This study was designed to identify one of the main components of venomous secretions of the endoparasitic wasp Asobara tabida. By using electrophoretic methods, partial amino acid sequencing and immunostaining, we demonstrated the presence of an aspartylglucosaminidase (AGA)-like protein in the venom of this insect. The enzyme had a polymeric conformation and was formed of 30 and 18 kDa subunits. The relative positions of several amino acids involved in substrate binding and catalytic activity of known AGA-proteins, which are usually lysosomal enzymes, were conserved in the NH2-terminal ends of these subunits. Antibodies raised against human AGA recognized the two subunits of the protein and a 44 kDa protein, suggesting the presence of a precursor molecule of the enzyme in the venom. However, no reliable measurement of the AGA activity could be performed on the venom extracts, which could be explained by the fact the enzyme would be stored in the reservoir of the venom apparatus under an inactive form. These results constitute the first description of an AGA-like protein in an insect venom and are discussed with respect to the knowledge acquired on lysosomal and venom enzymes. Biochemistry; Proteins Asobara tabida (Braconidae); Enzymes; Aspartylglucosaminidase like protein; Identification & isolation from venom extracts; Toxins and venoms none