Cloning and expression of rat heme oxygenase 1 in E.coli / 吉林大学学报(医学版)
Journal of Jilin University(Medicine Edition)
;
(6)2006.
Article
in Chinese
| WPRIM
| ID: wpr-590342
ABSTRACT
Objective To clone the rat heme oxygenase-1(RHO-1) from rat spleen and express RHO-1 in E.coli BL-21.Methods The total RNA was extracted from rat spleen and amplified by reverse transcription polymerase chain reaction(RT-PCR).PCR products were cloned into pMD18-T(TA)vector followed by DNA sequencing.RHO-1 cDNA fragments in TA vector were subcloned into the prokaryotic expression vector pET28a(+).The recombinant pET28a(+)/RHO-1(rRHO-1) plasmid was transformed into E.coli.The rRHO-1 was induced with IPTG and characterized by SDS-PAGE.Results The cloned RHO-1 gene was composed of 870 nucleotides,and was accordance with the sequence reported in GenBank.The prokaryotic expression vector was constructed successfully.The RHO-1 protein was successfully expressed in E.coli.Conclusion The prokaryotic expression vector of rRHO-1 has been constructed,and the fusion protein has been successfully expressed.
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Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
Journal of Jilin University(Medicine Edition)
Year:
2006
Type:
Article
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