The pEG-His1 vector was constructed for the expression of toxic gene products in E.coli. To obtain its exceptional tightness prior induction with IPTG, the lac I repressor gene has been included in the vector and is overexpressed in plasmid bearing cells.

Recombinant fusion proteins with a 6xHis tag can be easily and selectively purified using the unique Ni-NTA (nickel-nitrilotriacetic acid) technology. The Ni-NTA affinity matrix shows an optimal binding capacity and a minimized non-specific binding resulting in highly purified and reproducible 6xHis-tagged protein preparations.

Features:

• optimized promoter guarantees excellent expression levels
• very tight expression control due to overexpression of the Lac I repressor
• a convenient MCS allows flexible and easy cloning of the insert
• start codon is provided by an Nde I site
• inserts can be expressed as C-terminal tagged 6xHis fusion proteins for efficient and easy one-step purification of full length proteins by metal-chelate affinity chromatography
• an RGS motive and the proximate Poly(His)-Tag allow detection and/or immunoprecipitation of the expressed protein with commercial anti-RGS and anti-His antibodies