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    GE Healthcare glutathione sepharose resin ge healthcare
    Glutathione Sepharose Resin Ge Healthcare, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 289 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare glutathione sepharose
    Glutathione Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 10236 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore glutathione sepharose
    Mutation of S2152A within FLNa abolishes TCR-mediated T-cell adhesion, interaction with APCs and LFA-1 activation. (A) Jurkat T cells were transiently transfected with dsRed C1 vector (dsRed) or plasmids encoding wild type (WT) dsRed-tagged FLNa (FLNa WT) or dsRed-tagged S2152A or dsRed-tagged S2152E FLNa mutants (FLNa S215A and FLNa S2152E). After 24 h the expression of WT and its mutants were analyzed by anti-dsRed and FLNa immunoblotting. Detection of β-actin served as loading control. (B) Jurkat T cells transfected as described in (A) were left untreated (non) or stimulated for 30 min with CD3 antibodies. Cells were analyzed for adhesion to ICAM-1-coated 96 well plates. Bound cells were counted and calculated as percentage of input ( n = 4) (mean ± SEM; * p ≤ 0.05, *** p ≤ 0.001). (C) Cells were transfected as described in (A) and analyzed for their ability to form conjugates with DDAO-SE (red)-stained Raji B cells that were pulsed without (non) or with superantigen (SA) for 30 min at 37°C. The percentage of conjugates was defined as the number of double-positive events in the upper right quadrant ( n = 4) (mean ± SEM; *** p ≤ 0.001). (D) Jurkat T cells transfected as described in (A) were left untreated (non) or stimulated with anti-CD3 antibodies (CD3), followed by staining with the anti-LFA-1 antibody mAb24 to detect the high affinity conformation of LFA-1. mAb24 epitope expression was assessed by flow cytometry and data are normalized against LFA-1 expression detected by MEM48 ( n = 4) (mean ± SEM; *** p ≤ 0.001). (E) HEK 293T cells were transfected with either dsRed, dsRed-tagged FLNa wild type (FLAa WT) or its mutants (FLNa S2152A and FLNa S2152E). 24 h after transfection, whole cell extracts were prepared and analyzed for the expression of dsRed and dsRed-tagged FLNa forms by Western blotting using the indicated antibodies (left panel). Lysates were incubated with GST-fusion proteins bound to <t>glutathione-sepharose</t> beads. Precipitates were analyzed by Western blotting using the indicated antibodies (right panel). One representative experiment of 3 is shown. (mean ± SEM; * p ≤ 0.05, *** p ≤ 0.001).
    Glutathione Sepharose, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 557 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose gsh sepharose
    Interaction between Atf1 and APC/C. A , extracts were prepared from cultures of wild-type ( apc5 + - HA ) cells expressing GST alone or GST-Atf1. Atf1-binding proteins were isolated by <t>GSH-Sepharose</t> beads and analyzed by SDS-PAGE followed by immunoblotting
    Glutathione Sepharose Gsh Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare glutathione sepharose beads
    Anti-AQP1 specificity of the identified autoantibodies. (A) Patient’s autoantibodies recognize the AQP1 moiety of AQP1-GST. Five sera that had tested positive for binding to the AQP1-GST fusion protein were preincubated with an excess of GST immobilized on <t>Sepharose-glutathione</t> beads, then were tested by RIPA using 125 I-streptavidin labeled AQP1-GST. (B) Binding of anti-AQP1 autoantibodies is specifically inhibited by an extract from AQP1-expressing HEK293 cells, but not control HEK293 cells. Four anti-AQP1-positive sera were preincubated with extracts prepared from either EGFP-transfected or AQP1-GFP-transfected HEK293 cells, then were tested by RIPA for binding to the commercial AQP1 preparation. (C) Binding of anti-AQP1 autoantibodies is specifically inhibited by yeast-expressed human AQP1. Four exclusively anti-AQP1-positive sera were preincubated with human AQP1 or AQP4 that had been expressed in yeast and purified or with BSA as control, then were tested by RIPA using 125 I-streptavidin-labeled commercial AQP1-GST fusion protein. (D) AQP1 autoantibody binding is independent of the source of AQP1. Both the commercial AQP1-GST fusion protein and the in house AQP1 purified from yeast were biotinylated, indirectly labeled by preincubation with 125 I-streptavidin, and used in the RIPA. Five anti-AQP1-positive sera and one serum sample from a healthy control (HC) were tested.
    Glutathione Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 15875 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose columns
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose Columns, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 417 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 6b
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose 6b, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 95/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose slurry
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose Slurry, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 104 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4ff
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose 4ff, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 87/100, based on 114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose fastflow
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose Fastflow, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4bbeads
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose 4bbeads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare 4mb glutathione sepharose
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    4mb Glutathione Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose matrix
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose Matrix, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    GE Healthcare glutathione tagged sepharose
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Tagged Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare preequilibrated glutathione sepharose
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Preequilibrated Glutathione Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4btm
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose 4btm, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione 4fastflow sepharose
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione 4fastflow Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4b cartridge
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose 4b Cartridge, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare gamma glutathione sepharose beads
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Gamma Glutathione Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose gs4b beads
    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
    Glutathione Sepharose Gs4b Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. <t>Glutathione-Sepharose</t> beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P
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    Image Search Results


    Mutation of S2152A within FLNa abolishes TCR-mediated T-cell adhesion, interaction with APCs and LFA-1 activation. (A) Jurkat T cells were transiently transfected with dsRed C1 vector (dsRed) or plasmids encoding wild type (WT) dsRed-tagged FLNa (FLNa WT) or dsRed-tagged S2152A or dsRed-tagged S2152E FLNa mutants (FLNa S215A and FLNa S2152E). After 24 h the expression of WT and its mutants were analyzed by anti-dsRed and FLNa immunoblotting. Detection of β-actin served as loading control. (B) Jurkat T cells transfected as described in (A) were left untreated (non) or stimulated for 30 min with CD3 antibodies. Cells were analyzed for adhesion to ICAM-1-coated 96 well plates. Bound cells were counted and calculated as percentage of input ( n = 4) (mean ± SEM; * p ≤ 0.05, *** p ≤ 0.001). (C) Cells were transfected as described in (A) and analyzed for their ability to form conjugates with DDAO-SE (red)-stained Raji B cells that were pulsed without (non) or with superantigen (SA) for 30 min at 37°C. The percentage of conjugates was defined as the number of double-positive events in the upper right quadrant ( n = 4) (mean ± SEM; *** p ≤ 0.001). (D) Jurkat T cells transfected as described in (A) were left untreated (non) or stimulated with anti-CD3 antibodies (CD3), followed by staining with the anti-LFA-1 antibody mAb24 to detect the high affinity conformation of LFA-1. mAb24 epitope expression was assessed by flow cytometry and data are normalized against LFA-1 expression detected by MEM48 ( n = 4) (mean ± SEM; *** p ≤ 0.001). (E) HEK 293T cells were transfected with either dsRed, dsRed-tagged FLNa wild type (FLAa WT) or its mutants (FLNa S2152A and FLNa S2152E). 24 h after transfection, whole cell extracts were prepared and analyzed for the expression of dsRed and dsRed-tagged FLNa forms by Western blotting using the indicated antibodies (left panel). Lysates were incubated with GST-fusion proteins bound to glutathione-sepharose beads. Precipitates were analyzed by Western blotting using the indicated antibodies (right panel). One representative experiment of 3 is shown. (mean ± SEM; * p ≤ 0.05, *** p ≤ 0.001).

    Journal: Frontiers in Immunology

    Article Title: Filamin A Phosphorylation at Serine 2152 by the Serine/Threonine Kinase Ndr2 Controls TCR-Induced LFA-1 Activation in T Cells

    doi: 10.3389/fimmu.2018.02852

    Figure Lengend Snippet: Mutation of S2152A within FLNa abolishes TCR-mediated T-cell adhesion, interaction with APCs and LFA-1 activation. (A) Jurkat T cells were transiently transfected with dsRed C1 vector (dsRed) or plasmids encoding wild type (WT) dsRed-tagged FLNa (FLNa WT) or dsRed-tagged S2152A or dsRed-tagged S2152E FLNa mutants (FLNa S215A and FLNa S2152E). After 24 h the expression of WT and its mutants were analyzed by anti-dsRed and FLNa immunoblotting. Detection of β-actin served as loading control. (B) Jurkat T cells transfected as described in (A) were left untreated (non) or stimulated for 30 min with CD3 antibodies. Cells were analyzed for adhesion to ICAM-1-coated 96 well plates. Bound cells were counted and calculated as percentage of input ( n = 4) (mean ± SEM; * p ≤ 0.05, *** p ≤ 0.001). (C) Cells were transfected as described in (A) and analyzed for their ability to form conjugates with DDAO-SE (red)-stained Raji B cells that were pulsed without (non) or with superantigen (SA) for 30 min at 37°C. The percentage of conjugates was defined as the number of double-positive events in the upper right quadrant ( n = 4) (mean ± SEM; *** p ≤ 0.001). (D) Jurkat T cells transfected as described in (A) were left untreated (non) or stimulated with anti-CD3 antibodies (CD3), followed by staining with the anti-LFA-1 antibody mAb24 to detect the high affinity conformation of LFA-1. mAb24 epitope expression was assessed by flow cytometry and data are normalized against LFA-1 expression detected by MEM48 ( n = 4) (mean ± SEM; *** p ≤ 0.001). (E) HEK 293T cells were transfected with either dsRed, dsRed-tagged FLNa wild type (FLAa WT) or its mutants (FLNa S2152A and FLNa S2152E). 24 h after transfection, whole cell extracts were prepared and analyzed for the expression of dsRed and dsRed-tagged FLNa forms by Western blotting using the indicated antibodies (left panel). Lysates were incubated with GST-fusion proteins bound to glutathione-sepharose beads. Precipitates were analyzed by Western blotting using the indicated antibodies (right panel). One representative experiment of 3 is shown. (mean ± SEM; * p ≤ 0.05, *** p ≤ 0.001).

    Article Snippet: GST, GST-tagged Igl repeats 19–24 of human FLNa and GST-tagged cytoplasmic domain of CD18 (GST-CD18cyt ) were expressed in BL21 (DE3) cells and purified using glutathione-sepharose (Novagen or GE Healthcare) according to the manufacturer's instructions.

    Techniques: Mutagenesis, Activation Assay, Transfection, Plasmid Preparation, Expressing, Staining, Flow Cytometry, Cytometry, Western Blot, Incubation

    Interaction between Atf1 and APC/C. A , extracts were prepared from cultures of wild-type ( apc5 + - HA ) cells expressing GST alone or GST-Atf1. Atf1-binding proteins were isolated by GSH-Sepharose beads and analyzed by SDS-PAGE followed by immunoblotting

    Journal: The Journal of Biological Chemistry

    Article Title: The Transcription Factor Atf1 Binds and Activates the APC/C Ubiquitin Ligase in Fission Yeast *

    doi: 10.1074/jbc.M109.018309

    Figure Lengend Snippet: Interaction between Atf1 and APC/C. A , extracts were prepared from cultures of wild-type ( apc5 + - HA ) cells expressing GST alone or GST-Atf1. Atf1-binding proteins were isolated by GSH-Sepharose beads and analyzed by SDS-PAGE followed by immunoblotting

    Article Snippet: Ectopically expressed GST-Atf1 or endogenous Atf1 was isolated from equal amounts of extracts (∼1 mg) with glutathione (GSH)-Sepharose 4B (GE Healthcare) or anti-Atf1 antibodies ( ) bound Affi-prep-protein A (Bio-Rad) affinity chromatography, respectively, analyzed by SDS-PAGE followed by immunoblotting with anti-HA antibody (12CA5, 1:3,000; Roche Applied Science).

    Techniques: Expressing, Binding Assay, Isolation, SDS Page

    Anti-AQP1 specificity of the identified autoantibodies. (A) Patient’s autoantibodies recognize the AQP1 moiety of AQP1-GST. Five sera that had tested positive for binding to the AQP1-GST fusion protein were preincubated with an excess of GST immobilized on Sepharose-glutathione beads, then were tested by RIPA using 125 I-streptavidin labeled AQP1-GST. (B) Binding of anti-AQP1 autoantibodies is specifically inhibited by an extract from AQP1-expressing HEK293 cells, but not control HEK293 cells. Four anti-AQP1-positive sera were preincubated with extracts prepared from either EGFP-transfected or AQP1-GFP-transfected HEK293 cells, then were tested by RIPA for binding to the commercial AQP1 preparation. (C) Binding of anti-AQP1 autoantibodies is specifically inhibited by yeast-expressed human AQP1. Four exclusively anti-AQP1-positive sera were preincubated with human AQP1 or AQP4 that had been expressed in yeast and purified or with BSA as control, then were tested by RIPA using 125 I-streptavidin-labeled commercial AQP1-GST fusion protein. (D) AQP1 autoantibody binding is independent of the source of AQP1. Both the commercial AQP1-GST fusion protein and the in house AQP1 purified from yeast were biotinylated, indirectly labeled by preincubation with 125 I-streptavidin, and used in the RIPA. Five anti-AQP1-positive sera and one serum sample from a healthy control (HC) were tested.

    Journal: PLoS ONE

    Article Title: Anti-Aquaporin-1 Autoantibodies in Patients with Neuromyelitis Optica Spectrum Disorders

    doi: 10.1371/journal.pone.0074773

    Figure Lengend Snippet: Anti-AQP1 specificity of the identified autoantibodies. (A) Patient’s autoantibodies recognize the AQP1 moiety of AQP1-GST. Five sera that had tested positive for binding to the AQP1-GST fusion protein were preincubated with an excess of GST immobilized on Sepharose-glutathione beads, then were tested by RIPA using 125 I-streptavidin labeled AQP1-GST. (B) Binding of anti-AQP1 autoantibodies is specifically inhibited by an extract from AQP1-expressing HEK293 cells, but not control HEK293 cells. Four anti-AQP1-positive sera were preincubated with extracts prepared from either EGFP-transfected or AQP1-GFP-transfected HEK293 cells, then were tested by RIPA for binding to the commercial AQP1 preparation. (C) Binding of anti-AQP1 autoantibodies is specifically inhibited by yeast-expressed human AQP1. Four exclusively anti-AQP1-positive sera were preincubated with human AQP1 or AQP4 that had been expressed in yeast and purified or with BSA as control, then were tested by RIPA using 125 I-streptavidin-labeled commercial AQP1-GST fusion protein. (D) AQP1 autoantibody binding is independent of the source of AQP1. Both the commercial AQP1-GST fusion protein and the in house AQP1 purified from yeast were biotinylated, indirectly labeled by preincubation with 125 I-streptavidin, and used in the RIPA. Five anti-AQP1-positive sera and one serum sample from a healthy control (HC) were tested.

    Article Snippet: To test whether the antibodies bound to the AQP1 moiety of the AQP1-GST fusion protein, 10 µl of sera positive for anti-AQP1 autoantibodies was preincubated for 3 h at 4°C with excess GST (1.6 µg) immobilized on Sepharose-glutathione beads (GE Healthcare), then 5 µl of the treated samples was tested in the RIPA using 125 I-streptavidin-labeled AQP1-GST.

    Techniques: Binding Assay, Labeling, Expressing, Transfection, Purification

    The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. Glutathione-Sepharose beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P

    Journal: Scientific Reports

    Article Title: Novel Coronin7 interactions with Cdc42 and N-WASP regulate actin organization and Golgi morphology

    doi: 10.1038/srep25411

    Figure Lengend Snippet: The CRIB motifs in mammalian CRN7 and their impact on the rescue activity of the protein. ( a ) Sequence alignment of human CRN7-CRIB domains (NT and CT) with CRIB domains from human Coronin 1C and D. discoideum CRN7. The CRIB consensus shown on top. Similar amino acids boxed in yellow. Highly conserved amino acids marked in red. (b) In vitro binding assay for full length GFP-CRN7WT with Rac1 and Cdc42 GTPases in their CA/Q61L and DN/T17N forms. Glutathione-Sepharose beads coated with GST alone and GST fusions pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing GFP-CRN7. PonceauS staining shows the GST fusion proteins. GFP-CRN7 detected with GFP-specific mAb K3-184-2. (c) Quantification of GFP-CRN7 bound to Rac and Cdc42 proteins (CA and DN) using ImageJ. Input set at 100% (3 independent experiments; **P

    Article Snippet: GST-Cdc42 or CRN7 mutants were expressed in E. coli BL21 and purified from the soluble fraction using Glutathione Sepharose affinity columns (GE Healthcare).

    Techniques: Activity Assay, Sequencing, In Vitro, Binding Assay, Incubation, Expressing, Staining

    Effect of CRN7-CRIB motif mutations on Cdc42 binding and rescue potential of the proteins. ( a ) Conserved residues in the N- and C-terminal CRIB domains boxed in yellow were mutated to alanine marked in red. The GFP tag is at the N-terminus. ( b ) Binding assay for GFP-CRN7 WT and CRIB mutants (Mut1 and 2, left panel; Mut3 and 4, right panel) with Cdc42 GTPase (CA and DN). Glutathione-Sepharose beads coated with GST fusions, pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing the CRN7 WT or CRIB mutants. PonceauS staining shows the GST fusion proteins. Probing was with mAb K3-184-2. (c) Bar graph showing quantification of GFP-CRN7 WT and CRIB mutants bound to Cdc42 CA and DN using ImageJ. Input set at 100% (3 independent experiments; **P

    Journal: Scientific Reports

    Article Title: Novel Coronin7 interactions with Cdc42 and N-WASP regulate actin organization and Golgi morphology

    doi: 10.1038/srep25411

    Figure Lengend Snippet: Effect of CRN7-CRIB motif mutations on Cdc42 binding and rescue potential of the proteins. ( a ) Conserved residues in the N- and C-terminal CRIB domains boxed in yellow were mutated to alanine marked in red. The GFP tag is at the N-terminus. ( b ) Binding assay for GFP-CRN7 WT and CRIB mutants (Mut1 and 2, left panel; Mut3 and 4, right panel) with Cdc42 GTPase (CA and DN). Glutathione-Sepharose beads coated with GST fusions, pre-loaded with GDP (DN) or GTPγS (CA) and incubated with lysates from HEK293T cells expressing the CRN7 WT or CRIB mutants. PonceauS staining shows the GST fusion proteins. Probing was with mAb K3-184-2. (c) Bar graph showing quantification of GFP-CRN7 WT and CRIB mutants bound to Cdc42 CA and DN using ImageJ. Input set at 100% (3 independent experiments; **P

    Article Snippet: GST-Cdc42 or CRN7 mutants were expressed in E. coli BL21 and purified from the soluble fraction using Glutathione Sepharose affinity columns (GE Healthcare).

    Techniques: Binding Assay, Incubation, Expressing, Staining