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Recombinant Human MMP-2 Protein, CF

Catalog #: 902-MP
29 Citations 3 Reviews Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
902-MP-010
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (29)
FAQs
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Reviews (3)
Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human MMP-2 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
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.
Source
Chinese Hamster Ovary cell line, CHO-derived human MMP-2 protein
Ile34-Cys660
Accession #
P08253
N-terminal Sequence
Analysis
Ile34
Structure / Form
Pro form
Predicted Molecular Mass
71 kDa
SDS-PAGE
71 kDa, reducing conditions

Product Datasheets

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902-MP

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

902-MP

Formulation Supplied as a 0.2 μm filtered solution in Tris, CaCl2, NaCl and Brij-35.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Assay Procedure

Materials
  • Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij 35, pH 7.5 (TCNB)
  • Recombinant Human MMP-2 (rhMMP-2) (Catalog # 902-MP)
  • p-aminophenylmercuric acetate (APMA), (Sigma, Catalog # A-9563), 100 mM stock in DMSO
  • Fluorogenic Peptide Substrate I: MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (Catalog # ES001)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhMMP-2 to 100 µg/mL in Assay Buffer.
  2. Activate rhMMP-2 by adding APMA to a final concentration of 1 mM.
  3. Incubate at 37 °C for 1 hour.
  4. Dilute activated rhMMP-2 to 0.2 ng/µL in Assay Buffer.
  5. Dilute Substrate to 20 µM in Assay Buffer.
  6. Load into a black well plate 50 µL of the 0.2 ng/µL rhMMP-2 and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer and 50 µL of 20 µM Substrate.
  7. Read at excitation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes.
  8. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

 Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank

     **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).

Per Well:
  • rhMMP-2: 0.010 µg
  • Substrate: 10 µM
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: MMP-2

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP-2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites.

Long Name
Matrix Metalloproteinase 2
Entrez Gene IDs
4313 (Human); 17390 (Mouse)
Alternate 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)

Citations for Recombinant Human MMP-2 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

29 Citations: Showing 1 - 10
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  1. An Investigation of the Altered Textural Property in Woody Breast Myopathy Using an Integrative Omics Approach
    Authors: AA Welter, WJ Wu, R Maurer, TG O'Quinn, MD Chao, DL Boyle, ER Geisbrecht, SD Hartson, BC Bowker, H Zhuang
    Frontiers in Physiology, 2022-03-17;13(0):860868.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  2. Protease-Triggered Release of Stabilized CXCL12 from Coated Scaffolds in an Ex Vivo Wound Model
    Authors: S Spiller, T Wippold, K Bellmann-S, S Franz, A Saalbach, U Anderegg, AG Beck-Sicki
    Pharmaceutics, 2021-10-01;13(10):.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  3. Novel Ex Vivo Zymography Approach for Assessment of Protease Activity in Tissues with Activatable Antibodies
    Authors: B Howng, MB Winter, C LePage, I Popova, M Krimm, O Vasiljeva
    Pharmaceutics, 2021-09-02;13(9):.
    Species: Human
    Sample Types: Peptides
    Applications: Bioassay
  4. Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen
    Authors: F Uliana, M Vizovišek, L Acquasalie, R Ciuffa, A Fossati, F Frommelt, S Goetze, B Wollscheid, M Gstaiger, V De Filippi, U Auf dem Ke, R Aebersold
    Nature Communications, 2021-03-16;12(1):1693.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  5. Matrix metalloproteinase (MMP)-2, MMP-9, semen quality and sperm longevity in fractionated stallion semen
    Authors: M Kareskoski, J Vakkamäki, K Laukkanen, M Palviainen, A Johannisso, T Katila
    Theriogenology, 2021-02-02;164(0):93-99.
    Species: Equine
    Sample Types: Semen
    Applications: Gelatin Zymography Control
  6. Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)-A CleavEx Based Analysis
    Authors: K Falkowski, E Bielecka, IB Thøgersen, O Boche?ska, K P?aza, M Kali?ska, L S?siadek, M Magoch, A P?cak, M Wi?niewska, N Gruba, M Wysocka, A Wojtysiak, M Brzezi?ska, K Sychowska, A Pejkovska, M Rehders, G Butler, CM Overall, K Brix, G Dubin, A Lesner, A Kozik, JJ Enghild, J Potempa, T Kantyka
    Int J Mol Sci, 2020-06-19;21(12):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  7. Biodistribution of Nanostructured Lipid Carriers in Mice Atherosclerotic Model
    Authors: L Devel, G Almer, C Cabella, F Beau, M Bernes, P Oliva, F Navarro, R Prassl, H Mangge, I Texier
    Molecules, 2019-09-26;24(19):.
    Species: Human
    Sample Types: Peptide
    Applications: Bioassay
  8. Eradication of unresectable liver metastasis through induction of tumour specific energy depletion
    Authors: D Huo, J Zhu, G Chen, Q Chen, C Zhang, X Luo, W Jiang, X Jiang, Z Gu, Y Hu
    Nat Commun, 2019-07-11;10(1):3051.
    Species: Human
    Sample Types: Nanoparticles
    Applications: Bioassay
  9. Glycosaminoglycans influence enzyme activity of MMP2 and MMP2/TIMP3 complex formation - Insights at cellular and molecular level
    Authors: G Ruiz-Gómez, S Vogel, S Möller, MT Pisabarro, U Hempel
    Sci Rep, 2019-03-20;9(1):4905.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Enzyme Assay
  10. Reduced vasorin enhances angiotensin II signaling within the aging arterial wall
    Authors: G Pintus, R Giordo, Y Wang, W Zhu, SH Kim, L Zhang, L Ni, J Zhang, R Telljohann, KR McGraw, RE Monticone, C Ferris, L Liu, M Wang, EG Lakatta
    Oncotarget, 2018-06-05;9(43):27117-27132.
    Species: Rat
    Sample Types: Protein
    Applications: Enzyme Assay
  11. The enzymatic processing of ?-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site
    Authors: M Gioia, GF Fasciglion, D Sbardella, F Sciandra, M Casella, S Camerini, M Crescenzi, A Gori, U Tarantino, P Cozza, A Brancaccio, M Coletta, M Bozzi
    PLoS ONE, 2018-02-15;13(2):e0192651.
    Applications: Bioassay
  12. Downregulation of monocytic differentiation via modulation of CD147 by 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors
    Authors: MV Sasidhar, SK Chevooru, O Eickelberg, HP Hartung, O Neuhaus
    PLoS ONE, 2017-12-18;12(12):e0189701.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Zymography
  13. Gelatinases A and B and Antioxidant Enzyme Activity in the Early Phase of Acute Myocardial Infarction
    Authors: K Gopcevic, B Rovcanin, D Kekic, D Milasinovi, G Kocic, I Stojanovic
    Folia Biol. (Praha), 2017-01-01;63(1):20-26.
    Applications: Zymography
  14. Plantamajoside, a potential anti-tumor herbal medicine inhibits breast cancer growth and pulmonary metastasis by decreasing the activity of matrix metalloproteinase-9 and -2.
    Authors: Pei S, Yang X, Wang H, Zhang H, Zhou B, Zhang D, Lin D
    BMC Cancer, 2015-12-16;15(0):965.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  15. Stanniocalcin-1 Potently Inhibits the Proteolytic Activity of the Metalloproteinase Pregnancy-associated Plasma Protein-A.
    Authors: Kloverpris S, Mikkelsen J, Pedersen J, Jepsen M, Laursen L, Petersen S, Oxvig C
    J Biol Chem, 2015-07-20;290(36):21915-24.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  16. Protease-degradable electrospun fibrous hydrogels.
    Authors: Wade R, Bassin E, Rodell C, Burdick J
    Nat Commun, 2015-03-23;6(0):6639.
    Applications: Bioassay
  17. ADAM8 as a drug target in pancreatic cancer.
    Authors: Schlomann U, Koller G, Conrad C, Ferdous T, Golfi P, Garcia A, Hofling S, Parsons M, Costa P, Soper R, Bossard M, Hagemann T, Roshani R, Sewald N, Ketchem R, Moss M, Rasmussen F, Miller M, Lauffenburger D, Tuveson D, Nimsky C, Bartsch J
    Nat Commun, 2015-01-28;6(0):6175.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  18. Investigation of a MMP-2 activity-dependent anchoring probe for nuclear imaging of cancer.
    Authors: Temma, Takashi, Hanaoka, Hirofumi, Yonezawa, Aki, Kondo, Naoya, Sano, Kohei, Sakamoto, Takeharu, Seiki, Motoharu, Ono, Masahiro, Saji, Hideo
    PLoS ONE, 2014-07-10;9(7):e102180.
    Applications: Bioassay
  19. Soft matrix is a natural stimulator for cellular invasiveness.
    Authors: Gu, Zhizhan, Liu, Fei, Tonkova, Elina A, Lee, Soo Youn, Tschumperlin, Daniel J, Brenner, Michael
    Mol Biol Cell, 2013-12-11;25(4):457-69.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Control
  20. Astrocytes directly influence tumor cell invasion and metastasis in vivo.
    Authors: Wang, Ling, Cossette, Stephani, Rarick, Kevin R, Gershan, Jill, Dwinell, Michael, Harder, David R, Ramchandran, Ramani
    PLoS ONE, 2013-12-04;8(12):e80933.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Bioassay
  21. Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers.
    Authors: Djokic J, Fagotto-Kaufmann C, Bartels R, Nelea V, Reinhardt D
    J Biol Chem, 2013-06-19;288(31):22821-35.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  22. Resistance of corneal RFUVA-cross-linked collagens and small leucine-rich proteoglycans to degradation by matrix metalloproteinases.
    Authors: Zhang Y, Mao X, Schwend T, Littlechild S, Conrad G
    Invest Ophthalmol Vis Sci, 2013-02-05;54(2):1014-25.
    Species: Bovine
    Sample Types: Protein
    Applications: Enzyme Assay
  23. Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.
    Authors: Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura E, Dive V
    J Biol Chem, 2012-06-11;287(32):26647-56.
    Applications: Enzyme Assay
  24. Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp).
    Authors: Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y
    J. Bone Miner. Res., 2011-01-01;26(0):220.
    Species: Human
    Sample Types:
    Applications: Bioassay
  25. Development and validation of sandwich ELISA microarrays with minimal assay interference.
    Authors: Gonzalez RM, Seurynck-Servoss SL, Crowley SA
    J. Proteome Res., 2008-04-19;7(6):2406-14.
    Applications: ELISA (Standard)
  26. Borrelia burgdorferi-induced monocyte chemoattractant protein-1 production in vivo and in vitro.
    Authors: Zhao Z, McCloud B, Fleming R, Klempner MS
    Biochem. Biophys. Res. Commun., 2007-05-02;358(2):528-33.
    Applications: Zymography
  27. Role of platelet-derived growth factor and transforming growth factor beta1 the in the regulation of metalloproteinase expressions.
    Authors: Borrelli V, di Marzo L, Sapienza P, Colasanti M, Moroni E, Cavallaro A
    Surgery, 2006-09-01;140(3):454-63.
    Applications: Western Blot
  28. Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer.
    Authors: Zhou BB, Peyton M, He B, Liu C, Girard L, Caudler E, Lo Y, Baribaud F, Mikami I, Reguart N, Yang G, Li Y, Yao W, Vaddi K, Gazdar AF, Friedman SM, Jablons DM, Newton RC, Fridman JS, Minna JD, Scherle PA
    Cancer Cell, 2006-07-01;10(1):39-50.
    Species: Human
    Sample Types:
    Applications: Enzyme Assay
  29. Oxidized low-density lipoproteins stimulate extracellular matrix metalloproteinase Inducer (EMMPRIN) release by coronary smooth muscle cells.
    Authors: Haug C, Lenz C, Diaz F, Bachem MG
    Arterioscler. Thromb. Vasc. Biol., 2004-08-19;24(10):1823-9.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay

FAQs

  1. Can the enzyme be stored after activation, or do I need to use it immediately after activation?

    • We recommend only activating the amount of enzyme needed for your assay, and recommend activating the enzyme immediately prior to use. Any unactivated enzyme should be stored in aliquots at either the stock concentration at which the enzyme was supplied, or the reconstitution concentration, according to the product datasheet.

  2. Does this enzyme have a tag?

    • No, this enzyme does not have a tag.  Please refer to the Source section on the product-specific page or product datasheet for sequence information.

  3. If I use this enzyme at a higher concentration, do I need to change the concentration of APMA to activate it?

    • We have only optimized activation conditions for one particular concentration of this MMP enzyme as part of our regular QC testing for enzymatic activity. Activating the enzyme at any different concentration would have to be optimized by the end user.

  4. Does this MMP enzyme need to be activated to work?

    • Yes, this enzyme requires activation prior to use.

  5. What is the activity of this enzyme in units/µg?

    • We supply this enzyme as a mass and calculate its activity relative to mass (pmol/min/µg). We have not calibrated this enzyme to an international standard unit, so we are unable to provide a conversion to units/µg.

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Reviews for Recombinant Human MMP-2 Protein, CF

Average Rating: 4.7 (Based on 3 Reviews)

5 Star
66.67%
4 Star
33.33%
3 Star
0%
2 Star
0%
1 Star
0%

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Recombinant Human MMP-2 Protein, CF
By Andres Ocampo Carrillo on 03/04/2023
Application: Enzymatic activity in vitro
Reason for Rating: The product was very easy to dissolve and use in an enzymatic cleavage of proteins. The product showed an excellent cleavage activity.

rhMMP-2 was diluted up to a final concentration of 1 mM using p-amino phenylmercuric acetate (APMA) and mixed with chondrocyte lysate protein to test the cleavage of prolactin hormone (PRL) into 16K products. Western blot pictures showed the successful formation of several fragments after the mixture. L represents the Lysate, PRL Std the Prolactin Standard

Enzymatic activity in vitro Recombinant Human MMP-2 Protein, CF 902-MP
Recombinant Human MMP-2 Protein, CF
By Anonymous on 11/06/2020
Application: Enzymatic activity in vitro
Recombinant Human MMP-2 Protein, CF
By Anonymous on 11/09/2017
Application: Immunoassay Standard

The recombinant MMP-2 protein was used to build a calibration curve to measure MMP-2 in human serum samples.

Immunoassay Standard Recombinant Human MMP-2 Protein, CF 902-MP