A Disintegrin and Metalloproteinase with Thrombospondin 7（ADAMTS7）is a secreted zinc-dependent metalloproteinase belonging to the ADAMTS family, characterized by an N-terminal metalloproteinase domain, disintegrin-like module, and multiple thrombospondin type 1 repeats. Primarily expressed in cardiovascular tissues, skeletal muscle, and cartilage, ADAMTS7 exerts proteolytic functions by cleaving extracellular matrix (ECM) components, such as aggrecan and versican, thereby regulating ECM remodeling. Emerging evidence highlights its critical role in atherosclerosis: it promotes vascular smooth muscle cell (VSMC) migration and proliferation, accelerates plaque formation, and correlates with increased cardiovascular disease risk. Additionally, ADAMTS7 participates in osteoarthritis pathogenesis by degrading cartilage matrix proteins. As a multifunctional protease, it serves as a potential therapeutic target for cardiovascular and musculoskeletal disorders. ADAMTS7 interacts with COMP, likely forming a complex to modulate ECM homeostasis and tissue remodeling processes.Thus a functional ELISA assay was conducted to detect the interaction of recombinant mouse ADAMTS7 and recombinant rat COMP. Briefly, ADAMTS7 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to COMP-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST and incubated for 1h with anti-ADAMTS7 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 mouse ADAMTS7 and recombinant rat COMP was shown in Figure 1, the EC50 for this effect is 0.193µg/mL.