Recombinant E.Coli Dnak Substr

Purification of the Extracellular Domain of the Epidermal Growth Factor Receptor Produced by Recombinant Baculovirus-Infected Insect Cells in a 10-L R

with a recombinant baculovirus that carries a DNA insert encoding for the entire extracellular domain, including the N-terminal signal sequence.

Use of B-PER lysis reagent to purify recombinant proteins tagged with His6 or maltose binding protein

our extensive experience with B-PER for isolating fusion proteins in which the fusion partner is either IPIII-His (an internal protein of bacteriophage T4 with a His tag at the C-terminus)or MBP (the E.coli maltose binding protein).The two cases illustrate

Expression and Purification of Recombinant Human Progesterone Receptor in Baculovirus and Bacterial Systems

Human progesterone receptor (PR) is a member of the nuclear hormone receptor superfamily of transcriptional activators, which share a common modular structure consisting of a C-terminal ligand-binding domain (LBD), a highly conserved