Sentence examples for by immunoaffinity chromatography using from inspiring English sources
HSP70 purification was carried out by immunoaffinity chromatography using adenosine di-phosphate (ADP-agarose column) and the characterization of the purified protein was done using western blotting by mouse monoclonal anti-HSP70.
To this aim the 27 kDa AP protein was purified by immunoaffinity chromatography using the anti-AP mAb.
Recombinant p53 was purified by immunoaffinity chromatography using antibody PAb240 and then coupled to CNBr-activated Sepharose 4B.
After 48 h, the cells were lysed in RIPA buffer and TRIM32 was purified by immunoaffinity chromatography using 9E10-conjugated Protein G Sepharose beads.
Serum samples were cleared of the 14 most abundant major proteins by immunoaffinity chromatography using Human-14® immunoaffinity columns according to the manufacturer's protocol.
Hemichannels were purified by immunoaffinity chromatography using the carboxyl terminal epitope tag in a non-ionic detergent, OG, which maintains the hexameric structure of the hemichannel and its channel function [ 19, 20].
As part of SEAD, blood and urinary TSH and T4 were measured by the Ultramicro Immunodiagnostics Laboratory at the National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health (Bethesda, MD), by recycling immunoaffinity chromatography using an array of capillary immunoaffinity columns packed with antibody-coated glass beads (Phillips 2001).
Total IgG preparations were purified from each sample by protein G immunoaffinity chromatography using 1 ml HiTrap™ protein G fast flow columns (GE Healthcare) following the manufacturer's guidelines and stored at −80°C.
Recombinant envelope proteins were purified from growth conditioned cell culture media and subjected to immunoaffinity chromatography, using a monoclonal antibody specific for the HSV-1 flag epitope.
In addition, all recombinant factor V molecules that are purified employing immunoaffinity chromatography using a monoclonal antibody to factor V are fully active using the experimental protocol described here [as demonstrated by additional experiments using gel electrophoresis and a polyclonal antibody to factor V (not shown)].
It has several advantages over the conventional biochemical methods, such as immunoprecipitation and/or immunoaffinity chromatography, used for the purification of various glycoconjugates.
