Gst tag

Manufactured by Thermo Fisher Scientific

Sourced in United States

The GST tag is a protein purification tool used to facilitate the isolation and detection of recombinant fusion proteins. It functions by allowing the target protein to be selectively bound to a GST-specific resin, enabling its separation from other cellular components.

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3 protocols using gst tag

Western Blotting Analysis of Protein Samples

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Cells lysates, prepared by dissolving washed cells directly in SDS sample buffer, were resolved by SDS-PAGE with indicated percentage of acrylamide. Western blotting was performed using standard protocols. For quantification, western blots were analyzed by ImageJ. Antibodies used in this paper as follows: Flag tag (M2; Sigma, St. Louis, MO), actin (Sigma), phospho CTD Tyr1 (3D12; Active Motif, Carlsbad, CA), U2AF65 (Sigma), histone H3 protein (abcam, Cambridge, MA), phospho CTD Ser2 (3E10; Millipore, Billerica, MA), phospho CTD Ser5 (3E8; Millipore), phospho CTD Ser 7 (4E12, Millipore), Rpb1 CTD (8WG16; abcam), GST tag (Invitrogen, Carlsbad, CA), Rpb1 (N20; Santa Cruz, Santa Cruz, CA), Exosc10 (Rrp6) (Novus, Littleton, CO), Exosc9 (Rrp45) (Novus), Exosc3 (Rrp40) (Novus), and Dis3 (Novus).

Hsin J.P., Li W., Hoque M., Tian B, & Manley J.L. (2014). RNAP II CTD tyrosine 1 performs diverse functions in vertebrate cells. eLife, 3, e02112.

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Protein Expression and Purification

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Ammonia water, silver nitrate (AgNO₃), sodium citrate (Na₃C₆H₅O₇·2H₂O), hydrazine hydrate (N₂H₄·H₂O), glutathione (GSH), and phenylmethanesulfonyl fluoride (PMSF) were purchased from Sigma-Aldrich (American). Isopropylthio-β-d-galactoside (IPTG), Tris-HCl (pH 8.0), thrombin protease, and GST tag were purchased from Invitrogen (American). All chemicals and reagents were used as received without further purification.

Ran X., Zhang Q., Zhang Y., Chen J., Wei Z., He Y, & Guo L. (2020). Probing the Electron Transfer between iLOV Protein and Ag Nanoparticles. Molecules, 25(11), 2544.

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Purification and Analysis of GST-Tagged Proteins

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The crude extract of the supernatant of the GST and GST-Tag fusion proteins (Invitrogen, Carlsbad, CA, USA) were bound to G4B. A crude extract of the supernatant of the second protein bound to the GST-Tag fusion protein was added. The samples were placed on a shaker platform for 1 h at 4°C, and then centrifuged for 5 min at 500 × g at 4°C. The supernatants were discarded. A 2X SDS gel loading buffer of appropriate amount was added to each sample. They were boiled for 5 min at 100°C, subjected to sodium dodecyl sulphate-polyacrylamide gel (SDS-PAGE), and Coomassie Brilliant Blue stained, or detected by western blot analysis (16 (link)).

Shi Q., Li C., Li K, & Liu Q. (2016). Pallidin protein in neurodevelopment and its relation to the pathogenesis of schizophrenia. Molecular Medicine Reports, 15(2), 665-672.

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