Autor: |
B, Frorath, C C, Abney, H, Berthold, M, Scanarini, W, Northemann |
Rok vydání: |
1992 |
Předmět: |
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Zdroj: |
BioTechniques. 12(4) |
ISSN: |
0736-6205 |
Popis: |
Interleukin-6 (IL-6) is one of the most important mediators of the acute phase reaction in liver. For the production of recombinant rat IL-6 in Escherichia coli, a previously isolated cDNA coding for the rat IL-6 was cloned into the modified novel expression vector pGEX-3T. The IL-6 cDNA was highly expressed as a fusion protein with the glutathione S-transferase (GST) at its C-terminus and rat IL-6 at its N-terminus. The GST-IL-6 fusion protein was controlled by a tac-promoter and could be induced very efficiently by isopropyl-beta-D-thiogalactopyranoside. The synthesized GST-IL-6 fusion protein was insoluble and precipitated intracellularly in E. coli. Using an advanced technique, the insoluble protein was solubilized and purified to homogeneity by affinity chromatography using immobilized glutathione in a one-step procedure. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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