Overexpression of TrxA::BjMT2 (Thioredoxin::Metallothionein Type 2 from Brassica juncea) Fusion Protein in Escherichia coli and In Vitro Cleavage by TEV Protease

Abstract:

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BjMT2 cDNA clone gene isolated from Brassica juncea was constructed in pETM-20 and expressed in E.coli as a TrxA::BjMT2 fusion protein. After affinity chromatography and cleavage from the TrxA domain, pure BjMT2 protein was obtained which strongly reacted with the thiol reagent monobromobimane. The amino acid sequence determined by mass spectrograph revealed the polypeptide contains 80 amino acids and is full of 8 and 6 cysteines with CC, CXC and C-XX-C motifs clustered near -N and -C terminus, respectively.

Info:

Periodical:

Advanced Materials Research (Volumes 183-185)

Edited by:

Yanguo Shi and Jinlong Zuo

Pages:

947-951

DOI:

10.4028/www.scientific.net/AMR.183-185.947

Citation:

Y. Z. Song et al., "Overexpression of TrxA::BjMT2 (Thioredoxin::Metallothionein Type 2 from Brassica juncea) Fusion Protein in Escherichia coli and In Vitro Cleavage by TEV Protease", Advanced Materials Research, Vols. 183-185, pp. 947-951, 2011

Online since:

January 2011

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$35.00

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