Procollagen Lysine-2-Oxoglutarate-5-Dioxygenase 2 (PLOD2), also known as lysyl hydroxylase 2 (LH2), is a pivotal enzyme in collagen biosynthesis.Localized to the endoplasmic reticulum, PLOD2 catalyzes the hydroxylation of lysine residues within procollagen telopeptides—an essential post-translational modification that enables the formation of stable collagen cross-links. These cross-links are critical for maintaining the structural integrity and mechanical stability of connective tissues. Dysregulation of PLOD2 has been implicated in pathological conditions such as Bruck syndrome(a connective tissue disorder characterized by bone fragility) and various cancers, where it contributes to increased tissue stiffness and enhanced tumor cell migration. Notably, PLOD2 forms a direct functional interaction with FK506 Binding Protein 10 (FKBP10)​, which promotes PLOD2 dimerization—a key mechanism that enhances its enzymatic activity and ensures efficient collagen maturation.Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human PLOD2 and recombinant mouse FKBP10 . Briefly, biotin-linked PLOD2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100µl were then transferred to FKBP10-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 PLOD2 and FKBP10 was shown in Figure 1, the EC50 for this effect is 0.45 µg/mL.