Journal Article

PreJuSER-30237

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Purification of recombinantly expressed human cluster determinant 4 cytoplasmatic domain

Preußer, A. ; Jonas, G. ; Willbold, D.FZJ*

2003
Science Direct New York, NY [u.a.]

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Please use a persistent id in citations: doi:10.1016/S1570-0232(02)00731-6

Abstract: 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 functional without any specific refolding steps. The yield of the described purification procedure was similar to5 mg peptide per liter culture volume. (C) 2002 Elsevier Science B.V. All rights reserved.

Keyword(s): J ; purification (auto) ; Escherichia coli (auto) ; cluster determinant 4 (auto)

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biologische Strukturforschung (IBI-2)

Research Program(s):

1. Neurowissenschaften (L01)

Appears in the scientific report 2003

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