The pEG-His1 vector was constructed for the expression of toxic gene products in E. coli. To obtain its exceptional tightness prior to 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.
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 NdeI site
Inserts can be expressed as C-terminal tagged 6xHis fusion proteins for 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