高等学校化学研究 ›› 2011, Vol. 27 ›› Issue (3): 474-477.
WANG Shao-feng1,2, HAN Jia-yu2, FU Xue-qi1* and ZHAO Zhi-zhuang Joe1,2*
WANG Shao-feng1,2, HAN Jia-yu2, FU Xue-qi1* and ZHAO Zhi-zhuang Joe1,2*
摘要: PTPRU is an MAM domain-containing receptor-like protein tyrosine phosphatase. Previous studies have demonstrated an important role of the enzyme in the maintenance of epithelial integrity and in the regulation of the Wnt/?-catenin signaling pathway. To better understand the function of PTPRU, we cloned and expressed the intracellular portion of PTPRU as a GST fusion protein in E. coli cells. We purified the protein to homogeneity and used it to immunize mice for antibody production. The resultant antibody specifically recognized PTPRU over-expressed in the cell line. Western blot analyses demonstrated the partition of truncated forms of PTPRU containing the cadherin-like domain in the Triton X-100-insoluble fraction, and immunofluorescent cell staining revealed the localization of these proteins in punctate intracellular structures. Our data suggest that the cadherin-like domain of PTPRU has a major role in determining its intracellular localization.