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Captoq resin

Manufactured by GE Healthcare
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CaptoQ is a protein A affinity resin designed for the purification of monoclonal antibodies and Fc-fusion proteins. The resin utilizes a recombinant protein A ligand that exhibits high binding capacity and mild elution conditions to preserve the activity of the target biomolecules.

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Lab products found in correlation

Hiload 26 60 superdex 75 gel filtration column, by GE Healthcare (1 mentions)

3 protocols using captoq resin

1

Purification and Mass Analysis of Pyrophosphate

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Purification of pyrophosphate from heterocyclization reactions was achieved by passing the reaction mixture through a 5 kDa cut-off protein concentrator. The flow-through was applied to CaptoQ resin (GE Healthcare), washed with 15 column volumes dH2O and pyrophosphate eluted with 1M Na acetate pH 7.0.
Accurate mass measurements were carried out on ABSciex 5600 mass spectrometer with nanospray source. Samples were diluted 50% with ACN and infused at 1ul/min using the inbuilt syringe pump. Negative ionization spectra were collected from 60- 400m/z in MS mode. Masses 176.9 and 178.9 m/z were isolated in Q1, fragmented with collision energy 30V in Q2 and the fragments measured from 50-200m/z on the TOF analyzer. The TOF was externally calibrated with a mixture of Periodate (190.8847 m/z) and sulphanilic acid (172.0074 m/z)
Koehnke J., Mann G., Bent A.F., Ludewig H., Shirran S., Botting C., Lebl T., Houssen W., Jaspars M, & Naismith J.H. (2015). Structural analysis of leader peptide binding enables leader-free cyanobactin processing. Nature chemical biology, 11(8), 558-563.
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2

Recombinant Expression and Purification of Perdeuterated H-FABP

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Perdeuterated H-FABP was recombinantly expressed at the Institut Laue–Langevin (ILL) Deuteration Laboratory in Grenoble, France, and purified based on the procedure described previously (Zanotti et al., 1992 ▸ ). Briefly, Escherichia coli BL21(DE3) strain (Novagen), transformed with the pJexpress411 plasmid containing the synthetic cDNA coding for H-FABP, was over-expressed in perdeuterated minimal medium using d8-glycerol as carbon source (Artero et al., 2005 ▸ ). A high cell density fed-batch culture was grown at 30°C to an OD600 of 8.5. H-FABP expression was then induced by the addition of 0.5 mM IPTG and cells (40 g wet weight) were harvested at an OD600 of around 11. H-FABP was purified using 25 ml of Capto Q resin (GE Healthcare). The protein was eluted with 150 mM NaCl, 25 mM Tris-HCl pH 8.0. Finally, H-FABP was purified in a Hiload 26/60 Superdex 75 gel filtration column (GE Healthcare) in 20 mM Tris pH 7.5, 50 mM NaCl. The published crystallization conditions (Young et al., 1994 ▸ ) were optimized in terms of concentration and seeding conditions.
Howard E.I., Guillot B., Blakeley M.P., Haertlein M., Moulin M., Mitschler A., Cousido-Siah A., Fadel F., Valsecchi W.M., Tomizaki T., Petrova T., Claudot J, & Podjarny A. (2016). High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP–oleic acid complex: study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution. IUCrJ, 3(Pt 2), 115-126.
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3

Purification and Mass Analysis of Pyrophosphate

Check if the same lab product or an alternative is used in the 5 most similar protocols
Purification of pyrophosphate from heterocyclization reactions was achieved by passing the reaction mixture through a 5 kDa cut-off protein concentrator. The flow-through was applied to CaptoQ resin (GE Healthcare), washed with 15 column volumes dH2O and pyrophosphate eluted with 1M Na acetate pH 7.0.
Accurate mass measurements were carried out on ABSciex 5600 mass spectrometer with nanospray source. Samples were diluted 50% with ACN and infused at 1ul/min using the inbuilt syringe pump. Negative ionization spectra were collected from 60- 400m/z in MS mode. Masses 176.9 and 178.9 m/z were isolated in Q1, fragmented with collision energy 30V in Q2 and the fragments measured from 50-200m/z on the TOF analyzer. The TOF was externally calibrated with a mixture of Periodate (190.8847 m/z) and sulphanilic acid (172.0074 m/z)
Koehnke J., Mann G., Bent A.F., Ludewig H., Shirran S., Botting C., Lebl T., Houssen W., Jaspars M, & Naismith J.H. (2015). Structural analysis of leader peptide binding enables leader-free cyanobactin processing. Nature chemical biology, 11(8), 558-563.
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