Matrix Metalloproteinase 7 (MMP7), also known as matrilysin, is a small secreted protease belonging to the MMP family. It plays key roles in extracellular matrix degradation, tissue remodeling, wound healing, and cancer progression by cleaving substrates like collagen, fibronectin, and proteoglycans. Unlike other MMPs, MMP7 lacks a hemopexin domain but remains highly active in processing cytokines and growth factors. It is overexpressed in various cancers and inflammatory diseases. MMP7 activity is tightly regulated by Tissue Inhibitor of Metalloproteinases 1 (TIMP1), which binds to MMP7 in a 1:1 stoichiometry to inhibit its proteolytic function.To detect the activity of recombinant MMP7, a functional ELISA assay was performed to evaluate the interaction between recombinant human IMMP7 and recombinant human TIMP1.Briefly, MMP7 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to TIMP1-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST and incubated for 1h with anti-MMP7 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37℃, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37℃. Finally, add 50 µL stop solution to the wells and read at 450/630nm immediately. The binding activity of recombinant human IMMP7 and recombinant human TIMP1 was shown in Figure 1, the EC50 for this effect is 0.49 µg/mL..