Resourceq 6 ml column

Manufactured by GE Healthcare

The ResourceQ 6-ml column is a laboratory equipment designed for chromatographic separations. It is a pre-packed column that can be used for ion exchange chromatography applications. The column has a volume of 6 milliliters and is suitable for a variety of sample types and purification needs. Its core function is to facilitate the separation and purification of biomolecules, such as proteins, peptides, and nucleic acids, from complex mixtures.

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Lab products found in correlation

Resource q column, by GE Healthcare (1 mentions) Mono q 5 50 gl column, by GE Healthcare (1 mentions) Hitrap imac ff column, by GE Healthcare (1 mentions) Bl21 star de3, by Thermo Fisher Scientific (1 mentions) Kta explorer, by GE Healthcare (1 mentions) Superdex 200 column, by GE Healthcare (1 mentions) 13c glucose, by Eurisotop (1 mentions) 15 nh 4 cl, by Eurisotop (1 mentions) Membrane concentrator, by Merck Group (1 mentions) Pfastbac dual, by Thermo Fisher Scientific (1 mentions) Hi5 cells, by Thermo Fisher Scientific (1 mentions) Escherichia coli dh10bac, by Thermo Fisher Scientific (1 mentions) Histrap hp 5 ml column, by GE Healthcare (1 mentions) Bac to bac baculovirus expression system manual, by Thermo Fisher Scientific (1 mentions) Hiload 16 60 superdex 200 pg column, by GE Healthcare (1 mentions) Gsh agarose beads, by Merck Group (1 mentions) Ni nta agarose column, by Macherey-Nagel (1 mentions)

6 protocols using resourceq 6 ml column

Purification of Fungal Heme-Containing Monooxygenases

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The bacterial pellets were resuspended in the corresponding lysis buffer (Table S3 in the supplemental material), and the mixtures were incubated with 0.1 mg/ml of DNase I and 2 mg/ml lysozyme for 45 min. The solutions were sonicated and centrifuged to eliminate insoluble debris.
MetspHMFO and PsespHMFO (untagged proteins) were purified in a ResourceQ 6-ml column (GE Healthcare) with a linear NaCl gradient (60 to 160 mM in 4 column volumes [CV]) in 50 mM Tris-HCl, pH 8.0, followed by a MonoQ 5/50 GL column in which the protein fractions were eluted with a NaCl linear gradient (0 to 70 mM in 10 CV) in 50 mM Tris-HCl, pH 8.0 (Table S3).
His-tagged fusion proteins (MetspHMFO^His and PseniHMFO^His) were purified by affinity chromatography in a HiTrap IMAC FF column (GE Healthcare) with a linear imidazole gradient (20 m to 300 mM in 6 CV) in 500 mM NaCl, 20 mM Tris-HCl, pH 7.5, followed by anionic exchange chromatography with a ResourceQ column (GE Healthcare) with an NaCl linear gradient (0 to 500 mM in 5 CV) in 50 mM Tris-HCl, pH 7.5 (Table S3).
The purified HMFOs were dialyzed against 50 mM Tris-HCl, pH 7.0, and stored at −80°C, being stable for several months.

Viñambres M., Espada M., Martínez A.T, & Serrano A. (2020). Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production. Applied and Environmental Microbiology, 86(16), e00842-20.

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Preparation of T cell receptor TRAV22/TRBV7-9

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The T cell receptor with variable domains TRAV22/TRBV7-9 was prepared as described previously [20 (link), 21 (link)], apart from minor changes stated here. Expression was carried out in Escherichia coli BL21 (DE3) Star (Invitrogen). Inclusion bodies were solubilized in 50 mM Tris-HCl pH 8.0, 6 M guanidinium chloride, 100 mM NaCl, 10 mM EDTA, 5 mM DTT and then refolded in 100 mM Tris-HCl pH 8.0, 5 M urea, 400 mM L-arginine, 0.83 mg/l cysteamine. Purification was done by anion exchange chromatography on an ÄKTA explorer (GE Healthcare), with a Resource Q 6 ml column (GE Healthcare), followed by size exclusion chromatography on a Superdex 200 column (GE Healthcare) in TBS buffer. Purified staphylococcal enterotoxin E, a gift from Active Biotech Research AB, was prepared according to a previously published protocol [22 (link)].

Rödström K.E., Regenthal P, & Lindkvist-Petersson K. (2015). Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition. PLoS ONE, 10(7), e0131988.

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Isolation and Purification of (p)ppGpp

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(p)ppGpp was produced essentially as described previously^{33 (link)}. In brief, 5 µM SAS1 were incubated in SEC buffer together with 10 mM ATP and 10 mM GDP for 30 min at 37 °C to produce ppGpp or together with 10 mM ATP and 10 mM GTP for 2 h at 37 °C to produce pppGpp. Afterwards, the reaction was mixed with the same volume of chloroform and centrifuged (17300 × g, 5 min, 4 °C). The aqueous phase was removed and the organic phase mixed with one volume of double-destilled water and centrifuged (17300 × g, 5 min, 4 °C). The combined aqueous phases were subjected to anion-exchange chromatography using a ResourceQ. 6-ml column (GE Healthcare) at a flow rate of 6 ml/min and the nucleotides eluted with a gradient of NaCl. Fractions containing ppGpp or pppGpp were pooled followed by addition of lithium chloride with a concentration of 1 M and four volumes of ethanol. The suspension was then incubated at −20 °C for 20 min and centrifuged (5000 × g, 20 min, 4 °C). The resulting pellets were washed with absolute ethanol, dried and stored at −20 °C. Quality of the so-prepared alarmones was controlled by HPLC and yielded ppGpp and pppGpp in purities of 98% and 95%, respectively.

Steinchen W., Vogt M.S., Altegoer F., Giammarinaro P.I., Horvatek P., Wolz C, & Bange G. (2018). Structural and mechanistic divergence of the small (p)ppGpp synthetases RelP and RelQ. Scientific Reports, 8, 2195.

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Purification of Recombinant Human ASF1 Protein

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Recombinant human ASF1 [hASF1A(1-156)] was purified as already described from expression in Escherichia coli of a (His)₆–glutathione S-transferase (GST)–TEV site–Asf1 fusion protein using the pETM30 plasmid (38 (link)). Briefly, soluble (His)₆-tagged GST fusion protein was purified on reduced glutathione agarose beads (Sigma-Aldrich). After cleavage with recombinant (His)₆-Tobacco Etch Virus Protease (TEV) protease at room temperature overnight, the (His)₆-GST tag and the protease were trapped in a nickel-charged nitrilotriacetic acid (NTA) chelate immobilized onto agarose column (Macherey Nagel). The flow-through fraction containing ASF1 protein was further purified by anion exchange chromatography using a Resource Q 6-ml column (GE Healthcare). ASF1 was then concentrated using an Amicon device (Millipore), and the buffer was replaced with a 50 mM tris-HCl (pH 7.5). Unlabled ASF1 used for ITC experiments was purified from pellets of bacteria grown in LB medium and uniformly labeled ASF1 from bacteria gown in M9 minimal media supplemented with (¹⁵NH₄)Cl (0.5 g/liter; Eurisotop) as the sole nitrogen source and or ¹³C glucose (2 g/liter; Eurisotop).

Mbianda J., Bakail M., André C., Moal G., Perrin M.E., Pinna G., Guerois R., Becher F., Legrand P., Traoré S., Douat C., Guichard G, & Ochsenbein F. (2021). Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity. Science Advances, 7(12), eabd9153.

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Zika Virus NS1 Protein Purification

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The ZIKV NS1 construct (amino acid residues 2–352, Accession Number: AMA12085) was cloned into the baculovirus transfer vector pFastBac Dual (Invitrogen) under control of the polyhedrin promoter, in‐frame with an N‐terminal gp67 signal peptide for secretion and a His₆‐tag at the N‐terminus for purification. We placed green fluorescent protein (GFP) under control of the P10 promoter to visualize expression, which correlated well with expression of NS1. Recombinant pFastBac Dual plasmid was used to transform DH10Bac^™Escherichia coli (Invitrogen). Transfection and virus amplification were performed according to the Bac‐to‐Bac baculovirus expression system manual (Invitrogen) (Song et al, 2016b). NS1 proteins were produced by infecting suspension cultures of Hi5 cells (Invitrogen) for 2 days. Soluble NS1 was recovered from cell supernatants by metal affinity chromatography using a HisTrap HP 5 ml column (GE Healthcare), and then purified by ion‐exchange chromatography using a RESOURCE^™Q 6 ml column (GE Healthcare). For crystallization, the proteins were further purified by gel filtration chromatography using a Hiload 16/60 Superdex^® 200 PG column (GE Healthcare) with a running buffer of 20 mM Tris–HCl and 50 mM NaCl (pH 8.5), and the collected protein fractions were concentrated to 10 mg/ml using a membrane concentrator with a molecular weight cutoff of 10 kDa (Millipore).

Xu X., Song H., Qi J., Liu Y., Wang H., Su C., Shi Y, & Gao G.F. (2016). Contribution of intertwined loop to membrane association revealed by Zika virus full‐length NS1 structure. The EMBO Journal, 35(20), 2170-2178.

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Purification of Recombinant Human ASF1

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Recombinant human ASF1 (hASF1A(1-156)) was purified as already described from expression in E. coli of a (His)6-GST-Tev site-Asf1 fusion protein using the pETM30 plasmid.(37) Briefly, soluble (His)6-tagged GST fusion protein was purified on reduced glutathione (GSH) agarose beads (Sigma). After cleavage with recombinant (His)6-TEV protease at room temperature overnight, the (His)6-GST tag and the protease were trapped in a Ni-NTA agarose column (Macherey Nagel). The flow-through fraction containing ASF1 protein was further purified by anion exchange chromatography using a Resource Q 6mL column (GE Healthcare). ASF1 was then concentrated using an Amicon device (Millipore) and the buffer was replaced with a 50mM Tris-HCl (pH7.5). Unlabled ASF1 used for ITC experiments was purified from pellets of bacteria grown in LB medium, and uniformly labeled ASF1 from bacteria gown in M9 minimal media supplemented with ( 15 NH4)Cl (Eurisotop, 0.5 g/L) as the sole nitrogen source and or 13 C glucose (Eurisotop, 2 g/L).

Mbianda J., Bakail M., André C., Moal G., Perrin M.E., Guérois R., Bécher F., Legrand P., Traoré S., Douat C., Guichard G., & Ochsenbein F. (2020). Optimal Anchoring of a Urea-based Foldamer Inhibitor of ASF1 Histone Chaperone Through Backbone Plasticity.

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