Monos chromatography

Manufactured by GE Healthcare

Sourced in United States

MonoS chromatography is a type of ion exchange chromatography used for the separation and purification of biomolecules. It employs a cation exchange resin with sulfonic acid functional groups to bind and separate positively charged molecules based on their different net charges.

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Lab products found in correlation

Ni nta superflow, by Qiagen (2 mentions) Ni nta agarose, by GE Healthcare (1 mentions) Ni nta affinity chromatography, by GE Healthcare (1 mentions) Hitrap heparin high performance, by GE Healthcare (1 mentions) Superdex 200 gel filtration column, by GE Healthcare (1 mentions) Prep cell apparatus, by Bio-Rad (1 mentions) 293fectin, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Mono Q anion exchange chromatography (5 citations) Mono Q 5/50 ion-exchange chromatography (4 citations) Mono S column chromatography (4 citations) Mono Q anion exchange chromatography columns (2 citations) Mono Q 10/100 GL anion exchange chromatography (1 citations)

4 protocols using monos chromatography

Purification of Recombinant YB-1 and PARP1 Proteins

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Recombinant YB-1 and its mutants [YB-1 (Δ1), YB-1 (Δ1-2), or YB-1 (Δ1-2-3)] were overexpressed in Escherichia coli BL21 (DE3) and purified. YB-1 was purified by Ni-NTA affinity chromatography (GE Healthcare United States, catalog # GE17-5255-01), Mono-S chromatography (GE Healthcare, United States catalog # GE17-5168-01), and Superdex 16/600 chromatography (GE Healthcare, United States, catalog # GE28-9893-35) as described earlier (Alemasova et al., 2017 (link)). YB-1 mutants were purified by Ni-NTA and Mono-S chromatography.
Recombinant wild-type (wt) PARP1 and mutants PARP1^Y986S, PARP1^Y986H, and PARP1^G972R were overexpressed in E. coli Rosetta (DE3)pLysS (Novogen, catalog # 70956-3) and purified by Ni-NTA agarose (GE Healthcare United States, catalog # GE17-5255-01) affinity chromatography, HiTrap Heparin High Performance (GE Healthcare, United States, catalog # GE17-0407-01) affinity chromatography, and deoxyribonucleic acid−cellulose (single-stranded calf thymus DNA) (Sigma-Aldrich, United States, catalog #D8273) affinity chromatography as described previously (Sukhanova et al., 2004 (link)).
Yeast nicotinamide mononucleotide adenylyltransferase (NMNAT) was kindly provided by Dr. S.I. Shram (Institute of Molecular Genetic Russian Academy of Science, Moscow, Russia).

Naumenko K.N., Sukhanova M.V., Hamon L., Kurgina T.A., Anarbaev R.O., Mangerich A., Pastré D, & Lavrik O.I. (2022). The C-Terminal Domain of Y-Box Binding Protein 1 Exhibits Structure-Specific Binding to Poly(ADP-Ribose), Which Regulates PARP1 Activity. Frontiers in Cell and Developmental Biology, 10, 831741.

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Purification of 27F3 Fab and IgG

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27F3 Fab and IgG were expressed in 293F mammalian cells as previously described (Garces et al., 2015 (link); Irimia et al., 2016 (link)). The Fabs or IgG were purified from the supernatant by Ni-NTA Superflow (Qiagen), monoS chromatography (GE Healthcare).

Lang S., Xie J., Zhu X., Wu N.C., Lerner R.A, & Wilson I.A. (2017). Antibody 27F3 broadly targets influenza A group 1 and group 2 hemagglutinins through a further variation in VH1-69 antibody orientation on the HA stem. Cell reports, 20(12), 2935-2943.

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Histone Complexes and Nucleosome Reconstitution

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All recombinant histones (H2A, H2B, H4, H3.3, H3mm7, and H3.3 mutants) were bacterially produced and purified by Ni-NTA agarose chromatography followed by MonoS chromatography (GE Healthcare) as previously described^{61 (link),62 (link)}. To form histone complexes (H2A–H2B dimer and H3–H4 tetramer), H2A and H2B or H3 and H4 were mixed at an equimolecular ratio in 20 mM Tris-HCl (pH 8.0) buffer, containing 7 M guanidine hydrochloride and 20 mM 2-mercaptoethanol. After the samples were dialyzed against a refolding buffer (10 mM Tris-HCl (pH 7.5), 1 mM EDTA, 2 M NaCl, and 2 mM 2-mercaptoethanol), histone complexes were purified by chromatography on Superdex 200 gel filtration column (GE Healthcare), as previously described^{63 (link)}. The nucleosomes were reconstituted with the H2A–H2B dimer, the H3–H4 tetramer, and the 146 base-pair DNA derived from human alpha-satellite DNA by the salt-dialysis method^{63 (link)}. The reconstituted nucleosomes were purified using Prep Cell apparatus (Bio-Rad)^{64 (link)}.

Harada A., Maehara K., Ono Y., Taguchi H., Yoshioka K., Kitajima Y., Xie Y., Sato Y., Iwasaki T., Nogami J., Okada S., Komatsu T., Semba Y., Takemoto T., Kimura H., Kurumizaka H, & Ohkawa Y. (2018). Histone H3.3 sub-variant H3mm7 is required for normal skeletal muscle regeneration. Nature Communications, 9, 1400.

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Fab Purification for Crystallization

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H7.5 Fab for crystallization was prepared as previously described [30 (link)]. In brief, the heavy and light chains of H7.5 were cloned independently into the phCMV3 vector and fused with an N-terminal IgK secretion signal. A His₆ tag was added to the C-terminus of the Fab heavy chain. Recombinant cDNAs encoding the Fab heavy and light chains were purified and cotransfected into 293F cells by 293fectin (Invitrogen). After 6–7 days of expression at 37 °C, the Fabs were purified from the supernatant by Ni-NTA Superflow (Qiagen) and monoS chromatography (GE Healthcare).

Turner H.L., Pallesen J., Lang S., Bangaru S., Urata S., Li S., Cottrell C.A., Bowman C.A., Crowe JE J.r., Wilson I.A, & Ward A.B. (2019). Potent anti-influenza H7 human monoclonal antibody induces separation of hemagglutinin receptor-binding head domains. PLoS Biology, 17(2), e3000139.

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