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자료유형
학술저널
저자정보
Ra Mi Lee (건국대학교) Rae Hyung Ryu (건국대학교) Seong Won Jeong (건국대학교) Soo Jin Oh (과학기술연합대학원대학교) Hue Huang (University of California) Jin Soo Han (건국대학교) Chi Ho Lee (건국대학교) C. Justin Lee (과학기술연합대학원대학교) Lily Yeh Jan (University of California) Sang Min Jeong (건국대학교)
저널정보
한국실험동물학회 Laboratory Animal Research Laboratory Animal Research Vol.27 No.2
발행연도
2011.6
수록면
109 - 116 (8page)

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To clone the first anion channel from Xenopus laevis (X. laevis), we isolated a calcium-activated chloride channel (CLCA)-like membrane protein 6 gene (CMP6) in X. laevis. As a first step in gene isolation, an expressed sequence tags database was screened to find the partial cDNA fragment. A putative partial cDNA sequence was obtained by comparison with rat CLCAs identified in our laboratory. First stranded cDNA was synthesized by reverse transcription polymerase-chain reaction (RT-PCR) using a specific primer designed for the target cDNA. Repeating the 5’ and 3’ rapid amplification of cDNA ends, fulllength cDNA was constructed from the cDNA pool. The full-length CMP6 cDNA completed via 5’- and 3’-RACE was 2,940 bp long and had an open reading frame (ORF) of 940 amino acids. The predicted 940 polypeptides have four major transmembrane domains and showed about 50% identity with that of rat brain CLCAs in our previously published data. Semi-quantification analysis revealed that CMP6 was most abundantly expressed in small intestine, colon and liver. However, all tissues except small intestine, colon and liver had undetectable levels. This result became more credible after we did real-time PCR quantification for the target gene. In view of all CLCA studies focused on human or murine channels, this finding suggests a hypothetical protein as an ion channel, an X. laevis CLCA.

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Materials and Methods
Results
Discussion
Acknowledgments
References

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UCI(KEPA) : I410-ECN-0101-2013-510-000557319