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Serine proteases are a class of proteolytic enzymes that play regulatory roles in protein processing and degradation. Previous molecular characterization of a mosquito serine protease, AgSp24D, indicated that it is a nondigestive chymotrypsin-like enzyme that is developmentally regulated, and is strongly expressed during the adult stage. Since the biological role of AgSp24D is unknown, we were interested in further characterizing the gene product. Thus, a polyclonal antibody against an AgSp24D fusion protein was produced. The antiserum recognizes two polypeptides of 50 kDa and 60 kDa in immunoblots of whole body homogenates from adult mosquitoes. Western blot analysis showed the strongest signal in a homogenate of thoraces. The signal was also detected in the head, midgut, cuticle plus fat body, ovary, and Malpighian tubules. No signal was detected in the hemolymph. A comparison of Anopheles gambiae, Aedes aegypti, Armigeres subalbatus, Drosophila melanogaster, Acheta domesticus, Manduca sexta, and bovine cardiac muscle and skeletal muscle showed that the polyclonal antibody cross-reacted to similarly sized polypeptides in all samples.