MMP-2 Protein, Human, Recombinant

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MMP-2 Protein, Human, Recombinant: Product Information

Purity
> (74.7+17.3) % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its ability to cleave the fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2 (AnaSpec, Catalog # 27076). The specific activity is > 1,000 pmoles/min/µg.
2. Measured by its binding ability in a functional ELISA.
3. Immobilized human MMP2 at 10 μg/mL (100 μl/well) can bind human TIMP2/Fc (Cat: 10396-H01H). The EC50 of human TIMP2/Fc is 0.02 μg/mL.
(Activation description: The proenzyme needs to be activated by APMA for an activated form)
Protein Construction
A DNA sequence encoding the native human MMP2 (NP_004521.1) (Met 1-Cys 660) was expressed and purified.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Ala 30
Molecule Mass
The recombinant human MMP2 consists of 631 amino acids and migrates as an 72 kDa band as predicted in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile 0.05 % Brij-35, 150 mM NaCl, 5 mM CaCl2, 50 mM Tris, pH 7.5.
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

MMP-2 Protein, Human, Recombinant: Images

Measured by its binding ability in a functional ELISA. Immobilized human MMP2 at 10 μg/mL (100 μl/well) can bind human TIMP2/Fc (Cat: 10396-H01H). The EC50 of human TIMP2/Fc is 0.02 μg/mL

MMP-2 Protein, Human, Recombinant: Alternative Names

CLG4 Protein, Human; CLG4A Protein, Human; MMP-2 Protein, Human; MMP-II Protein, Human; MONA Protein, Human; TBE-1 Protein, Human

MMP-2 Background Information

Matrix Metalloproteinase-2 (MMP-2) is an enzyme that degrades components of the extracellular matrix and thus plays a pivotal role in cell migration during physiological and pathological processes. MMP-2 expression is dependent on extracellular matrix metalloproteinase inducer (EMMPRIN), Her2/neu, growth factors, cytokines, and hormones. Pro-MMP-2 activation needs MT1-MMP and TIMP-2 contribution. MMP-2 is changed in distribution and increased in amount in the ventral cochlear nucleus after unilateral cochlear ablation. A low level of MMP-2 is linked to favorable prognosis in patients with a hormone receptor-negative tumor, usually associated with high risk. As a zymogen requiring proteolytic activation for catalytic activity, MMP-2 has been implicated broadly in the invasion and metastasis of many cancer model systems, including human breast cancer (HBC). Blocking MMP-2 secretion and activation during breast carcinoma development may decrease metastasis. The detection of active MMP-2 alone or the rate of pro-MMP-2 and active MMP-2 is considered a very sensitive indicator of cancer metastasis. Modulation of MMP-2 expression and activation through specific inhibitors and activators may thus provide a new mechanism for breast cancer treatment.
Full Name
matrix metallopeptidase 2
References
  • Thompson EW, et al. (1994) Collagen induced MMP-2 activation in human breast cancer. Breast Cancer Res Treat. 31(2-3): 357-70.
  • Jezierska A, et al. (2009) Matrix metalloproteinase-2 involvement in breast cancer progression: a mini-review. Med Sci Monit. 15(2): RA32-40.
  • Fredrich M, et al. (2010) MMP-2 is involved in synaptic remodeling after cochlear lesion. Neuroreport. 21(5): 324-7.
  • A graphene oxide-based FRET sensor for rapid and sensitive detection of matrix metalloproteinase 2 in human serum sample
    Author
    Song, E;Cheng, D;Song, Y;Jiang, M;Yu, J;Wang, Y;
    Year
    2013
    Journal
    Biosens Bioelectron
    Application
    enzyme
  • Enzyme-responsive liposomes modified adenoviral vectors for enhanced tumor cell transduction and reduced immunogenicity
    Author
    Wan, Y;Han, J;Fan, G;Zhang, Z;Gong, T;Sun, X;
    Year
    2013
    Journal
    Biomaterials
  • Fiber-optic protease sensor based on the degradation of thin gelatin films
    Author
    Schyrr, B;Boder-Pasche, S;Ischer, R;Smajda, R;
    Year
    2014
    Journal
    Sensing and Bio-Sensing Research
    Application
    enzyme
  • Bio-inspired polymer envelopes around adenoviral vectors to reduce immunogenicity and improve in vivo kinetics
    Author
    Fan, G;Fan, M;Wang, Q;Jiang, J;Wan, Y;Gong, T;Zhang, Z;Sun, X;
    Year
    2015
    Journal
    Acta Biomater
    Application
    enzyme (control)
  • Laminin Promotes Metalloproteinase Mediated Dystroglycan Processing to Regulate Oligodendrocyte Progenitor Cell Proliferation
    Author
    Leiton, CV;Aranmolate, A;Eyermann, C;Menezes, MJ;Escobar-Hoyos, LF;Husain, S;Winder, SJ;Colognato, H;
    Year
    2015
    Journal
    J. Neurochem.
    Application
    enzyme
  • Modular Design and Facile Synthesis of Enzyme-Responsive Peptide-Linked Block Copolymers for Efficient Delivery of Doxorubicin
    Author
    Ke, W;Li, J;Zhao, K;Zha, Z;Han, Y;Wang, Y;Yin, W;Zhang, P;Ge, Z;
    Year
    2016
    Journal
    Biomacromolecules
    Application
    enzyme
  • Activatable Near-Infrared Probe for Fluorescence Imaging of γ-Glutamyl Transpeptidase in Tumor Cells and In Vivo
    Author
    Luo, Z;Feng, L;An, R;Duan, G;Yan, R;Shi, H;He, J;Zhou, Z;Ji, C;Chen, HY;Ye, D;
    Year
    2017
    Journal
    Chemistry
    Application
    control (negative)
  • Peptide Microarray-Based Metal Enhanced Fluorescence Assay for Multiple Profiling of Matrix Metalloproteinases Activities
    Author
    Lei, Z;Zhang, H;Wang, Y;Meng, X;Wang, Z;
    Year
    2017
    Journal
    Anal. Chem.
    Application
    enzyme(FRET-Peptide Microarray-Based MEF Assay)
  • Smart Asymmetric Vesicles with Triggered Availability of Inner Cell-Penetrating Shells for Specific Intracellular Drug Delivery
    Author
    Li, J;Xiao, S;Xu, Y;Zuo, S;Zha, Z;Ke, W;He, C;Ge, Z;
    Year
    2017
    Journal
    ACS Appl Mater Interfaces
    Application
    enzyme(cleave the stealthy PEG shell)
  • Evaluation of Matrix Metalloproteinase Inhibition by Peptide Microarray-Based Fluorescence Assay on Polymer Brush Substrate and in Vivo Assessment
    Author
    Lei, Z;Chen, H;Zhang, H;Wang, Y;Meng, X;Wang, Z;
    Year
    2017
    Journal
    ACS Appl Mater Interfaces
    Application
    enzyme
  • A coiled-coil masking domain for selective activation of therapeutic antibodies
    Author
    Trang, VH;Zhang, X;Yumul, RC;Zeng, W;Stone, IJ;Wo, SW;Dominguez, MM;Cochran, JH;Simmons, JK;Ryan, MC;Lyon, RP;Senter, PD;Levengood, MR;
    Year
    2019
    Journal
    Nat. Biotechnol.
    Application
    enzyme
  • Peptide Microarray-Based Fluorescence Assay for Quantitatively Monitoring the Tumor-Associated Matrix Metalloproteinase-2 Activity
    Author
    Jian, M;Su, M;Gao, J;Wang, Z;
    Year
    2019
    Journal
    Sensors and Actuators B: Chemical
    Application
    enzyme
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