Recombinant Human MMP-2 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human MMP-2 Protein, CF Summary

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.
Source
Chinese Hamster Ovary cell line, CHO-derived human MMP-2 protein
Ile34-Cys660
Accession #
N-terminal Sequence
Ile34
Structure / Form
Pro form
Protein/Peptide Type
Recombinant Enzymes
Gene
MMP2
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
71 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
71 kDa, reducing conditions
Publications
Read Publications using
902-MP in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, CaCl2, NaCl and Brij-35.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Assay Procedure
  • 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

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human MMP-2 Protein, CF

  • 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)

Background

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.

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Publications for MMP-2 (902-MP)(20)

We have publications tested in 4 confirmed species: Human, Rat, Bovine, N/A.

We have publications tested in 9 applications: Bioassay, Cleavage, Ctrl, ELISA Standard, EnzAct, Enzyme Assay, WB Ctrl, Zymography Positive Ctrl, Zymography Standard.


Filter By Application
Bioassay
(8)
Cleavage
(1)
Ctrl
(1)
ELISA Standard
(1)
EnzAct
(2)
Enzyme Assay
(3)
WB Ctrl
(1)
Zymography Positive Ctrl
(2)
Zymography Standard
(1)
All Applications
Filter By Species
Human
(10)
Rat
(1)
Bovine
(1)
N/A
(6)
All Species
Showing Publications 1 - 10 of 20. Show All 20 Publications.
Publications using 902-MP Applications Species
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 Reduced vasorin enhances angiotensin II signaling within the aging arterial wall Oncotarget, 2018;9(43):27117-27132. 2018 [PMID: 29930755] (EnzAct, Rat) EnzAct Rat
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 The enzymatic processing of ?-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site PLoS ONE, 2018;13(2):e0192651. 2018 [PMID: 29447293] (Bioassay) Bioassay
MV Sasidhar, SK Chevooru, O Eickelberg, HP Hartung, O Neuhaus Downregulation of monocytic differentiation via modulation of CD147 by 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors PLoS ONE, 2017;12(12):e0189701. 2017 [PMID: 29253870] (Zymography Positive Ctrl, Human) Zymography Positive Ctrl Human
K Gopcevic, B Rovcanin, D Kekic, D Milasinovi, G Kocic, I Stojanovic Gelatinases A and B and Antioxidant Enzyme Activity in the Early Phase of Acute Myocardial Infarction Folia Biol. (Praha), 2017;63(1):20-26. 2017 [PMID: 28374671] (Zymography Standard) Zymography Standard
Pei S, Yang X, Wang H, Zhang H, Zhou B, Zhang D, Lin D 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(0):965. 2015 [PMID: 26674531] (Bioassay, Human) Bioassay Human
Kloverpris S, Mikkelsen J, Pedersen J, Jepsen M, Laursen L, Petersen S, Oxvig C Stanniocalcin-1 Potently Inhibits the Proteolytic Activity of the Metalloproteinase Pregnancy-associated Plasma Protein-A. J Biol Chem, 2015;290(36):21915-24. 2015 [PMID: 26195635] (Enzyme Assay, Human) Enzyme Assay Human
Wade R, Bassin E, Rodell C, Burdick J Protease-degradable electrospun fibrous hydrogels. Nat Commun, 2015;6(0):6639. 2015 [PMID: 25799370] (Bioassay, N/A) Bioassay N/A
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 ADAM8 as a drug target in pancreatic cancer. Nat Commun, 2015;6(0):6175. 2015 [PMID: 25629724] (Bioassay, Human) Bioassay Human
Temma, Takashi, Hanaoka, Hirofumi, Yonezawa, Aki, Kondo, Naoya, Sano, Kohei, Sakamoto, Takeharu, Seiki, Motoharu, Ono, Masahiro, Saji, Hideo Investigation of a MMP-2 activity-dependent anchoring probe for nuclear imaging of cancer. PLoS ONE, 2014;9(7):e102180. 2014 [PMID: 25010662] (Bioassay, N/A) Bioassay N/A
Gu, Zhizhan, Liu, Fei, Tonkova, Elina A, Lee, Soo Youn, Tschumperlin, Daniel J, Brenner, Michael Soft matrix is a natural stimulator for cellular invasiveness. Mol Biol Cell, 2014;25(4):457-69. 2014 [PMID: 24336521] (Ctrl, Human) Ctrl Human
Show All 20 Publications.

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Blogs on MMP-2.

MMP-2: More Than a Cancer Marker
Matrix metalloproteinases (MMP) are a family of endopeptidases involved in the breakdown of extracellular matrix (ECM) during both normal physiological and disease processes. MMP-2 is a zinc-dependent family member that selectively cleaves collagen...  Read full blog post.

CD63: is it pro-metastatic or anti-metastatic?
CD63 is a type II membrane protein belonging to tetraspanin superfamily and it play key roles in the activation of several cellular signaling cascades along with acting as TIMP1 receptor. It is expressed by activated platelets, monocytes,...  Read full blog post.

Integrin alpha v beta 3 - a target for inhibiting tumor angiogenesis
Integrins are a family of transmembrane proteins involved in diverse processes including cell adhesion, signal transduction, cell migration, and differentiation. They exist as heterodimers consisting of noncovalently linked alpha and beta subunits....  Read full blog post.

Cytokeratin 18 - A Intermediate Filament Cyotskeletal Component
Keratins, also called cytokeratins, are a family of filamentous structural proteins that form the intermediate filaments within epithelial cells. Keratins are differentially expressed depending on both the epithelial cell origin and degree of differen...  Read full blog post.

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Bioinformatics

Gene Symbol MMP2
Uniprot