Expression and Purification of Soluble STAT5b/STAT3 Proteins for SH2 Domain Binding Assay.
Expression and Purification of Soluble STAT5b/STAT3 Proteins for SH2 Domain Binding Assay.
复制标题
用于 SH2 结构域结合测定的可溶性 STAT5b/STAT3 蛋白的表达和纯化。
DOI：
--
复制
发表时间：
2017
影响因子：
--
通讯作者：
K. Takakuma
中科院分区：
文献类型：
--
作者：
A. Asai;K. Takakuma
当一个大的疏水全长蛋白在细菌中表达时，在可溶性部分获得重组蛋白通常是具有挑战性的。克服这一挑战的一种方法是表达在保持生物活性的同时提高溶解度的缺失突变体。在本章中，我们描述了一种表达STAT5b和STAT3蛋白截短形式的方案，这些蛋白是可溶性的，并保留了sh2介导的磷酸化酪氨酸肽识别活性。
When a large hydrophobic full-length protein is expressed in bacteria, it is often challenging to obtain recombinant proteins in the soluble fraction. One way to overcome this challenge is expression of deletion mutants that have improved solubility while maintaining biological activity. In this chapter, we describe a protocol for expression of truncated forms of STAT5b and STAT3 proteins that are soluble and retain SH2-mediated activity for phospho-Tyr peptide recognition.