Expression and purification of recombinant human chemokine SDF-1β in E. coli

郑红; 朱锡华

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Expression and purification of recombinant human chemokine SDF-1β in E. coli

Updated：2026-03-12

- Expression and purification of recombinant human chemokine SDF-1β in E. coli
- Expression and purification of recombinant human chemokine SDF-1β in E. coli
- 解放军医学杂志（英文版） 2002年第1期页码：24-28
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  中图分类号： R346
- 纸质出版：2002
- Accepted：
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Expression and purification of recombinant human chemokine SDF-1β in E. coli[J]. 解放军医学杂志（英文版）, 2002,(1):24-28.

[1]郑红,,,,,,,,,,朱锡华.Expression and purification of recombinant human chemokine SDF-1β in E. coli[J].Journal of Medical Colleges of PLA,2002(01):24-28.
Expression and purification of recombinant human chemokine SDF-1β in E. coli[J]. 解放军医学杂志（英文版）, 2002,(1):24-28. DOI：

[1]郑红,,,,,,,,,,朱锡华.Expression and purification of recombinant human chemokine SDF-1β in E. coli[J].Journal of Medical Colleges of PLA,2002(01):24-28. DOI：

摘要

Abstract

<正>Objective: To obtain recombinant human SDF-1β expressed in E. coli and purify SDF-lfi with bio-logical activity from the bacterium. Methods: A thioredoxin-SDF-1β fusion protein （26×103） composed of230 amino acid residues was expressed in E. coli AD494 （DE3）pLysS under the induction of IPTG whenpET32a（ + ）-SDF-1β was used as an expression vector. Purified SDF-lfi was produced through following pro-cedures: Bacteria lysis

metal-chelated affinity chromatography （MAC）

enterokinase digestion to separateSDF-lfi from fusion protein

cation exchange chromatography （CEC） and reverse-phase high performance liq-uid chromatography （RP-HPLC）. Western blot with anti-SDF-1β monoclonal antibody （mAb）

N-terminalamino acid sequencing

ligand-binding assay and cytosensor/microphysiometry were used to investigate thebiochemical characters and biological activities of the purified SDF-1β. Results: From 10% to 15% of totalbacterium protein was expressed as fusion protein. Approximately 400 fig purified SDF-1β (7. 8?

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