Protein g resin

Manufactured by Thermo Fisher Scientific

Sourced in United States

Protein G resin is a chromatographic medium used for the purification of immunoglobulins (IgG) from various biological samples. It consists of Protein G, a bacterial cell wall protein, covalently coupled to an agarose support matrix. Protein G has a high affinity for the Fc region of IgG, allowing for the selective capture and separation of IgG from complex mixtures.

Automatically generated - may contain errors

Lab products found in correlation

Leupeptin, by Nacalai Tesque (1 mentions) Sample buffer, by Fujifilm (1 mentions) Image scanner, by Canon (1 mentions) C digit, by LI COR (1 mentions) X ray film, by Fujifilm (1 mentions) Np 40, by Nacalai Tesque (1 mentions) Premade sodium dodecylsulfate polyacrylamide gel, by Nacalai Tesque (1 mentions) Canoscan software, by Canon (1 mentions) Image studio software, by LI COR (1 mentions) Blocking one, by Nacalai Tesque (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Ecl reagent, by Cytiva (1 mentions) Expi293 cell, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Protein A/G magnetic resins Protein A/G agarose resin Protein A/G resin/mg protein Pierce protein G agarose resin Protein A/G UltraLink Resin Immobilized Protein A/G resin slurry Protein G agarose resin Protein G Ultralink Resin Protein A/G resin Pierce Protein A/G Ultralink Resin

7 protocols using protein g resin

Peach Protein Immunoprecipitation Workflow

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total peach protein samples (1 mg) were precleared with protein G resin (Invitrogen, Carlsbad, CA, USA) at 4 °C for 4 h and then incubated with a CNBr-conjugated peach antibody at 4 °C overnight. After extensive washes, the IP complexes were eluted with 0.2 M glycine (pH 2.5) and analyzed by SDS-PAGE followed by silver staining or WB analysis. Protein bands from the silver-stained gels corresponding to the band visualized in the WB were excised for in-gel trypsin digestion and MS analysis.
For co-IP experiments, proteins were incubated with the same antibodies used for the IP assays, with anti-mouse IgG as the control. After extensive washes, the IP complexes were eluted with 0.2 M glycine (pH 2.5) and subjected to in-solution trypsin digestion and MS analysis.

Zeng W., Niu L., Wang Z., Wang X., Wang Y., Pan L., Lu Z., Cui G., Weng W., Wang M., Meng X, & Wang Z. (2020). Application of an antibody chip for screening differentially expressed proteins during peach ripening and identification of a metabolon in the SAM cycle to generate a peach ethylene biosynthesis model. Horticulture Research, 7, 31.

+ Open protocol

+ Expand

Immunoprecipitation and Mass Spectrometry of Dairy Cow Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total dairy cow protein samples (1 mg) were precleared with protein G resin (Invitrogen, Carlsbad, CA, USA) at 4 °C for 4 h and then incubated with a CNBr-conjugated peach antibody overnight. After extensive washes, the IP complexes were eluted with 0.2 M glycine (pH 2.5) and analyzed by SDS-PAGE followed by silver staining or Western blotting. Protein bands from the silver-stained gels corresponding to the visualized band in the WB were excised for in-gel trypsin digestion and MS analysis. For the co-IP assay, proteins were incubated with the same antibodies used for the IP assays. After extensive washes, the IP complexes were eluted with 0.2 M glycine (pH 2.5) and subjected to in-solution trypsin digestion and MS analysis. Anti-mouse IgG was used as a control.

Zhang Y., Wang Y., Liu R., Fei Z., Fan X., Jiang J., Sun L., Meng X, & Liu C. (2024). Antibody array-based proteome approach reveals proteins involved in grape seed development. Plant Physiology, 195(1), 462-478.

+ Open protocol

+ Expand

Passive IgG Transfer from Adenovirus-MVA Mice

Check if the same lab product or an alternative is used in the 5 most similar protocols

Whole IgG from adenovirus-primed, MVA boost-immunized mice was purified using Pierce columns prepacked with 2 ml of protein G resin according to the manufacturer's instructions (Thermo Scientific, United Kingdom). Two milligrams of purified whole IgG obtained from immunized animals was injected into each naive CD1 mouse.

Bauza K., Malinauskas T., Pfander C., Anar B., Jones E.Y., Billker O., Hill A.V, & Reyes-Sandoval A. (2014). Efficacy of a Plasmodium vivax Malaria Vaccine Using ChAd63 and Modified Vaccinia Ankara Expressing Thrombospondin-Related Anonymous Protein as Assessed with Transgenic Plasmodium berghei Parasites. Infection and Immunity, 82(3), 1277-1286.

+ Open protocol

+ Expand

Protein Immunoblotting from Cell Lysates

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cells were lysed in lysis buffer (50 Mm HEPES-NaOH, Ph 7.5, 150 Mm NaCl, 3 Mm MgCl₂, 1 Mm dithiothreitol, 1 Mm phenylmethane sulfonylfluoride, 1 μg/ML leupeptin, 1 Mm EDTA, 1 Mm Na₃VO₄, 10 Mm NaF, and 0.5% NP-40; Nacalai Tesque) [15 (link),16 (link),31 (link),32 (link)]. For denatured conditions, cell lysates were denatured in sample buffers (Fujifilm). The denatured samples and denatured immunoprecipitated complexes composed of primary antibody-captured antigen and Protein G resin (Thermo Fisher Scientific) were separated on premade sodium dodecylsulfate-polyacrylamide gel (Nacalai Tesque). The electrophoretically separated proteins were transferred to a polyvinylidene fluoride membrane (Fujifilm), blocked with Blocking One (Nacalai Tesque), and immunoblotted using primary antibodies, followed by peroxidase enzyme-conjugated secondary antibodies [15 (link),16 (link),31 (link),32 (link)]. The peroxidase-reactive bands were exposed on X-ray films (Fujifilm), captured using an image scanner (Canon, Tokyo, Japan), and scanned using CanoScan software (Canon). We also used a chemiluminescence scanner (C-DiGit, LI-COR, Lincoln, NE, USA) and captured immunoreactive bands through Image Studio software (LI-COR). We performed some sets of experiments in immunoblotting studies and quantified other immunoreactive bands with Image J software ver. 2.15.0.

Fukatsu S., Miyamoto Y., Oka Y., Ishibashi M., Shirai R., Ishida Y., Endo S., Katoh H, & Yamauchi J. (2023). Investigating the Protective Effects of a Citrus Flavonoid on the Retardation Morphogenesis of the Oligodendroglia-like Cell Line by Rnd2 Knockdown. Neurology International, 16(1), 33-61.

+ Open protocol

+ Expand

SARS-CoV-2 Spike Protein Immunoblotting

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cell lysates in RIPA buffer (PBS, pH 7.4, with 1.0% NP-40, 0.1% SDS, 0.5% sodium deoxycholate, protease inhibitor cocktail), recombinant proteins or E. coli lysates of SARS-CoV-2 S2-truncated mutants were resolved with 12% SDS-PAGE and transferred to PVDF membrane (Millipore). After blocking with 5% skim milk in TBST, membranes were probed with anti-S2 antibodies or mouse anti-6×His antibody (1:2500; Qiagen). Antibody-reactive bands were detected via HRP-conjugated secondary reagents and chemiluminescence with ECL reagent (Cytiva). For immunoprecipitation, 800 µg lysates were mixed with 4A5 or control IgG2a at 4°C for 16 h. Protein G resin (Thermo Fisher Scientific) was used to capture antigen-antibody complexes for subsequent western blot analysis.

Heo C.K., Lim W.H., Yang J., Son S., Kim S.J., Kim D.J., Poo H, & Cho E.W. (2023). Novel S2 subunit-specific antibody with broad neutralizing activity against SARS-CoV-2 variants of concern. Frontiers in Immunology, 14, 1307693.

+ Open protocol

+ Expand

Nanobody-Fc Fusion Protein Production

Check if the same lab product or an alternative is used in the 5 most similar protocols

Nanobodies targeting RBD were expressed and secreted as Fc fusions by cloning into pFUSE-hlgG1-Fc2 (Invivogen) using the NcoI and EcoRI restriction sites or by Gibson assembly. For each nanobody-Fc fusion, 100 mL of Expi293 cells (ThermoFisher Cat# A14527) were transfected with 90-150 μg of plasmid. After 1 day, cells were enhanced with 3 mM valproic acid and 0.45% glucose. Cell supernatants were harvested 4 days after transfection. Before purification, supernatants were treated with benzonase nuclease and protease inhibitor, then passed through a 0.22 μm filter. Nanobody-Fc fusion supernatants were passed over a column with 4 mL protein G resin (ThermoFisher Cat# 20399), which was then washed with 40 mL of HBS, eluted with 100 mM citrate (pH 3) and then neutralized to pH 7 with concentrated HEPES (pH 8). Nanobody-Fc fusions were then dialyzed twice with HBS (pH 7.5).

Wellner A., McMahon C., Gilman M.S., Clements J.R., Clark S., Nguyen K.M., Ho M.H., Hu V.J., Shin J.E., Feldman J., Hauser B.M., Caradonna T.M., Wingler L.M., Schmidt A.G., Marks D.S., Abraham J., Kruse A.C, & Liu C.C. (2021). Rapid generation of potent antibodies by autonomous hypermutation in yeast. Nature chemical biology, 17(10), 1057-1064.

+ Open protocol

+ Expand

Competitive Binding Analysis of AAV8/luc with THR

Check if the same lab product or an alternative is used in the 5 most similar protocols

For THR competitive binding analysis, 10 μl of Protein G resin (Thermo Fisher Scientific, USA) was incubated with 1 μg of either a human transferrin (hTf) antibody or a goat IgG antibody control at 4 °C overnight. The next day, 1×10¹⁰ vg of AAV8/luc was incubated with HSA of physiological concentration, THR or the PEPXT-1 control peptide at different dilutions, or DPBS on ice for 2 h. HTf was added into the complex at a 1:100 dilution of the physiological concentration and incubated on ice for another 2 h. After that, the mixture was added to the complex of Protein G resin and transferrin antibody and then incubated at 4 °C overnight. Finally, the complex was stringently washed three times with cold DPBS. DNA from the complex was extracted and subjected to qPCR to determine AAV genome copy number per cell using luc specific primers (Table S1).

Zhang X., He T., Chai Z., Samulski R.J, & Li C. (2018). Blood-brain barrier shuttle peptides enhance AAV transduction in the brain after systemic administration. Biomaterials, 176, 71-83.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!