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GE Healthcare glutathione resin
Glutathione Resin, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/glutathione resin/product/GE Healthcare
Average 92 stars, based on 57 article reviews
Price from $9.99 to $1999.99
glutathione resin - by Bioz Stars, 2020-08
92/100 stars

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Centrifugation:

Article Title: Expansion of DUB functionality generated by alternative isoforms – USP35, a case study
Article Snippet: .. After centrifugation at 11,000 g (Beckman JA-10), the supernatant was batch-bound to a glutathione resin (glutathione–Sepharose, GE Healthcare). ..

Mutagenesis:

Article Title: ERK1/2 Regulate Exocytosis through Direct Phosphorylation of the Exocyst Component Exo70
Article Snippet: .. Wild type Exo70, Exo70(S250A) and Exo70(S250D) mutant were expressed as GST fusion proteins in the pGEX-6P vector and purified from bacteria lysates with glutathione resin (GE Healthcare). ..

Purification:

Article Title: An FHA domain-mediated protein interaction network of Rad53 reveals its role in polarized cell growth
Article Snippet: .. Glutathione resin was used for their purification according to manufacturer's instruction (GE Healthcare). .. PATH purification of FHA-interacting proteins 2 liters of yeast cells (BY4741) were grown in YPD medium to an OD600 of 1.5.

Article Title: A Helical Conotoxin from Conus imperialis Has a Novel Cysteine Framework and Defines a New Superfamily *
Article Snippet: .. After purification with glutathione resin (GE Healthcare), the GST fusion protein was cleaved with thrombin. .. The recombinant im23a was purified on a Zobax C18 semi-preparative column (Agilent Technologies).

Article Title: ERK1/2 Regulate Exocytosis through Direct Phosphorylation of the Exocyst Component Exo70
Article Snippet: .. Wild type Exo70, Exo70(S250A) and Exo70(S250D) mutant were expressed as GST fusion proteins in the pGEX-6P vector and purified from bacteria lysates with glutathione resin (GE Healthcare). ..

Article Title: CAML Does Not Modulate Tetherin-Mediated Restriction of HIV-1 Particle Release
Article Snippet: .. The recombinant protein was cleaved from glutathione resin using Prescission protease (GE Lifesciences) and purified by FPLC. .. The recombinant protein was injected into rabbits by Cocalico Biologicals, and antisera specificity verified by ELISA and Western blotting against tetherin.

Incubation:

Article Title: 1.92 Angstrom Zinc-Free APOBEC3F Catalytic Domain Crystal Structure
Article Snippet: .. Cells were clarified at 14,000 xg for 20min., and supernatant was collected and incubated with glutathione resin (GE Healthcare). .. GST-A3F bound resin was washed with 50mM Tris pH 7.5, 100mM NaCl, and 5mM DTT.

Article Title: Promotion of RAD51-mediated Homologous DNA Pairing by the RAD51AP1-UAF1 Complex
Article Snippet: .. GST- or MBP-tagged RAD51AP1 (3 μg) and UAF1 (3 μg) were incubated in 30 μl reaction buffer (25 mM Tris-HCl at pH 7.5, 10% glycerol, 0.5 mM EDTA, 0.01% Igepal, 1mM DTT, 150 mM KCl) on ice for 30 min, and then 15 μl glutathione resin (GE Healthcare) or amylose resin (New England Biolabs) was added to capture RAD51AP1 through its GST or MBP tag, respectively. ..

Fast Protein Liquid Chromatography:

Article Title: CAML Does Not Modulate Tetherin-Mediated Restriction of HIV-1 Particle Release
Article Snippet: .. The recombinant protein was cleaved from glutathione resin using Prescission protease (GE Lifesciences) and purified by FPLC. .. The recombinant protein was injected into rabbits by Cocalico Biologicals, and antisera specificity verified by ELISA and Western blotting against tetherin.

Recombinant:

Article Title: CAML Does Not Modulate Tetherin-Mediated Restriction of HIV-1 Particle Release
Article Snippet: .. The recombinant protein was cleaved from glutathione resin using Prescission protease (GE Lifesciences) and purified by FPLC. .. The recombinant protein was injected into rabbits by Cocalico Biologicals, and antisera specificity verified by ELISA and Western blotting against tetherin.

Plasmid Preparation:

Article Title: ERK1/2 Regulate Exocytosis through Direct Phosphorylation of the Exocyst Component Exo70
Article Snippet: .. Wild type Exo70, Exo70(S250A) and Exo70(S250D) mutant were expressed as GST fusion proteins in the pGEX-6P vector and purified from bacteria lysates with glutathione resin (GE Healthcare). ..

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  • 94
    GE Healthcare glutathione sepharose resin
    The OAR of Rtf1 interacts directly with the CTR of Spt5. (A) Recombinant GST (pGEX-3X), GST-Rtf1-His 6 (pAP21), GST-Rtf1ΔOAR-His 6 (pMM26), and GST-OAR (pMM25) proteins, bound to <t>glutathione-Sepharose</t> beads, were incubated with the same amount of
    Glutathione Sepharose Resin, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 198 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glutathione sepharose resin/product/GE Healthcare
    Average 94 stars, based on 198 article reviews
    Price from $9.99 to $1999.99
    glutathione sepharose resin - by Bioz Stars, 2020-08
    94/100 stars
      Buy from Supplier

    94
    GE Healthcare glutathione sepharose
    Lentiviral IN affinity for imp7 correlates with infection phenotype in imp7 KD cells . (A) GST-imp7 (top left), GST (middle), or GST-LEDGF 326–530 (bottom) immobilized on glutathione <t>sepharose</t> beads were incubated in the absence (lane 1), or presence (lanes 2–6) of untagged recombinant HIV-1, HIV-2, SIVmac, EIAV, or BIV IN in the pull-down buffer containing 130 mM NaCl. Proteins bound to glutathione sepharose beads were resolved in an SDS PAGE gel and detected by staining with Coomassie Blue. Input quantities of each soluble protein used are shown to the right. Migration positions of GST-Imp7, INs, GST, and GST-LEDGF 326–530 , and the molecular weight markers are indicated. (B) Non-tagged Imp7 was incubated in the absence (lane 3) or presence (lanes 4–9) of C-terminally hexahistidine-tagged INs from HIV-1, HIV-2, SIVmac, EIAV, BIV and Ni-NTA agarose beads in a pull down buffer containing 150 mM NaCl. Proteins captured on the resin were separated in a tricine SDS PAGE gel and detected with Coomassie Blue. Lanes 1 and 2 show 100% and 20% Imp7 input, respectively. (C) GST (lanes 3, 6, 9, 12, 15), GST-LEDGF 326–530 (lanes 4, 7, 10, 13, 16), or GST-imp7 (lanes 5, 8, 11, 14, 17) were incubated without (lanes 3–5), or with non-tagged HIV-1 (lanes 6–8, 12–14) or HIV-2 (lanes 9–11, 15–16) INs. The pull-down buffer contained 150 mM (lanes 3–11) or 400 mM (lanes 12–17) NaCl. Lanes 1 and 2 contained input quantities of HIV-1 and HIV-2 INs, respectively. (D) DxR KD and imp7 KD cell populations were infected with VSV-G pseudotyped HIV-1, (pHR'), SIVmac, HIV-2 and EIAV vectors expressing GFP at an MOI of 0.03 and the percentage of GFP+ cells counted 24 hours after infection by flow cytometry. Data are expressed as average percentage of infection relative to control (shDxR) ± SD of two independent experiments performed in duplicate.
    Glutathione Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 1321 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glutathione sepharose/product/GE Healthcare
    Average 94 stars, based on 1321 article reviews
    Price from $9.99 to $1999.99
    glutathione sepharose - by Bioz Stars, 2020-08
    94/100 stars
      Buy from Supplier

    Image Search Results


    The OAR of Rtf1 interacts directly with the CTR of Spt5. (A) Recombinant GST (pGEX-3X), GST-Rtf1-His 6 (pAP21), GST-Rtf1ΔOAR-His 6 (pMM26), and GST-OAR (pMM25) proteins, bound to glutathione-Sepharose beads, were incubated with the same amount of

    Journal: Molecular and Cellular Biology

    Article Title: The Recruitment of the Saccharomyces cerevisiae Paf1 Complex to Active Genes Requires a Domain of Rtf1 That Directly Interacts with the Spt4-Spt5 Complex

    doi: 10.1128/MCB.00270-13

    Figure Lengend Snippet: The OAR of Rtf1 interacts directly with the CTR of Spt5. (A) Recombinant GST (pGEX-3X), GST-Rtf1-His 6 (pAP21), GST-Rtf1ΔOAR-His 6 (pMM26), and GST-OAR (pMM25) proteins, bound to glutathione-Sepharose beads, were incubated with the same amount of

    Article Snippet: Clarified lysates were incubated with 1 ml of bovine serum albumin (BSA)-blocked 50% glutathione-Sepharose resin (GE Healthcare) for 1 h at 4°C to purify GST and GST-OAR.

    Techniques: Recombinant, Incubation

    E193K variant affects LRRK2-DRP1 complex. (A) Extracts of mouse adult forebrain were incubated with anti-LRRK2 antibodies or rat IgG. The immunocomplexes were isolated with protein G-Sepharose and the samples were resolved by SDS-PAGE and analyzed by immunoblotting with anti DRP1 and anti LRRK2 antibodies. Arrowhead indicates unspecific band recognized by anti-rabbit secondary antibody. (B) We isolated on streptavidin resin strep-FLAG-LRRK2 full-length (full-length), strep-FLAG-LRRK2ΔWD40 (ΔWD40) and strep-FLAG-LRRK2ΔN–terminal (ΔN–terminal) protein from HEK293 over-expressing cells. Interacting proteins were resolved by western-blotting. (C) We performed a GST-pull down approach to explore the interactome associated to LRRK2 N-terminal Armadillo domain. GST-fusion proteins corresponding to Armadillo domain of LRRK2 WT and LRRK2 E193K (E193K) were used to retain interactors from adult forebrain lysate. The complexes were isolated with GSH-Sepharose beads, the samples were resolved by SDS-PAGE and analyzed by immunoblotting with anti DRP1 and anti P-Ser616 DRP1 antibodies. (D) We evaluated the extent of DRP1 and P-Ser616 DRP1 bound to WT and E193K Armadillo domain expressed as ratio over WT domain. Graph reports mean ± SE; n = 4; ** p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: The LRRK2 Variant E193K Prevents Mitochondrial Fission Upon MPP+ Treatment by Altering LRRK2 Binding to DRP1

    doi: 10.3389/fnmol.2018.00064

    Figure Lengend Snippet: E193K variant affects LRRK2-DRP1 complex. (A) Extracts of mouse adult forebrain were incubated with anti-LRRK2 antibodies or rat IgG. The immunocomplexes were isolated with protein G-Sepharose and the samples were resolved by SDS-PAGE and analyzed by immunoblotting with anti DRP1 and anti LRRK2 antibodies. Arrowhead indicates unspecific band recognized by anti-rabbit secondary antibody. (B) We isolated on streptavidin resin strep-FLAG-LRRK2 full-length (full-length), strep-FLAG-LRRK2ΔWD40 (ΔWD40) and strep-FLAG-LRRK2ΔN–terminal (ΔN–terminal) protein from HEK293 over-expressing cells. Interacting proteins were resolved by western-blotting. (C) We performed a GST-pull down approach to explore the interactome associated to LRRK2 N-terminal Armadillo domain. GST-fusion proteins corresponding to Armadillo domain of LRRK2 WT and LRRK2 E193K (E193K) were used to retain interactors from adult forebrain lysate. The complexes were isolated with GSH-Sepharose beads, the samples were resolved by SDS-PAGE and analyzed by immunoblotting with anti DRP1 and anti P-Ser616 DRP1 antibodies. (D) We evaluated the extent of DRP1 and P-Ser616 DRP1 bound to WT and E193K Armadillo domain expressed as ratio over WT domain. Graph reports mean ± SE; n = 4; ** p

    Article Snippet: Briefly, 5 μg of each GST fusion protein was loaded onto glutathione-sepharose resin (GE-Healthcare, Freiburg) and co-incubated with adult mouse brain lysate (1 mg of total protein).

    Techniques: Variant Assay, Incubation, Isolation, SDS Page, Expressing, Western Blot

    DDK promotes Sld3‐dependent Cdc45 recruitment Reaction scheme for Sld3/7/Cdc45 recruitment experiments. DNA substrate was bound to beads, and reaction mixtures were removed after each step. Immunoblots of recruitment reactions performed as described in (A), with the indicated proteins omitted. In (C), a mid‐reaction wash in high salt (0.5 M NaCl) buffer ( HSW ) was included following DDK phosphorylation as indicated. Recruitment reaction performed as in (A), using wild‐type (wt) or a Cdc45‐binding mutant (3E1) of Sld3. Schematic showing the position of Cdc45‐interacting region in Sld3. Alignments were generated in Jalview using Clustal. Sld3 from various fungal species is included (S.c., Saccharomyces cerevisiae , S.m., Saccharomyces mikatae, S.b., Saccharomyces bayanus, S.ca., Saccharomyces castellii, S.ku., Saccharomyces kudriavzevii ). Residue numbers correspond to S. cerevisiae Sld3. Residues were substituted for Glu as indicated. Wild‐type or mutant FLAG ‐Sld3 was added to an S‐phase protein extract and tested for interaction with Cdc45. Immunoprecipitated proteins were analysed by immunoblot. Reaction scheme for in vitro replication reactions. Reaction mixtures were removed after each step. Reaction performed as in (G). Nascent DNA was separated in a 0.7% alkaline agarose gel in this and all subsequent replication reactions.

    Journal: The EMBO Journal

    Article Title: Phosphopeptide binding by Sld3 links Dbf4‐dependent kinase to MCM replicative helicase activation

    doi: 10.15252/embj.201593552

    Figure Lengend Snippet: DDK promotes Sld3‐dependent Cdc45 recruitment Reaction scheme for Sld3/7/Cdc45 recruitment experiments. DNA substrate was bound to beads, and reaction mixtures were removed after each step. Immunoblots of recruitment reactions performed as described in (A), with the indicated proteins omitted. In (C), a mid‐reaction wash in high salt (0.5 M NaCl) buffer ( HSW ) was included following DDK phosphorylation as indicated. Recruitment reaction performed as in (A), using wild‐type (wt) or a Cdc45‐binding mutant (3E1) of Sld3. Schematic showing the position of Cdc45‐interacting region in Sld3. Alignments were generated in Jalview using Clustal. Sld3 from various fungal species is included (S.c., Saccharomyces cerevisiae , S.m., Saccharomyces mikatae, S.b., Saccharomyces bayanus, S.ca., Saccharomyces castellii, S.ku., Saccharomyces kudriavzevii ). Residue numbers correspond to S. cerevisiae Sld3. Residues were substituted for Glu as indicated. Wild‐type or mutant FLAG ‐Sld3 was added to an S‐phase protein extract and tested for interaction with Cdc45. Immunoprecipitated proteins were analysed by immunoblot. Reaction scheme for in vitro replication reactions. Reaction mixtures were removed after each step. Reaction performed as in (G). Nascent DNA was separated in a 0.7% alkaline agarose gel in this and all subsequent replication reactions.

    Article Snippet: The supernatant was subjected to GST affinity purification by incubation with 0.8 ml packed bead volume of glutathione sepharose resin (GE Healthcare) that had been pre‐washed in buffer A/500 mM KCl.

    Techniques: Western Blot, Binding Assay, Mutagenesis, Generated, Immunoprecipitation, In Vitro, Agarose Gel Electrophoresis

    Lentiviral IN affinity for imp7 correlates with infection phenotype in imp7 KD cells . (A) GST-imp7 (top left), GST (middle), or GST-LEDGF 326–530 (bottom) immobilized on glutathione sepharose beads were incubated in the absence (lane 1), or presence (lanes 2–6) of untagged recombinant HIV-1, HIV-2, SIVmac, EIAV, or BIV IN in the pull-down buffer containing 130 mM NaCl. Proteins bound to glutathione sepharose beads were resolved in an SDS PAGE gel and detected by staining with Coomassie Blue. Input quantities of each soluble protein used are shown to the right. Migration positions of GST-Imp7, INs, GST, and GST-LEDGF 326–530 , and the molecular weight markers are indicated. (B) Non-tagged Imp7 was incubated in the absence (lane 3) or presence (lanes 4–9) of C-terminally hexahistidine-tagged INs from HIV-1, HIV-2, SIVmac, EIAV, BIV and Ni-NTA agarose beads in a pull down buffer containing 150 mM NaCl. Proteins captured on the resin were separated in a tricine SDS PAGE gel and detected with Coomassie Blue. Lanes 1 and 2 show 100% and 20% Imp7 input, respectively. (C) GST (lanes 3, 6, 9, 12, 15), GST-LEDGF 326–530 (lanes 4, 7, 10, 13, 16), or GST-imp7 (lanes 5, 8, 11, 14, 17) were incubated without (lanes 3–5), or with non-tagged HIV-1 (lanes 6–8, 12–14) or HIV-2 (lanes 9–11, 15–16) INs. The pull-down buffer contained 150 mM (lanes 3–11) or 400 mM (lanes 12–17) NaCl. Lanes 1 and 2 contained input quantities of HIV-1 and HIV-2 INs, respectively. (D) DxR KD and imp7 KD cell populations were infected with VSV-G pseudotyped HIV-1, (pHR'), SIVmac, HIV-2 and EIAV vectors expressing GFP at an MOI of 0.03 and the percentage of GFP+ cells counted 24 hours after infection by flow cytometry. Data are expressed as average percentage of infection relative to control (shDxR) ± SD of two independent experiments performed in duplicate.

    Journal: Retrovirology

    Article Title: HIV-1 exploits importin 7 to maximize nuclear import of its DNA genome

    doi: 10.1186/1742-4690-6-11

    Figure Lengend Snippet: Lentiviral IN affinity for imp7 correlates with infection phenotype in imp7 KD cells . (A) GST-imp7 (top left), GST (middle), or GST-LEDGF 326–530 (bottom) immobilized on glutathione sepharose beads were incubated in the absence (lane 1), or presence (lanes 2–6) of untagged recombinant HIV-1, HIV-2, SIVmac, EIAV, or BIV IN in the pull-down buffer containing 130 mM NaCl. Proteins bound to glutathione sepharose beads were resolved in an SDS PAGE gel and detected by staining with Coomassie Blue. Input quantities of each soluble protein used are shown to the right. Migration positions of GST-Imp7, INs, GST, and GST-LEDGF 326–530 , and the molecular weight markers are indicated. (B) Non-tagged Imp7 was incubated in the absence (lane 3) or presence (lanes 4–9) of C-terminally hexahistidine-tagged INs from HIV-1, HIV-2, SIVmac, EIAV, BIV and Ni-NTA agarose beads in a pull down buffer containing 150 mM NaCl. Proteins captured on the resin were separated in a tricine SDS PAGE gel and detected with Coomassie Blue. Lanes 1 and 2 show 100% and 20% Imp7 input, respectively. (C) GST (lanes 3, 6, 9, 12, 15), GST-LEDGF 326–530 (lanes 4, 7, 10, 13, 16), or GST-imp7 (lanes 5, 8, 11, 14, 17) were incubated without (lanes 3–5), or with non-tagged HIV-1 (lanes 6–8, 12–14) or HIV-2 (lanes 9–11, 15–16) INs. The pull-down buffer contained 150 mM (lanes 3–11) or 400 mM (lanes 12–17) NaCl. Lanes 1 and 2 contained input quantities of HIV-1 and HIV-2 INs, respectively. (D) DxR KD and imp7 KD cell populations were infected with VSV-G pseudotyped HIV-1, (pHR'), SIVmac, HIV-2 and EIAV vectors expressing GFP at an MOI of 0.03 and the percentage of GFP+ cells counted 24 hours after infection by flow cytometry. Data are expressed as average percentage of infection relative to control (shDxR) ± SD of two independent experiments performed in duplicate.

    Article Snippet: For GST pull-downs, 10 micrograms BSA and 10 micrograms untagged IN protein were added to ice-cold suspension of 15 μl glutathione sepharose (settled resin volume) carrying immobilized GST or a GST fusion protein (2 mg/ml) in 800 μl pull down buffer 1 (PDB1: 130 mM NaCl, 2 mM MgCl2 , 2 mM DTT, 0.1% NP-40, 50 mM Bis-Tris propane-HCl, pH 7.45).

    Techniques: Infection, Incubation, Recombinant, SDS Page, Staining, Migration, Molecular Weight, Expressing, Flow Cytometry, Cytometry