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HITRAPHonesty, Integrity, Trust, Responsibility, Accountability, and Service to People
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(iii) pass the diluted filtrate and then 10-20 mL PBS through the HiTrap column at flow rate of 1 mL per min,
Our [PLA.sub.2] assays were performed on mosquito samples that have been partially enriched using Heparin column chromatography (1ml HiTrap Heparin, Sigma, USA).
Strep-tag II column (5 x 1mL Lot: 10183115) and HiTrap protein G (5 x 1mL Lot: 17-0404-01) were bought from GE Healthcare (Freiburg, Germany).
Fractions containing ST2166 were pooled, dialyzed against the Tris buffer, and then subjected to an anion exchange chromatography using a tandem of three HiTrap Q HP columns equilibrated with the Tris buffer.
HiTrap Mabselect SuRe columns were purchased from GE Healthcare and [C.sub.18] trap column was purchased from Harvard Apparatus (Holliston, MA USA).
Proteins were isolated from an HiTrap Chelating HP column under either native (Figure S1B) or denaturing (8 M urea (Figure S1C)) conditions and eluted using an imidazole gradient, ranging from 10 to 500 mM in an AKTA FPLC protein purification system (GE Healthcare Life Sciences, Australia).
The protein purified from the soluble supernatant by [Ni.sup.2+]-affinity chromatography (HiTrap HP; GE Healthcare Bio-Sciences, Piscataway, NJ, USA) was eluted with Buffer A (20 mM Tris-HCl, 250 mM imidazole, and 0.5 M NaCl, pH 7.9) and dialyzed against a dialysis buffer (20 mM HEPES and 100 mM NaCl, pH 7.0; Buffer B).
Anti-Plexin C1 monoclonal antibodies were purified from hybridoma supernatants on AKTA-Purifier Chromatography (GE, Massachusetts, USA) using protein G affinity column (HiTrap protein G, GE).
The matrix in the HiTrap HP column was balanced with binding buffer (50 mM Na[H.sub.2]P[O.sub.4] pH 7.4, 25 mM NaCl, 10 mM imidazole).
The HiTrap Chelating HP column was purchased from GE Healthcare (Uppsala, Sweden).
Although whole nuclear extracts did not show histone succinylation activity, we found that the strong cation exchange column-binding fraction (HiTrap SP column, 1.0 M KCl-eluted fraction) of nuclear extracts indeed possessed succinylation activity.
Afterwards, the polyclonal antibody against CPS was purified as IgG fraction from the resulted antiserum by affinity chromatography on a HiTrap Protein G column (GE Healthcare).