التفاصيل البيبلوغرافية
| العنوان: |
Procedures for the analysis and purification of his-tagged proteins. |
| المؤلفون: |
Kneusel RE; Qiagen, Hilden, Germany., Crowe J, Wulbeck M, Ribbe J |
| المصدر: |
Methods in molecular medicine [Methods Mol Med] 1998; Vol. 13, pp. 293-308. |
| نوع المنشور: |
Journal Article |
| اللغة: |
English |
| بيانات الدورية: |
Publisher: Humana Press Country of Publication: United States NLM ID: 101123138 Publication Model: Print Cited Medium: Print ISSN: 1543-1894 (Print) Linking ISSN: 15431894 NLM ISO Abbreviation: Methods Mol Med Subsets: PubMed not MEDLINE |
| أسماء مطبوعة: |
Original Publication: Totowa, N.J. : Humana Press, c1996- |
| مستخلص: |
The heterologous expression of recombinant proteins is a valuable tool in the study of gene expression, and has resulted in the development of many systems to express and purify hybrid proteins. Most of these systems are based on the fusion of the protein of interest with a naturally occurrIng protein (glu-tathione S-transferase, maltose binding protein, or protein A) and using their natural affinity to substrates (glutathione, amylose, or immunoglobulins) coupled to columns in the purification step. Among the main drawbacks with these systems are that the affinity tag may affect protein structure and function, and that it 1s not possible to purify insoluble proteins. |
| تواريخ الأحداث: |
Date Created: 20110311 Date Completed: 20121002 Latest Revision: 20110310 |
| رمز التحديث: |
20240829 |
| DOI: |
10.1385/0-89603-485-2:293 |
| PMID: |
21390850 |
| قاعدة البيانات: |
MEDLINE |
