[Expression of recombinant human Flt3 ligand in Escherichia coli and its purification and characterization]

[Expression of recombinant human Flt3 ligand in Escherichia coli and its purification and characterization] Research Abstract Details 

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[Expression of recombinant human Flt3 ligand in Escherichia coli and its purification and characterization] Abstract Text:

W Zheng,J Liu,X ,X Pei,Z Sun,

OBJECTIVE: To establish a highly efficient expression system of recombinant human Flt3 ligand (rhFL) in E. coli and a suitable purification method of the expressed products. METHOD: Human FL encoding cDNA was introduced into pProEXHT plasmid to express a 6 x His-FL fusion protein in E. coli. The fusion protein expressed in inclusion body was isolated, solubilized and refolded, and then purified by chromatography on a metal-chelating affinity column (MCAC). Its activity was detected by stimulating the proliferation of CD(34)(+) cells. RESULT: The amount of rhFL expressed was about 15% of total bacterial proteins and the purity of rhFL was 90% after MCAC. The combination of rhFL, granulocyte colony-stimulating factor and erythropoietin could stimulate CD(34)(+) cells to a 400 fold expansion. CONCLUSION: The purified rhFL had a potent activity to stimulate hematopoietic stem cells to expanse in vitro.

[Expression of recombinant human Flt3 ligand in Escherichia coli and its purification and characterization] Publishing Authors By Initials

W Zheng,J Liu,X ,X Pei,Z Sun,

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[Expression of recombinant human Flt3 ligand in Escherichia coli and its purification and characterization] Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Zhonghua xue ye xue za zhi = Zhonghua xueyexue zaz

VOLUME: 22

Page Numbers: 306-9

Journal Abbreviation: Zhonghua Xue Ye Xue Za Zhi

ISSN: 0253-2727

DAY: 5

MONTH: Jun

YEAR: 2001

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LANGUAGE: chi

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AFFILIATION: Beijing Red Cross Chaoyang Hospital, Beijing 100020, China.

Country: China

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MEDLINETA: Zhonghua Xue Ye Xue Za Zhi

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