Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology · 2007
[Expression of human anti-rabies Scds-Fv fusion protein in E.coli].
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Cai Kun, Wang Hui, Shi Jing, Bao Shi-zhong, Hou Xiao-jun, Yin Jun
Аннотация
AIM: To express the anti-rabies MBP-ScdsFv fusion protein in E.coli and identify it's activity assay.
METHODS: A full length of ScdsFv gene was Cloned into prokaryotic vector pMAL-p2x by recombinant DNA, Then the recombinant plasmid pMAL-ScdsFv was transformed to E.coli ER2566 for expression and induced by IPTG. The fusion protein was digested by Factor Xa, purified by Ni(+) and amylose resin affinity chromatography and Identified by SDS-PAGE and Western blot. The binding activity of the protein was determined by ELISA.
RESULTS: Recombinant plasmid pMAL-ScdsFv was successfully constructed. The anti-rabies ScdsFv protein which was digested by Factor Xa and purified by Ni-NTA and amylose resin affinity chromatography had good binding activity and high stability.
CONCLUSION: The anti-rabies ScdsFv protein is of good binding activity and high stability, and it can be used for the immune therapy.
METHODS: A full length of ScdsFv gene was Cloned into prokaryotic vector pMAL-p2x by recombinant DNA, Then the recombinant plasmid pMAL-ScdsFv was transformed to E.coli ER2566 for expression and induced by IPTG. The fusion protein was digested by Factor Xa, purified by Ni(+) and amylose resin affinity chromatography and Identified by SDS-PAGE and Western blot. The binding activity of the protein was determined by ELISA.
RESULTS: Recombinant plasmid pMAL-ScdsFv was successfully constructed. The anti-rabies ScdsFv protein which was digested by Factor Xa and purified by Ni-NTA and amylose resin affinity chromatography had good binding activity and high stability.
CONCLUSION: The anti-rabies ScdsFv protein is of good binding activity and high stability, and it can be used for the immune therapy.