Protein g ultralink resin

Manufactured by Thermo Fisher Scientific

Protein G Ultralink Resin is a high-performance affinity chromatography resin designed for the purification of immunoglobulins and other antibody-containing samples. It features a high-capacity, cross-linked agarose matrix and immobilized recombinant Protein G ligand, which selectively binds to the Fc region of immunoglobulins. The resin offers efficient and gentle capture of a wide range of antibody isotypes from various sample sources.

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Lab products found in correlation

Protease inhibitor cocktail, by Merck Group (2 mentions) Ripa buffer, by Merck Group (2 mentions) Nicotine hydrogen tartrate, by Merck Group (1 mentions) Odyssey blocking buffer, by LI COR (1 mentions) Coomassie plus protein assay, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail tablet, by Roche (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions) Mouse anti ha, by Santa Cruz Biotechnology (1 mentions) Laemmli sample buffer, by Bio-Rad (1 mentions) Ezview red anti flag m2 affinity gel, by Merck Group (1 mentions) Rnase cocktail, by Thermo Fisher Scientific (1 mentions) 3xflag peptide, by Merck Group (1 mentions) Mouse anti g3bp1, by Merck Group (1 mentions)

Close spelling variants of this product

Protein G resin

7 protocols using protein g ultralink resin

Polyclonal IgG Purification from Survivor Plasma

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We obtained de-identified previously collected plasma samples from survivors of Argentine hemorrhagic fever from the immune plasma bank at the Instituto Nacional de Enfermedades Virales Humanas (INEVH), based in Pergamino, Argentina. Provision of samples was approved by the INEVH Ethics Committee and the Harvard University Faculty of Medicine Committee on Human Studies (identified as not involving human subjects under 45CFR46.102(f)). We purified polyclonal IgG from de-identified Argentine hemorrhagic fever survivor plasma samples and from CR1 plasma with Protein G Ultralink Resin (Thermo Fisher Scientific) as previously described.^{14 (link)}

Clark L.E., Mahmutovic S., Raymond D.D., Dilanyan T., Koma T., Manning J.T., Shankar S., Levis S.C., Briggiler A.M., Enria D.A., Wucherpfennig K.W., Paessler S, & Abraham J. (2018). Vaccine-elicited receptor-binding site antibodies neutralize two New World hemorrhagic fever arenaviruses. Nature Communications, 9, 1884.

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Radiolabeled Epibatidine Binding Assay

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[³H]Epibatidine ([³H]EB, ~55 Ci/mmol) was purchased from Perkin Elmer Life Science (Boston, MA). Sazetidine-A dihydrochloride (Xiao et al., 2006) was synthesized by RTI, International (Research Triangle, NC) and supplied by NIDA. Nicotine hydrogen tartrate was purchased from Sigma-Aldrich (St. Louis, MO). Varenicline tartrate was a kind gift from Ms. Carolyn Kelman (Pfizer, Groton, CT). Osmotic minipumps were purchased from Alzet (Cupertino, CA). The monoclonal antibody mAb 290, which binds β2 subunits incorporated in assembled nAChRs (Sallette et al., 2005 (link)), was purchased from Sigma Aldrich, and the polyclonal antibodies sc-1772 and sc-11372, which bind the α4 and β2 subunits of nAChRs, respectively, were purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA). Odyssey blocking buffer and the fluorescently tagged antibodies donkey anti-goat 800CW and donkey anti-rabbit 680LT were purchased from LI-COR (Lincoln, NE). Protein G Ultra Link Resin, dimethyl pimelimidate (DMP), Triton X-100 detergent and Coomassie Plus Protein Assay were purchased from Thermo Fisher Scientific (Pittsburgh, PA). All other reagents were purchased from Sigma Aldrich unless noted otherwise.

Hussmann G.P., DeDominicis K.E., Turner J.R., Yasuda R.P., Klehm J., Forcelli P.A., Xiao Y., Richardson J.R., Sahibzada N., Wolfe B.B., Lindstrom J., Blendy J.A, & Kellar K.J. (2014). Chronic Sazetidine-A Maintains Anxiolytic Effects and Slower Weight Gain Following Chronic Nicotine Without Maintaining Increased Density of Nicotinic Receptors in Rodent Brain. Journal of neurochemistry, 129(4), 721-731.

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Coimmunoprecipitation of Protein Interactions

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For coimmunoprecipitation cells from a confluent 10 cm culture dish were washed once with cold PBS and harvested in 500 μl lysisbuffer (50 mM Tris-HCl, pH 7,5; 150 mM NaCl; 1 mM EDTA, pH 8,0; 1% NP-40; 1% TritonX-100 with Protease Inhibitor cocktail tablet (04 693 159, Roche)) on ice. After homogenization with a 25-gauge needle protein lysates were cleared by centrifugation at 12,000 g for 10 min at 4°C. For the input control a 50 μl aliquot was taken and mixed with 2 x sample buffer. The remaining lysate was used for immunoprecipitation with the appropriate antibody and Protein G Ultralink Resin (Thermo Scientific) over night at 4°C. Ultralink beads were washed three times with IP washing buffer (50 mM Tris-HCl pH8,5; 500 mM NaCl; 5 mM EDTA pH 8,0, 0,05% NP-40, 1 mg/ml BSA and Protease Inhibitor cocktail tablet) and finally resuspended in 2 x sample buffer (125 mM Tris-HCl pH 6.8, 20% Glycerol, 4% SDS, 5% β-Mercaptoethanol, 0,025% Bromphenolblue) for SDS-PAGE and Western blot analysis.

Serth K., Schuster-Gossler K., Kremmer E., Hansen B., Marohn-Köhn B, & Gossler A. (2015). O-Fucosylation of DLL3 Is Required for Its Function during Somitogenesis. PLoS ONE, 10(4), e0123776.

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Argentine Hemorrhagic Fever Survivor Plasma

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We obtained 5 de-identified plasma samples from Argentine hemorrhagic fever survivors from the immune plasma bank at the Instituto Nacional de Enfermedades Virales Humanas (INEVH), based in Pergamino, Argentina, where these samples are routinely stored. Provision of the previously collected survivor plasma samples was approved by the INEVH Ethics Committee, and the Harvard University Faculty of Medicine Committee on Human Studies (identified as not involving human subjects under 45CFR46.102(f)). We obtained an additional 5 plasma survivor samples through INEVH under a Boston Children’s Hospital Institutional Review Board and INEVH Ethics Committee approved protocol (IRB: IRB-P00007578) after informed consent was obtained from all subjects. Neutralizing antibody titers from the donors at the time of plasma collection had previously been determined by the fixed-virus/variable serum technique, with Vero cell monolayers infected with the XJCl₃ attenuated strain of JUNV virus, and defined as a plaque neutralization reduction of 80% (PRNT₈₀). Because the heparin that is contained in the plasma samples could interfere with the interpretation of the results of the pseudotype assay, we purified IgG from these samples using Protein G Ultralink^® Resin (Thermo scientific), as instructed by the manufacturer.

Mahmutovic S., Clark L., Levis S.C., Briggiler A.M., Enria D.A., Harrison S.C, & Abraham J. (2015). Molecular basis for antibody-mediated neutralization of New World hemorrhagic fever mammarenaviruses. Cell host & microbe, 18(6), 705-713.

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Purification and Mass Spectrometry of PQN-59 Complexes

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N2 worms were grown on OP50-seeded NGM plates, and embryos were harvested from gravid worms by bleaching (500 mM NaOH, 15% bleach). Embryos were resuspended in IP buffer (100 mM KCl, 50 mM Tris pH 7.5, 1 mM MgCl₂, 1 mM DTT, 5% glycerol, 0.05% NP40, 1 mM EDTA, Protease Inhibitor Cocktail (Roche)) and frozen in liquid nitrogen. For protein extraction, the embryos were ground on dry ice using a mortar and pestle. The embryonic protein homogenate was thawed on ice and centrifuged at 14,000 rpm for 30 minutes. Equivalent amounts of PQN-59 serum or pre-serum, for control, were incubated with 10 μl of Protein G UltraLink Resin (Thermo Scientific) on ice for 1 hour and 30 minutes. After three washing steps of the beads with IP buffer, approximately 2 mg of embryonic protein homogenate was added and combined samples were incubated for 2 hours on ice. Beads were then washed three times with IP buffer and an additional three times with a “last wash” IP buffer (100 mM KCl, 50 mM Tris pH 7.5, 1 mM MgCl₂, 1 mM DTT, 1 mM EDTA). PQN-59 complexes were eluted in 0.15% trifluoroacetic acid (TFA). Isolated samples were then frozen on dry ice and subjected to mass spectrometry analysis. Three IP samples from two separate protein homogenates were used in the analysis.

Carlston C., Weinmann R., Stec N., Abbatemarco S., Schwager F., Wang J., Ouyang H., Ewald C.Y., Gotta M, & Hammell C.M. (2021). PQN-59 antagonizes microRNA-mediated repression during post-embryonic temporal patterning and modulates translation and stress granule formation in C. elegans. PLoS Genetics, 17(11), e1009599.

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Immunoprecipitation of Endogenous FUS

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Cellular extracts of SH-SY5Y cells were prepared in 1x RIPA buffer (Millipore, 20-188) supplemented with protease inhibitor cocktail (Sigma, P-8340, 1:500) and 1mM sodium orthovanadate with syringe homogenization. The cellular lysates were first pre-cleared with Protein G UltraLink Resin (Thermo Scientific Pierce, 53126), then endogenous FUS was immunoprecipitated with mouse anti-FUS antibody (Santa Cruz, sc-47711) and Protein G UltraLink Resin. The negative control immunoprecipitation antibody was mouse anti-HA (Santa Cruz, sc-7392). The bound proteins were eluted by boiling with Laemmli sample buffer (Biorad, 161-0737).

Kamelgarn M., Chen J., Kuang L., Arenas A., Zhai J., Zhu H, & Gal J. (2016). Proteomic analysis of FUS interacting proteins provides insights into FUS function and its role in ALS. Biochimica et biophysica acta, 1862(10), 2004-2014.

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Immunoprecipitation of SOD1-G3BP1 Complexes

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The lysates were prepared in 1× RIPA buffer (Millipore) supplemented with protease inhibitor cocktail (Sigma, P-8340, 1:500) and 1 mM sodium orthovanadate. Mouse spinal cord extracts were prepared using a dounce homogenizer. Transfected cell lysates were homogenized by passing through a 23-gauge needle several times. Immunoprecipitations were performed at 4 °C for 2 h. The endogenous G3BP1 immunoprecipitations were done from spinal cord extracts with rabbit anti-G3BP1 Antibody (Millipore, 07-1801) and Protein A UltraLink Resin (Thermo Scientific Pierce, 53139). The FLAG immunoprecipitations were performed using EZview Red Anti-FLAG M2 Affinity Gel (Sigma, F2426) and the bound proteins were eluted with 3xFLAG peptide (Sigma, F4799). Where indicated, RNase Cocktail (Ambion Life Technologies, AM2286) was added to the immunoprecipitation mixtures at 1:100 dilution.
The in vitro SOD1–G3BP1 binding assays were performed using 2 μg WT or G93A mutant human SOD1 purified from insect cells as described [27 (link)] and 1.5 μg of 6xHis-tagged human G3BP1 purified from E. coli (Fitzgerald Industries, 80R-1601) in 500 μl 1× RIPA buffer. The mixtures were incubated at 37 °C for 2 h, cooled to 4 °C and G3BP1 was immunoprecipitated with mouse anti-G3BP1 (Millipore, 05-1938) and Protein G UltraLink Resin (Thermo Scientific Pierce, 53126).

Gal J., Kuang L., Barnett K.R., Zhu B.Z., Shissler S.C., Korotkov K.V., Hayward L.J., Kasarskis E.J, & Zhu H. (2016). ALS mutant SOD1 interacts with G3BP1 and affects stress granule dynamics. Acta Neuropathologica, 132(4), 563-576.

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