Verified Samples in WB: RAW264.7, NIH/3T3, Mouse uterus, Rat liver

WB 1:500-1:1000

Polyclonal

IgG

Recombinant Human MMP-2 Protein expressed by E.coli

MMP-2

72 kDa Gelatinase, 72 kDa Type IV Collagenase, CLG4, CLG4A, Gelatinase A, MMP-2, MMP-II, MMP2, MONA, Matrix Metalloproteinase-2, TBE-1

74 kDa

69 kDa-72 kDa

1 mg/mL

Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.

PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4

Antigen Affinity Purification

Cancer, Cell Biology, Cardiovascular, Metabolism

Unconjugated

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.