Abcam, ab280347, Recombinant human MMP2 protein (Active)

Size: 10µg / 50µg / 100µg / 250µg
Recombinant human MMP2 protein (Active) is a Human Full Length protein in the 110 to 660 aa range with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for Functional studies. The predicted molecular weight of ab280347 protein is 63 kDa. - Save time and ensure accurate results - use our recombinant MMP-2 protein as a control - Optimal protein bioactivity, stability and reproducibility - Available in different sizes to fit your experimental needs
Key facts
Purity:>95% SDS-PAGE,
Endotoxin level:<0.005 EU/µg,
Expression system:HEK 293 cells,
Tags:Tag free,
Applications:FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Fully active determined by its ability to cleave human MMP2 fluorogenic peptide substrate (MCa-PLGL-Dpa-AR-NH2.,
Accession:P08253,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.4Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

Product details:
Ensure the validity of your result using our recombinant human MMP2 protein ab280347 as a control.
The ab280347 MMP2 protein is sourced from HEK293 cells and can be used as a positive control in SDS-PAGE, mass spectrometry and HPLC.
Check out our protein gel staining guide for SDS-PAGE
Premium Bioactive Protein range
The ab280347 MMP2 protein is part of the premium bioactive protein range which are ideal for preclinical cell culture and functional studies. These recombinant proteins are of the highest activity, purity, and consistency, meeting rigorous biophysical characterization.
More premium bioactive proteins can be found

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The MMP-2 protein also known as matrix metalloproteinase-2 or gelatinase A is an enzyme involved in the breakdown of extracellular matrix components. It plays a critical role in tissue remodeling and cell migration. Comprised of a molecular weight of approximately 72 kDa this metalloproteinase is secreted as an inactive proenzyme that requires activation. MMP2 is expressed in various tissues including the brain heart and blood vessels where it contributes to normal physiological processes and pathological conditions.
Biological function summary
Matrix metalloproteinase-2 is mainly involved in the degradation of type IV and V collagens gelatin and fibronectin. As part of the metalloproteinase family it works alongside other MMPs to maintain tissue homeostasis and repair. MMP-2 forms part of a complex network that ensures the timely degradation of matrix components balancing synthesis and breakdown. It remains regulated by tissue inhibitors of metalloproteinases (TIMPs) preventing excessive degradation that could lead to tissue damage.
Pathways
MMP-2 plays a significant role within the extracellular matrix (ECM) remodeling and angiogenesis pathways. It interacts with various proteins including integrins and TIMP-2 to modulate cellular behaviors such as migration and invasion. MMP-2 contributes to processes like wound healing and embryonic development through its involvement in ECM degradation and new tissue formation.
Matrix metalloproteinase-2 is linked to cancer progression and cardiovascular diseases. In cancer abnormal MMP-2 activity facilitates tumor invasion and metastasis by breaking down matrix barriers. Increased MMP-2 expression associates with poor prognosis in cancers like breast and prostate. In cardiovascular diseases such as atherosclerosis it contributes to plaque destabilization and vascular remodeling. The imbalance in MMP-2 activity and its regulation by proteins like TIMP-1 are involved in the pathology of these disorders.