Datx2 was identified as the Drosophila homolog of SCA-2, a human gene associated to a neurodegenerative disorder caused by an expansion of a polyglutamine stretch in the encoded protein ataxin-2 (ATX-2). Based on sequence similarity, Da2bp1 also was assigned as the Drosophila homolog of a human protein, named A2BP1, which was initially identified as an ataxin-2 binding protein. Both proteins contain RNA recognition motifs, which is in accord with evidences of their involvement in RNA metabolism.  While ATX-2 is broadly expressed, A2BP1 was detected in muscular tissues and brain. Therefore, although the functions of both proteins are still poorly understood it is possible that interactions between the two proteins could contribute to the tissue restriction of SCA2 pathology. Both proteins are evolutionarily conserved, with orthologs present in fungi to humans. To contribute to the understanding of the cellular role of ataxin-2, our laboratory is working in the molecular and cellular characterization of the Drosophila orthologs, Datx2 and Da2bp1.  Datx2 gene expresses two transcripts, which codify proteins differing only in the amino-terminal, which is 61 amino-acids longer in isoform named Datx2. So far, the only functional information available for Datx2 gene indicates that it is a dosage-sensitive regulator of actin filament formation, and that its lack of function causes female sterility, loss or degeneration of tissues, and lethality. For Da2bp1 there is virtually no information, besides the sequence of a full-length cDNA (ID#LD15974).  We report here the generation of polyclonal antibodies against Datx2 and Da2bp1. The antibodies were generated against the protein fragments expressed in fusion with a tag of six histidine residues (His-tag), using a pQE vector. From Datx2, we expressed the 60 amino acid residues (position 1 to 61), specific for this isoform, and for Da2bp1, we expressed 62 amino acid residues (positions 272 to 334) of the protein deduced from the full-length cDNA.  Results of immunoblots of Drosophila S2 cell extracts probed with the affinity-purified antibodies revealed proteins with the expected masses: ~ 120 kDa, for Datx2, and ~85 kDa, for Da2bp1.