Meprin A Alpha (MEP1a) is a zinc-dependent metalloprotease belonging to the astacin family (M12) and plays a crucial role in extracellular matrix (ECM) remodeling, cell adhesion, and inflammation. It is primarily expressed in the kidney, intestine, and immune cells, where it cleaves substrates such as collagen, fibronectin, and cytokines, influencing tissue repair and disease progression. MEP1A exists in both membrane-bound and secreted forms, regulating processes like fibrosis, cancer metastasis, and inflammatory responses. Besides,Trefoil Factor 2 (TFF2) has been identified as an interactor of MEP1a, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse MEP1a and recombinant mouse TFF2. Briefly, MEP1a was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to TFF2-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST and incubated for 1h with anti-MEP1a 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 MEP1a and recombinant mouse TFF2 was shown in Figure 1, the EC50 for this effect is 0.452 µg/mL.