Bone Morphogenetic Protein 1 (BMP1) is a metalloprotease that plays a crucial role in extracellular matrix (ECM) remodeling and tissue development. It processes procollagens and other ECM precursors, contributing to bone formation, wound healing, and organogenesis. Unlike other BMP family members, BMP1 lacks osteoinductive activity but is essential for activating TGF-β superfamily proteins, including growth factors involved in skeletal and connective tissue regulation. BMP1 cleaves and inactivates Myostatin (MSTN), a negative regulator of muscle growth, thereby indirectly promoting muscle hypertrophy by reducing MSTN-mediated inhibition of myogenesis.Thus a functional ELISA assay was conducted to detect the interaction of recombinant human BMP1 and recombinant human MSTN. Briefly, BMP1 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to MSTN-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST and incubated for 1h with anti-BMP1 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 BMP1 and recombinant human MSTN was shown in Figure 1, the EC50 for this effect is 0.014 μg/mL.