can modulate host immune mechanisms through excretory-secretory products (ESP). As one of the components of ESP, it is unknown whether Abelson tyrosine protein kinase (Abl) is involved in parasite-host immune interaction. To investigate the immunoregulatory function of Abl in , we cloned and expressed the gigantica Abl protein and assessed its effect on specific immune functions of buffalo peripheral blood mononuclear cells (PBMCs). Recombinant Abelson tyrosine protein kinase (rAbl) was expressed in . Western blot analysis was performed to assess the reactivity of anti-rAbl antibodies with rAbl, serum from -infected buffalo, and excretion and secretion products of . Immunohistochemical analysis was conducted to determine the localization of Abl in tissues from larval stages and adult worms of . Furthermore, immunofluorescence analysis was utilized to evaluate the binding ability of the rAbl protein to buffalo peripheral blood mononuclear cells (PBMCs), as well as to investigate the effects of varying concentrations of rAbl protein (5, 10, 20, 40, and 80 μg/mL) on the functional responses of PBMCs. Anti-rAbl antibodies specifically recognize rAbl, serum from buffalo infected with , and ESP. rAbl is localized in the cecum and capsule of juvenile worms, as well as in the testis and viellaria of adult worms. Additionally, rAbl enhances cell proliferation, migration, nitric oxide (NO) production, and phagocytosis, while also increasing the transcription levels of cytokines (IFN-γ, IL-12, TNF-α, IL-4, IL-10, and TGF-β). The results indicate that rAbl can influence the immune function of PBMCs. Further investigation into the immunomodulatory properties of the rAbl protein will enhance our understanding of the immune interaction mechanisms between trematodes and their hosts.