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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
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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 domestic us, Manduca sexta, and bovine cardiac muscle and skeletal muscle showed that the poly clonal antibody cross-reacted to similarly sized polypeptides in all samples.
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