Matrix Metalloproteinase 7 (MMP7) is a member of the matrix metalloproteinases (MMPs) family which are zinc and calcium dependent endopeptidases. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site. MMP-7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and can degrade a variety of extracellular matrix substrates and other substrates and plays important regulatory roles in many human pathophysiological processes.Besides,Matrix Metalloproteinase 2 (MMP2) has been identified as an interactor of MMP7, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human MMP7 and recombinant human MMP2. Briefly, biotin-linked MMP7 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100μl were then transferred to MMP2-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37℃. Finally, add 50μl stop solution to the wells and read at 450nm immediately. The binding activity of MMP7 and MMP2 was shown in Figure 1, the EC50?for this effect is 0.30ug/mL.