 °C. A goat anti-human IgG Fc antibody conjugated to horseradish peroxidase (HRP, Sigma) was utilized as a secondary antibody per manufacturer’s recommended dilution for a duration of one hour at 37 °C. Reactions were performed using a 1-step TMB turbo substrate (Sigma) for 30 minutes before a 1 M sulfuric acid stop solution was added. Absorbance at 450 nm was measured within 30 minutes to calculate relative self-antibody concentrations.

Wang S.K., Green L.A., Gutwein A.R., Drucker N.A., Motaganahalli R.L., Gupta A.K., Fajardo A, & Murphy M.P. (2018). Description of Human AAA by Cytokine and Immune Cell Aberrations Compared to Risk-Factor Matched Controls. Surgery, 164(2), 354-358.

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Western Blot Analysis of HIF-1α, MMP-2, VEGF

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Radioimmunoprecipitation assay buffer (RIPA) was used to extract proteins from cells, which were separated by 10% sodium dodecylsulfate-polyaclylamidegel electrophoresis (SDS-PAGE) and then transferred to polyvinylidene fluoride (PVDF) membranes. The membranes were blocked with 5% skimmed milk resolved in PBS (pH 7.4, with 0.1% Tween 20) for 60 min. Afterward, primary antibodies was added to the membrane which were incubated at 37°C for 60 minutes. After removal of excess primary antibody, horseradish peroxidase (HRP)-linked secondary antibody diluted in 0.01 M PBS was added to the membrane and incubated at room temperature for 30 min, and then washed with 0.01 M PBS for four times. Enhanced BM chemiluminescence blotting substrate (Roche Diagnostics) was used to detect the antigens. The luminescence intensity was quantified by Image J. mouse-anti-human HIF-1α (1:250, Sigma-Aldrich), MMP-2 (1:1000, Sigma-Aldrich), VEGF (1:1000, Sigma-Aldrich), and MVD (1:1000, Sigma-Aldrich).

Ma Y., Liu G., Yang J., Li X., Yang X., Fang S, & Zhao B. (2022). The Efficacy of Combined Therapy of Regorafenib with Detoxicating and Stasis Softening Chinese Herbal Spleen Tonics in Mid-/Late-Stage Hepatocellular Carcinoma. Contrast Media & Molecular Imaging, 2022, 9316873.

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Melanoma Cell Lines and shRNA Knockdown

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shRNAs against human MT1-MMP (TRCN0000050855) and MMP2 (TRCN0000051526) were purchased from Sigma and were previously described[12 (link), 13 (link)]. The primary melanoma cells line WM115, the syngeneic metastatic WM266–4, and the metastatic melanoma cell lines V2387 and K457 were originally purchased from ATCC or a gift or Dr. Marianne Broome Powell (Stanford University, Stanford, CA). Cells were maintained in DMEM supplemented with 10% FCS, 1% glutamine, and 1% penicillin-streptomycin.

Marusak C., Bayles I., Ma J., Gooyit M., Gao M., Chang M, & Bedogni B. (2016). The thiirane-based selective MT1-MMP/MMP2 inhibitor ND-322 reduces melanoma tumor growth and delays metastatic dissemination. Pharmacological research, 113(Pt A), 515-520.

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Comprehensive Cell Culture Protocol

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DMEM medium, fetal bovine serum (FBS), EDTA, and penicillin-streptomycin were purchased from Hyclone; dimethyl sulfoxide and MTT were purchased from Gibco; trypsin-EDTA was purchased from Sigma; PVDF membrane was purchased from Pall Life Sciences; Western blot-related chemical reagents were from Shanghai Beyotime biotechnology Co. LTD; ECL reagent was purchased from Amersham Biosciences; DDR-1 monoclonal antibody and HRP tagged IgG secondary antibody were purchased from Cell Signaling; nilotinib and transwell chambers were purchased from Sigma; MMP-2 and MMP-9 ELISA kits were purchased from R&D; other reagents were purchased from Shanghai Sangon Biotechnology Co., LTD; and Labsystem Version1.3.1 microplate reader was purchased from Bio-rad.

Li S., Zhang Z., Xue J., Guo X., Liang S, & Liu A. (2015). Effect of Hypoxia on DDR1 Expression in Pituitary Adenomas. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 21, 2433-2438.

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