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Fig. 1 | BMC Biotechnology

Fig. 1

From: Novel prokaryotic expression of thioredoxin-fused insulinoma associated protein tyrosine phosphatase 2 (IA-2), its characterization and immunodiagnostic application

Fig. 1

Map of the vector constructed for the expression of TrxIA-2ic in E. coli. The pTrxFus vector was used to create a C-terminal fusion to E. coli thioredoxin. The IA-2ic optimised sequence was inserted into the multiple cloning site of the expression vector and expressed as amino terminal fusion to the E. coli protein thioredoxin. This vector includes an enterokinase (EK) cleavage site that allows release of the native protein from Trx. To drive expression of thioredoxin fusions, pTrxFus uses the pL promoter from the λ bacteriophage and the AspA transcription terminator. Plasmid selection and maintenance is ensured by the presence of a beta-lactamase gene (BLA) that provides ampicillin resistance. SmaI and XbaI sites are indicated at the 3’ and 5’ ends of the IA-2ic sequence. RBS: ribosome binding site

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BMC Biotechnology

ISSN: 1472-6750

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