Purification and Characterization of Recombinant Human SNX9 Protein Expressed in E.coli

China Biotechnology

2008, Vol. 28

Issue (8): 11-17 DOI:

Purification and Characterization of Recombinant Human SNX9 Protein Expressed in E.coli

YOU Xiao-Juan Jin-song LIU

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Abstract

SNX9 is a novel SNX family protein，which plays important roles in protein sorting and transporting. The prokaryotic expression vector pET-SNX9 construct was transformed into E.coli BL21(DE3) cell and induced by IPTG. The induced fusion protein (SNX9) was expressed successfully in soluble form. SDS-PAGE indicated that the molecular weight of SNX9 was about 70 kD, and the recombinant protein was confirmed by western blotting. After affinity and gel filtration chromatography purification, the purity of SNX9 could reach over 95%. Gel filtration elution volume suggested that SNX9 existed as a dimer in solution. Homogeneity was further confirmed by Native-PAGE and Dynamic Light Scattering (DLS) experiments. In the thermo stability experiment, SNX9 was stable below 15 ℃ relatively. All these information paved the way for future structural and functional study of SNX9.

Key words： Sorting Nexin 9(SNX9) soluble expression purification homogeneity

Received: 03 March 2008 Published: 25 August 2008

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Corresponding Authors: Jin-song LIU

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Cite this article:

YOU Xiao-Juan Jin-song LIU. Purification and Characterization of Recombinant Human SNX9 Protein Expressed in E.coli. China Biotechnology, 2008, 28(8): 11-17.

URL:

https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2008/V28/I8/11

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