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Chapter title |
Purification of Polyhistidine-Tagged Proteins.
|
---|---|
Chapter number | 14 |
Book title |
Protein Chromatography
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Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6412-3_14 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6410-9, 978-1-4939-6412-3
|
Authors |
Sinéad T. Loughran, Ronan T. Bree, Dermot Walls |
Editors |
Dermot Walls, Sinéad T. Loughran |
Abstract |
His-tagging is the most widespread and versatile strategy used to purify recombinant proteins for biochemical and structural studies. Recombinant DNA methods are first used to engineer the addition of a short tract of poly-histidine tag (His-tag) to the N-terminus or C-terminus of a target protein. The His-tag is then exploited to enable purification of the "tagged" protein by Immobilized Metal Affinity Chromatography (IMAC). Here, we describe efficient procedures for the isolation of highly purified His-tagged target proteins from an E. coli host using IMAC. |
Mendeley readers
The data shown below were compiled from readership statistics for 120 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 120 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Bachelor | 36 | 30% |
Student > Ph. D. Student | 12 | 10% |
Other | 8 | 7% |
Student > Master | 8 | 7% |
Professor | 3 | 3% |
Other | 11 | 9% |
Unknown | 42 | 35% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 41 | 34% |
Agricultural and Biological Sciences | 14 | 12% |
Engineering | 5 | 4% |
Chemistry | 4 | 3% |
Neuroscience | 3 | 3% |
Other | 8 | 7% |
Unknown | 45 | 38% |