کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1216141 | 1494161 | 2009 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expression and purification of soluble E-Syt2: Low protein stability impedes tag removal
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Expression and purification of soluble E-Syt2: Low protein stability impedes tag removal Expression and purification of soluble E-Syt2: Low protein stability impedes tag removal](/preview/png/1216141.png)
چکیده انگلیسی
Affinity tags are valuable tools for high-throughput protein isolation in automated screenings or downstream processing approaches and are also widely used in laboratory applications for quick and easy access to many proteins. Here, we describe the preparative purification of soluble extended synaptotagmin 2 (rE-Syt2) at bench scale for basic structural and functional studies. Due to the low protein stability, a classical purification procedure without affinity tag was more powerful than isolation of His(6)-tagged rE-Syt2 and subsequent proteolytic tag-removal. Furthermore, expression analysis of truncated rE-Syt2 variants suggested a concept of interdependent-domain organization in proteins containing multiple C2 domains.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Chromatography B - Volume 877, Issues 16–17, 1 June 2009, Pages 1643–1650
Journal: Journal of Chromatography B - Volume 877, Issues 16–17, 1 June 2009, Pages 1643–1650
نویسندگان
Gerhard J. Groer, Martin Haslbeck, André Gessner,