Purification of recombinantly expressed human cluster determinant 4 cytoplasmic domain.

@article{Preusser2003PurificationOR,
  title={Purification of recombinantly expressed human cluster determinant 4 cytoplasmic domain.},
  author={A. Preusser and Gesa Jonas and Dieter Willbold},
  journal={Journal of chromatography. B, Analytical technologies in the biomedical and life sciences},
  year={2003},
  volume={786 1-2},
  pages={39-44}
}
A DNA fragment coding for the human CD4 cytoplasmic domain (residues 394-433) was cloned into the pET15b expression vector. The resulting plasmid was used for synthesis of the polyhistidine-tagged 5.10(3) M(r) CD4 peptide in Escherichia coli BL21(DE3)Star. The CD4 cytoplasmic domain was purified under denaturing and reducing conditions by a two-step procedure using immobilized metal affinity chromatography and gel permeation chromatography. The purified CD4 cytoplasmic domain is soluble and… CONTINUE READING