Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 81, Issue 11, Pages 1857-1861Publisher
WILEY-BLACKWELL
DOI: 10.1002/prot.24364
Keywords
BL21(DE3); E; coli protein expression strain; His-tag affinity purification; LOBSTR
Categories
Funding
- Lundbeck Foundation
- Sapere Aude DFF postdoc grant
- NIH [GM077537]
- Lundbeck Foundation [R54-2010-5657] Funding Source: researchfish
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His-tag affinity purification is one of the most commonly used methods to purify recombinant proteins expressed in E. coli. One drawback of using the His-tag is the co-purification of contaminating histidine-rich E. coli proteins. We engineered a new E. coli expression strain, LOBSTR (low background strain), which eliminates the most abundant contaminants. LOBSTR is derived from the E. coli BL21(DE3) strain and carries genomically modified copies of arnA and slyD, whose protein products exhibit reduced affinities to Ni and Co resins, resulting in a much higher purity of the target protein. The use of LOBSTR enables the pursuit of challenging low-expressing protein targets by reducing background contamination with no additional purification steps, materials, or costs, and thus pushes the limits of standard His-tag purifications. Proteins 2013; 81:1857-1861. (c) 2013 Wiley Periodicals, Inc.
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