VEGF Co-Regulated Chemokine 1 (VCC1), also known as CXC chemokine ligand 17 (CXCL17), is a recently identified secretory protein that functions as both a chemokine and an angiogenic factor. It is primarily expressed in mucosal tissues, particularly in the respiratory and digestive tracts, where it contributes to immune surveillance by recruiting dendritic cells and macrophages. VCC1 demonstrates dual functionality: it promotes angiogenesis through mechanisms synergistic with VEGF while also exerting antimicrobial activities in epithelial barriers. Its expression is often upregulated in inflammatory conditions and various cancers, where it may influence tumor microenvironment formation and immune modulation. Besides,Chemokine C-C-Motif Receptor 8 (CCR8) has been identified as an interactor of VCC1, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human VCC1 and recombinant human CCR8. Briefly, VCC1 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to CCR8-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST and incubated for 1h with anti-VCC1 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 VCC1 and recombinant human CCR8 was shown in Figure 1, the EC50?for this effect is 0.05 μg/mL.