1. Measured by its ability to cleave the fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2. The specific activity is > 1,000 pmoles/min/µg. (Activation description: The proenzyme needs to be activated by APMA for an activated form) 2. Measured by its binding ability in a functional ELISA. Immobilized Human MMP-2 at 2 μg/ml (100 μl/well) can bind Human TIMP2 hFc, the EC50 of Human TIMP2 hFc is 6.0-30.0 ng/mL.

MMP-2 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 72 kDa and the accession number is A0A024R6R4.

Human

HEK293 Cells

TBE-1,MONA,MMP-II,MMP-2,matrix metallopeptidase 2,CLG4A,CLG4

A DNA sequence encoding the native human MMP2 (NP_004521.1) (Met 1-Cys 660) was expressed and purified. Predicted N terminal: Ala 30

≥ 90 % as determined by SDS-PAGE ≥ 90 % as determined by SEC-HPLC.

A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

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 a 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.