The ADP-ribosylation factor 5 (ARF5) is a member of the ARF family of small GTPases, which play critical roles in intracellular vesicular trafficking, organelle structure, and membrane dynamics. As a Class II ARF protein, ARF5 cycles between inactive GDP-bound and active GTP-bound states, regulating cargo transport between the Golgi apparatus and plasma membrane. It is implicated in maintaining Golgi integrity, facilitating secretory pathways, and modulating lipid metabolism. ARF5 antibodies are essential tools for studying these functions, enabling detection and localization of ARF5 in cells or tissues via techniques like Western blotting, immunofluorescence, and immunohistochemistry. Researchers use these antibodies to explore ARF5's role in physiological processes (e.g., cytokinesis, cell adhesion) and pathological conditions, including cancer metastasis and neurodegenerative diseases linked to trafficking defects. Commercial ARF5 antibodies are typically raised against specific epitopes, such as recombinant human ARF5 protein fragments, and validated for specificity using knockdown or knockout controls. Their applications extend to drug discovery, particularly in targeting ARF5-associated pathways in tumors. However, variability in antibody performance across experimental models requires careful validation. Studies using ARF5 antibodies continue to uncover its regulatory interplay with ARF-GEFs/GAPs and effector molecules, advancing understanding of membrane trafficking networks.