Recombinant Human MMP-2 Protein

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.

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. Immobilized human MMP2 at 10 μg/mL (100 μl/well) can bind human TIMP2/Fc. 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)

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.