收稿日期: 2010-05-24
修回日期: 2010-05-27
网络出版日期: 2011-03-15
基金资助
国家自然科学基金(30670889,30771193)资助
Screening proteins interacting with hCLP46 using tandem affinity purification
Received date: 2010-05-24
Revised date: 2010-05-27
Online published: 2011-03-15
徐峰 , 穆昕 , 王嵬 , 刘利新 . 串联亲和纯化技术筛选hCLP46 的相互作用蛋白[J]. 中国科学院大学学报, 2011 , 28(2) : 210 -216 . DOI: 10.7523/j.issn.2095-6134.2011.2.011
hCLP46 (human CAP10-like protein46), a novel gene, has been screened out from the cDNA library of MDS-AML Patient’s CD34+ stem cell. For to further studying the biological characteristics of this gene tandem affinity purification (TAP) has been used to isolate proteins which specifically interact with hCLP46, and seven specific protein bands were detected. By using liquid chromatography-mass spectrometry and protein database searching, a series of endoplasmic reticulum chaperones were identified. Two major ER chaperone systems, the BiP/Grp94 and the calnexin (CNX)/ calreticulin (CRT) systems, are important in the maturation of hCLP46.
Key words： crosslinker; tandem affinity purification(TAP); MDS; hCLP46
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