@article{1f7a17a0a1c411ddb6ae000ea68e967b,
title = "The biological activity of a recombinantly expressed (His)(6)-tagged peanut allergen (rAra h 1) is unaffected by endotoxin removal",
abstract = "The application of recombinant (His)(6)-tagged proteins in cell culture assays is associated with problems due to lipopolysaccharide (LPS) contamination. LPS stimulates cells of the immune system, thereby masking antigen-specific activation of T cells. Due to the affinity of LPS for histidine it is associated with difficulties to remove LPS from recombinant (His)(6)-tagged proteins. Here we describe that the Triton X-114 phase separation method can be used to remove LPS from (His)(6)-tagged proteins and that the recombinant proteins retain their biological activity.",
keywords = "Allergens, Antigens, Plant, Basophils, Cells, Cultured, Cloning, Molecular, Dose-Response Relationship, Drug, Glycoproteins, Histamine Release, Histidine, Humans, Interleukin-10, Leukocytes, Mononuclear, Lipopolysaccharides, Plant Proteins, Polyethylene Glycols, Protein Binding, Recombinant Proteins, T-Lymphocytes, Time Factors, Tumor Necrosis Factor-alpha",
author = "Jensen, {Louise Bjerremann} and Torp, {Anna Maria} and Andersen, {Sven Bode} and Skov, {Per Stahl} and Poulsen, {Lars K.} and Knol, {Edward F.} and {van Hoffen}, Els",
year = "2008",
doi = "10.1016/j.jim.2008.02.012",
language = "English",
volume = "335",
pages = "116--20",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier",
number = "1-2",
}