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    GE Healthcare gstrap ff column
    Specific binding of PpAtg24 phox homology (PX) domain to phosphatidylinositol-3-phosphate (PtdIns(3)P). (A) Purity of the <t>GST-PpAtg24</t> PX domain detected on SDS-PAGE. The GST-fused PpAtg24 PX domain was purified using an E. coli Rosetta DE3 by <t>GSTrap</t> FF
    Gstrap Ff Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 2296 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Specific binding of PpAtg24 phox homology (PX) domain to phosphatidylinositol-3-phosphate (PtdIns(3)P). (A) Purity of the GST-PpAtg24 PX domain detected on SDS-PAGE. The GST-fused PpAtg24 PX domain was purified using an E. coli Rosetta DE3 by GSTrap FF

    Journal: Molecular Biology of the Cell

    Article Title: A Sorting Nexin PpAtg24 Regulates Vacuolar Membrane Dynamics during Pexophagy via Binding to Phosphatidylinositol-3-Phosphate D⃞

    doi: 10.1091/mbc.E04-09-0842

    Figure Lengend Snippet: Specific binding of PpAtg24 phox homology (PX) domain to phosphatidylinositol-3-phosphate (PtdIns(3)P). (A) Purity of the GST-PpAtg24 PX domain detected on SDS-PAGE. The GST-fused PpAtg24 PX domain was purified using an E. coli Rosetta DE3 by GSTrap FF

    Article Snippet: The GST fusion protein was purified using a GSTrap FF column (Amersham Pharmacia Biotech).

    Techniques: Binding Assay, SDS Page, Purification

    Recombinant derivatives of KRMP-3. (A) Schematic representation of KRMP-3, rKRMP-3, rBR and rGYR. KRMP-3, wild-type full-length KRMP-3 containing the signal peptide (SP) sequence and consisting of 101 amino acid residues; rKRMP-3, KRMP-3 devoid of the SP sequence and contains 81 amino acid residues and its N-terminally tagged with an affinity GST; rBR, the basic region of KRMP-3 containing 43 amino acid residues (21–63) and N-terminally tagged with an affinity GST; rGYR, the Gly/Tyr-rich region of KRMP-3 containing the C-terminal 38 amino acid residues (64–101) and N-terminally tagged with GST as well. (B) Expression and purification of recombinant KRMP-3, GYR and BR in E . coli . Arrows represent the induced proteins by IPTG. M: protein molecular mass markers; lane 1: uninduced whole-cell lysate; lane 2, 4, 6: whole-cell lysate of rKRMP-3, rGYR and rBR induced by 0.8 mM IPTG; lane 3, 5, 7: purified rKRMP-3, rGYR and rBR eluted from GSTrap FFcolumn.

    Journal: PLoS ONE

    Article Title: Dual Roles of the Lysine-Rich Matrix Protein (KRMP)-3 in Shell Formation of Pearl Oyster, Pinctada fucata

    doi: 10.1371/journal.pone.0131868

    Figure Lengend Snippet: Recombinant derivatives of KRMP-3. (A) Schematic representation of KRMP-3, rKRMP-3, rBR and rGYR. KRMP-3, wild-type full-length KRMP-3 containing the signal peptide (SP) sequence and consisting of 101 amino acid residues; rKRMP-3, KRMP-3 devoid of the SP sequence and contains 81 amino acid residues and its N-terminally tagged with an affinity GST; rBR, the basic region of KRMP-3 containing 43 amino acid residues (21–63) and N-terminally tagged with an affinity GST; rGYR, the Gly/Tyr-rich region of KRMP-3 containing the C-terminal 38 amino acid residues (64–101) and N-terminally tagged with GST as well. (B) Expression and purification of recombinant KRMP-3, GYR and BR in E . coli . Arrows represent the induced proteins by IPTG. M: protein molecular mass markers; lane 1: uninduced whole-cell lysate; lane 2, 4, 6: whole-cell lysate of rKRMP-3, rGYR and rBR induced by 0.8 mM IPTG; lane 3, 5, 7: purified rKRMP-3, rGYR and rBR eluted from GSTrap FFcolumn.

    Article Snippet: Purification of rKRMP-3, rBR and rGYR The GST-tagged recombinant proteins were purified by GSTrap FF columns (GE Healthcare).

    Techniques: Recombinant, Sequencing, Expressing, Purification

    Purification of recombinant LBH from E. coli . (A) Coding region of the recombinant pGEX-2T-LBH expression vector depicting the thrombin cleavage site and the BamHI restriction enzyme recognition sequences (italics) used to directionally clone the LBH coding region into pGEX-2T. (B) SDS-PAGE analysis with Coomassie staining. M: Molecular weight standard; lane 1: total soluble lysate; lane 2: proteins from the soluble lysate that were not retained on the GST Sepharose High Trap HP affinity column; lane 3: proteins that were retained and subsequently eluted from the GSTrap HP affinity column; lane 4: protein products after thrombin digestion; and lane 5: purified LBH resolved by Superdex™ 75 size-exclusion chromatography.

    Journal: Biochemical and biophysical research communications

    Article Title: Biophysical Characterization Reveals Structural Disorder in the Developmental Transcriptional Regulator LBH

    doi: 10.1016/j.bbrc.2009.12.032

    Figure Lengend Snippet: Purification of recombinant LBH from E. coli . (A) Coding region of the recombinant pGEX-2T-LBH expression vector depicting the thrombin cleavage site and the BamHI restriction enzyme recognition sequences (italics) used to directionally clone the LBH coding region into pGEX-2T. (B) SDS-PAGE analysis with Coomassie staining. M: Molecular weight standard; lane 1: total soluble lysate; lane 2: proteins from the soluble lysate that were not retained on the GST Sepharose High Trap HP affinity column; lane 3: proteins that were retained and subsequently eluted from the GSTrap HP affinity column; lane 4: protein products after thrombin digestion; and lane 5: purified LBH resolved by Superdex™ 75 size-exclusion chromatography.

    Article Snippet: After centrifugation for 30 min at 35,000 g , the soluble fraction containing the GST-LBH fusion protein was loaded at a flow rate of 1 mL/min onto tandem 5 mL GSTrap FF affinity columns (equilibrated at 4°C in GST-binding buffer) connected to an AKTAbasic 100 Explorer FPLC system (GE Healthcare).

    Techniques: Purification, Recombinant, Expressing, Plasmid Preparation, SDS Page, Staining, Molecular Weight, Affinity Column, Size-exclusion Chromatography

    Quantitative measurement confirms that BD 245 work together to create high affinity to H3K14ac. (A) The indicated GST ‐ BD constructs of PBRM 1 were expressed and purified from Escherichia coli , pulled down by the indicated peptides, and immunoblotted with anti‐ GST antibody. (B) The bands in (A) were quantified with NIH ImageJ, and the ratios of bands associated with H3K14ac/H3 were calculated from three experiments. The P ‐values were calculated using the two‐tailed Student's t ‐test. *: P

    Journal: Molecular Oncology

    Article Title: High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1

    doi: 10.1002/1878-0261.12434

    Figure Lengend Snippet: Quantitative measurement confirms that BD 245 work together to create high affinity to H3K14ac. (A) The indicated GST ‐ BD constructs of PBRM 1 were expressed and purified from Escherichia coli , pulled down by the indicated peptides, and immunoblotted with anti‐ GST antibody. (B) The bands in (A) were quantified with NIH ImageJ, and the ratios of bands associated with H3K14ac/H3 were calculated from three experiments. The P ‐values were calculated using the two‐tailed Student's t ‐test. *: P

    Article Snippet: 2.2 Protein expression and purification Polybromo‐1 constructs consisting of BD2, BD4, BD234, and BD245 were subcloned into pGST parallel expression vectors (Sheffield et al ., ) individually expressed in Escherichia coli strain BL21, purified over a GST column (GE Healthcare, Pittsburgh, PA, USA; Catalog #17‐5130‐01), eluted with 10 mm reduced glutathione, and dialyzed against 2 L of dialysis buffer (25 mm Tris/HCl, 500 mm NaCl, pH 8.0) to remove glutathione.

    Techniques: Construct, Purification, Two Tailed Test

    10D7 antibody binds to the GTP-bound form of native cellular Irga6 but not to a myristoylation-deficient mutant. L929 fibroblasts were transfected with Irga6wt, -G2A, -Δ7-12, -K82A, -S83N, or -E106A constructs. Cells were lysed 24 h later in Thesit in the absence or presence of 0.5 m m GTPγS, and Irga6 was immunoprecipitated with 10D7-Protein A-Sepharose beads. Irga6 proteins were detected in Western blot by rabbit anti-Irga6 polyclonal 165 serum. Signals were quantified using ImageQuant TLv2005, and values for immunoprecipitated proteins were normalized to the corresponding lysates. Mean values of at least three independent experiments are shown in the histogram . The 10D7 epitope is dependent on GTPγS in wild type Irga6 but constitutively expressed in functionally dominant negative mutants Irga6-K82A and -E106A. The myristoylation-deficient mutant, Irga6-G2A, cannot express the 10D7 epitope whether GTPγS is present or not. The mutant Irga6-Δ7-12 expresses 10D7 epitope independently of GTPγS.

    Journal: The Journal of Biological Chemistry

    Article Title: Inactive and Active States of the Interferon-inducible Resistance GTPase, Irga6, in Vivo * * S⃞

    doi: 10.1074/jbc.M804846200

    Figure Lengend Snippet: 10D7 antibody binds to the GTP-bound form of native cellular Irga6 but not to a myristoylation-deficient mutant. L929 fibroblasts were transfected with Irga6wt, -G2A, -Δ7-12, -K82A, -S83N, or -E106A constructs. Cells were lysed 24 h later in Thesit in the absence or presence of 0.5 m m GTPγS, and Irga6 was immunoprecipitated with 10D7-Protein A-Sepharose beads. Irga6 proteins were detected in Western blot by rabbit anti-Irga6 polyclonal 165 serum. Signals were quantified using ImageQuant TLv2005, and values for immunoprecipitated proteins were normalized to the corresponding lysates. Mean values of at least three independent experiments are shown in the histogram . The 10D7 epitope is dependent on GTPγS in wild type Irga6 but constitutively expressed in functionally dominant negative mutants Irga6-K82A and -E106A. The myristoylation-deficient mutant, Irga6-G2A, cannot express the 10D7 epitope whether GTPγS is present or not. The mutant Irga6-Δ7-12 expresses 10D7 epitope independently of GTPγS.

    Article Snippet: The soluble fraction was purified on a glutathione-Sepharose affinity column (GSTrap FF 5 ml; Amersham Biosciences) equilibrated with PBS, 2 mm dithiothreitol.

    Techniques: Mutagenesis, Transfection, Construct, Immunoprecipitation, Western Blot, Dominant Negative Mutation