A modified tandem affinity purification tag technique for the purification of protein complexes in mammalian cells

被引：47

作者：

Drakas, R ^{[1
]}

Prisco, M ^{[1
]}

Baserga, R ^{[1
]}

机构：

[1] Thomas Jefferson Univ, Kimmel Canc Ctr, Philadelphia, PA 19107 USA

来源：

PROTEOMICS | 2005年 / 5卷 / 01期

关键词：

biotinylation; insulin receptor substrate-1; tandem affinity purification tag technique;

D O I：

10.1002/pmic.200400919

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The tandem affinity purification (TAP) tag technique has been used with success to identify under nondenaturing conditions protein complexes in yeast. The technique can be used in mammalian cells, but we found that the original technique does not yield enough recovery for the identification of proteins when mammalian cells growing in monolayer have to be used. We present here a modified TAP tag technique that allows sufficient recovery of proteins from mouse fibroblasts growing in monolayer cultures. The recovery allows protein identification by mass spectrometry.

引用

页码：132 / 137

页数：6

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