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.