The gene of Bs-Ag2 from Baylisascaris schroederi was amplified, cloned and sequenced. Sequence analysis indicated that the nucleotide sequences of the Bs-Ag2 from adult, L2 and L3 of B. schroederi were completely identical. A homology search performed by BLAST revealed that Bs-Ag2 shared the highest amino acid sequence identity with As16 protein from Ascaris suum (94%). The recombinant Bs-Ag2 proteins can be successfully expressed in Escherichia coli BL21 (DE3). The rBs-Ag2 was used to evaluate their ability to induce immune protective responses in BALB/c mice against L3-challenge infection in a mouse-B. schroederi model. There was a 63.66% reduction (P<0.001) of recovery of larvae compared with that in the control group. Specific anti-Bs-Ag2 antibodies from immune protected mice had significantly higher levels of immunoglobulin G (IgG) (P<0.0001). Our data supported the use of Bs-Ag2 as a potential candidate for vaccination against B. schroederi infection.