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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 10185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose beads
    TBK1 phosphorylates RKIP at serine 109 BMDM cells were infected with VSV (MOI 0.1) or HSV (MOI 5) for the indicated times. Cell lysates were analyzed by immunoblotting with the indicated antibodies. BMDM cells were transfected with control or TBK1 siRNA. 72 h after transfection, cells were analyzed by immunoblotting with antibodies for phospho‐RKIP or TBK1. Immunoblot analysis of RKIP phosphorylation in control or TBK1 −/− mouse embryonic fibroblasts after VSV (MOI 0.1) infection for the indicated times. Recombinant flag‐tagged TBK1 was immunoprecipitated with anti‐flag M2 beads in flag‐TBK1‐transfected 293T cells. Followed this, in vitro kinase assay was carried out in the reaction mixture containing 2 mM ATP, 100 μM GST‐RKIP, or 100 μM GST‐GFP together with 5 μM flag‐TBK1 at 30°C for 30 min. Assay mixtures were immunoblotted with the indicated antibodies for phospho‐RKIP, flag, GST, or his. Immunoblot analysis of extracts of RAW264.7 cells stably overexpressing flag‐RKIP, flag‐S109A, and flag‐S109D, and infected with VSV (MOI 0.1) for the indicated times, followed by immunoprecipitation with anti‐flag beads. BMDM cells were infected with VSV (MOI 0.1) for the indicated times. The cell lysates were immunoprecipitated with anti‐TBK1 (left) or anti‐RKIP (right). The immunoprecipitates were analyzed by immunoblot with anti‐RKIP or anti‐TBK1 antibody. The levels of the endogenous RKIP, TBK1, and p‐RKIP were detected by immunoblot analysis. Co‐immunoprecipitation and immunoblot analysis of 293T cells transfected with myc‐TBK1 alone or with flag‐RKIP, flag‐S109A, or flag‐S109D. GST pull‐down experiment was performed with 1 μg fusion protein GST‐GFP, GST‐his‐RKIP, or GST‐his‐S109D mixed with 20 μl pre‐cleared <t>agarose</t> beads in 800 μl reaction medium, followed by adding 1 μg flag‐TBK1 and incubating at 4°C for 3 h with gentle rotation. Pull‐down (lane 1–3) and input samples (lane 4) were separated by SDS–PAGE followed by immunoblotting with anti‐GST or anti‐flag antibody. Immunoprecipitation and immunoblot analysis of 293T cells transfected with indicated combinations of vector for myc‐TBK1, flag‐RKIP, flag‐S109A, flag‐S109D, HA‐GSK3β or flag‐GFP. In vitro assay was carried out in the reaction mixture containing 2 mM ATP, 50 μM GST‐TBK1 together with 100 μM GST‐his‐RKIP, 100 μM GST‐his‐S109D, 100 μM GST‐his‐S109A, or 100 μM GST, respectively, at 30°C for 30 min, followed by immunoblotting with anti‐p‐TBK1 or anti‐GST antibody. . Source data are available online for this figure.
    Glutathione Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 15926 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare gamma glutathione sepharose beads
    TBK1 phosphorylates RKIP at serine 109 BMDM cells were infected with VSV (MOI 0.1) or HSV (MOI 5) for the indicated times. Cell lysates were analyzed by immunoblotting with the indicated antibodies. BMDM cells were transfected with control or TBK1 siRNA. 72 h after transfection, cells were analyzed by immunoblotting with antibodies for phospho‐RKIP or TBK1. Immunoblot analysis of RKIP phosphorylation in control or TBK1 −/− mouse embryonic fibroblasts after VSV (MOI 0.1) infection for the indicated times. Recombinant flag‐tagged TBK1 was immunoprecipitated with anti‐flag M2 beads in flag‐TBK1‐transfected 293T cells. Followed this, in vitro kinase assay was carried out in the reaction mixture containing 2 mM ATP, 100 μM GST‐RKIP, or 100 μM GST‐GFP together with 5 μM flag‐TBK1 at 30°C for 30 min. Assay mixtures were immunoblotted with the indicated antibodies for phospho‐RKIP, flag, GST, or his. Immunoblot analysis of extracts of RAW264.7 cells stably overexpressing flag‐RKIP, flag‐S109A, and flag‐S109D, and infected with VSV (MOI 0.1) for the indicated times, followed by immunoprecipitation with anti‐flag beads. BMDM cells were infected with VSV (MOI 0.1) for the indicated times. The cell lysates were immunoprecipitated with anti‐TBK1 (left) or anti‐RKIP (right). The immunoprecipitates were analyzed by immunoblot with anti‐RKIP or anti‐TBK1 antibody. The levels of the endogenous RKIP, TBK1, and p‐RKIP were detected by immunoblot analysis. Co‐immunoprecipitation and immunoblot analysis of 293T cells transfected with myc‐TBK1 alone or with flag‐RKIP, flag‐S109A, or flag‐S109D. GST pull‐down experiment was performed with 1 μg fusion protein GST‐GFP, GST‐his‐RKIP, or GST‐his‐S109D mixed with 20 μl pre‐cleared <t>agarose</t> beads in 800 μl reaction medium, followed by adding 1 μg flag‐TBK1 and incubating at 4°C for 3 h with gentle rotation. Pull‐down (lane 1–3) and input samples (lane 4) were separated by SDS–PAGE followed by immunoblotting with anti‐GST or anti‐flag antibody. Immunoprecipitation and immunoblot analysis of 293T cells transfected with indicated combinations of vector for myc‐TBK1, flag‐RKIP, flag‐S109A, flag‐S109D, HA‐GSK3β or flag‐GFP. In vitro assay was carried out in the reaction mixture containing 2 mM ATP, 50 μM GST‐TBK1 together with 100 μM GST‐his‐RKIP, 100 μM GST‐his‐S109D, 100 μM GST‐his‐S109A, or 100 μM GST, respectively, at 30°C for 30 min, followed by immunoblotting with anti‐p‐TBK1 or anti‐GST antibody. . Source data are available online for this figure.
    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
    TBK1 phosphorylates RKIP at serine 109 BMDM cells were infected with VSV (MOI 0.1) or HSV (MOI 5) for the indicated times. Cell lysates were analyzed by immunoblotting with the indicated antibodies. BMDM cells were transfected with control or TBK1 siRNA. 72 h after transfection, cells were analyzed by immunoblotting with antibodies for phospho‐RKIP or TBK1. Immunoblot analysis of RKIP phosphorylation in control or TBK1 −/− mouse embryonic fibroblasts after VSV (MOI 0.1) infection for the indicated times. Recombinant flag‐tagged TBK1 was immunoprecipitated with anti‐flag M2 beads in flag‐TBK1‐transfected 293T cells. Followed this, in vitro kinase assay was carried out in the reaction mixture containing 2 mM ATP, 100 μM GST‐RKIP, or 100 μM GST‐GFP together with 5 μM flag‐TBK1 at 30°C for 30 min. Assay mixtures were immunoblotted with the indicated antibodies for phospho‐RKIP, flag, GST, or his. Immunoblot analysis of extracts of RAW264.7 cells stably overexpressing flag‐RKIP, flag‐S109A, and flag‐S109D, and infected with VSV (MOI 0.1) for the indicated times, followed by immunoprecipitation with anti‐flag beads. BMDM cells were infected with VSV (MOI 0.1) for the indicated times. The cell lysates were immunoprecipitated with anti‐TBK1 (left) or anti‐RKIP (right). The immunoprecipitates were analyzed by immunoblot with anti‐RKIP or anti‐TBK1 antibody. The levels of the endogenous RKIP, TBK1, and p‐RKIP were detected by immunoblot analysis. Co‐immunoprecipitation and immunoblot analysis of 293T cells transfected with myc‐TBK1 alone or with flag‐RKIP, flag‐S109A, or flag‐S109D. GST pull‐down experiment was performed with 1 μg fusion protein GST‐GFP, GST‐his‐RKIP, or GST‐his‐S109D mixed with 20 μl pre‐cleared <t>agarose</t> beads in 800 μl reaction medium, followed by adding 1 μg flag‐TBK1 and incubating at 4°C for 3 h with gentle rotation. Pull‐down (lane 1–3) and input samples (lane 4) were separated by SDS–PAGE followed by immunoblotting with anti‐GST or anti‐flag antibody. Immunoprecipitation and immunoblot analysis of 293T cells transfected with indicated combinations of vector for myc‐TBK1, flag‐RKIP, flag‐S109A, flag‐S109D, HA‐GSK3β or flag‐GFP. In vitro assay was carried out in the reaction mixture containing 2 mM ATP, 50 μM GST‐TBK1 together with 100 μM GST‐his‐RKIP, 100 μM GST‐his‐S109D, 100 μM GST‐his‐S109A, or 100 μM GST, respectively, at 30°C for 30 min, followed by immunoblotting with anti‐p‐TBK1 or anti‐GST antibody. . Source data are available online for this figure.
    Glutathione Sepharose Gs4b Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4ff beads
    TBK1 phosphorylates RKIP at serine 109 BMDM cells were infected with VSV (MOI 0.1) or HSV (MOI 5) for the indicated times. Cell lysates were analyzed by immunoblotting with the indicated antibodies. BMDM cells were transfected with control or TBK1 siRNA. 72 h after transfection, cells were analyzed by immunoblotting with antibodies for phospho‐RKIP or TBK1. Immunoblot analysis of RKIP phosphorylation in control or TBK1 −/− mouse embryonic fibroblasts after VSV (MOI 0.1) infection for the indicated times. Recombinant flag‐tagged TBK1 was immunoprecipitated with anti‐flag M2 beads in flag‐TBK1‐transfected 293T cells. Followed this, in vitro kinase assay was carried out in the reaction mixture containing 2 mM ATP, 100 μM GST‐RKIP, or 100 μM GST‐GFP together with 5 μM flag‐TBK1 at 30°C for 30 min. Assay mixtures were immunoblotted with the indicated antibodies for phospho‐RKIP, flag, GST, or his. Immunoblot analysis of extracts of RAW264.7 cells stably overexpressing flag‐RKIP, flag‐S109A, and flag‐S109D, and infected with VSV (MOI 0.1) for the indicated times, followed by immunoprecipitation with anti‐flag beads. BMDM cells were infected with VSV (MOI 0.1) for the indicated times. The cell lysates were immunoprecipitated with anti‐TBK1 (left) or anti‐RKIP (right). The immunoprecipitates were analyzed by immunoblot with anti‐RKIP or anti‐TBK1 antibody. The levels of the endogenous RKIP, TBK1, and p‐RKIP were detected by immunoblot analysis. Co‐immunoprecipitation and immunoblot analysis of 293T cells transfected with myc‐TBK1 alone or with flag‐RKIP, flag‐S109A, or flag‐S109D. GST pull‐down experiment was performed with 1 μg fusion protein GST‐GFP, GST‐his‐RKIP, or GST‐his‐S109D mixed with 20 μl pre‐cleared <t>agarose</t> beads in 800 μl reaction medium, followed by adding 1 μg flag‐TBK1 and incubating at 4°C for 3 h with gentle rotation. Pull‐down (lane 1–3) and input samples (lane 4) were separated by SDS–PAGE followed by immunoblotting with anti‐GST or anti‐flag antibody. Immunoprecipitation and immunoblot analysis of 293T cells transfected with indicated combinations of vector for myc‐TBK1, flag‐RKIP, flag‐S109A, flag‐S109D, HA‐GSK3β or flag‐GFP. In vitro assay was carried out in the reaction mixture containing 2 mM ATP, 50 μM GST‐TBK1 together with 100 μM GST‐his‐RKIP, 100 μM GST‐his‐S109D, 100 μM GST‐his‐S109A, or 100 μM GST, respectively, at 30°C for 30 min, followed by immunoblotting with anti‐p‐TBK1 or anti‐GST antibody. . Source data are available online for this figure.
    Glutathione Sepharose 4ff Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione gsh sepharose beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Glutathione Gsh Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 129 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione coated sepharose beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Glutathione Coated Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare slurry glutathione sepharose beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Slurry Glutathione Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4g beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Glutathione Sepharose 4g Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose cl4b beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Glutathione Sepharose Cl4b Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 81/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore glutathione sepharose 4b beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
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    GE Healthcare prepared glutathione sepharose beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Prepared Glutathione Sepharose 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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    GE Healthcare glutathione sepharose 6b beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
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    GE Healthcare glutathione sepharose tm4b beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
    Glutathione Sepharose Tm4b Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare prebounded glutathione sepharose beads
    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on <t>GSH</t> <t>agarose</t> beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.
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    GE Healthcare glutathione sepharose gth beads
    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    GE Healthcare glutathione sepharose high performance beads
    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    GE Healthcare glutathione sepharose 4b matrix beads
    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on <t>GTH</t> beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native <t>agarose</t> gel. Position of Relaxed and Form U DNA is indicated.
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    The 2BC non-structural protein of EV-A71 interacts with syntaxin-17 (STX17) and synaptosome-associated protein of 29 kDa (SNAP29). ( A ) Yeast two-hybrid assays of 2BC and STX17. Yeasts were transformed with pGBKT7 or pGBKT7-STX17 together with pACT2 or pACT2–2BC. Yeasts were then grown on selective medium without tryptophan (-W) or without leucine, tryptophan, and histidine (-LWH); ( B ) HeLa cells were transfected with pDEST27 or pDEST27–2BC in combination with pCherry-STX17 for 48 h. The transfected cells were examined under a confocal microscope with objective 63× (scale bar 10µm) for the presence of co-localization; and ( C ) the Pearson’s correlation coefficient was determined; ( D ) HEK-293T cells were co-transfected with FLAG-STX17 and <t>GST-2BC</t> for 48 h. Lysates were collected for co-immunoprecipitation (IP) using glutathione (GST) <t>sepharose.</t> Western Blot was performed to detect FLAG-STX17 and GST fusion proteins; ( E ) RD cells were infected with EV-A71 for 8 hpi and lysates of infected cells were then harvested prior to co-immunoprecipitation (co-IP) assay using anti-STX17 and anti-SNAP29. The final IP eluates and discarded IP flow through were collected for WB to detect 2BC (anti-2C polyclonal antibody) and structural proteins (mAB979) of EV-A71. One-way ANOVA: * p
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    The 2BC non-structural protein of EV-A71 interacts with syntaxin-17 (STX17) and synaptosome-associated protein of 29 kDa (SNAP29). ( A ) Yeast two-hybrid assays of 2BC and STX17. Yeasts were transformed with pGBKT7 or pGBKT7-STX17 together with pACT2 or pACT2–2BC. Yeasts were then grown on selective medium without tryptophan (-W) or without leucine, tryptophan, and histidine (-LWH); ( B ) HeLa cells were transfected with pDEST27 or pDEST27–2BC in combination with pCherry-STX17 for 48 h. The transfected cells were examined under a confocal microscope with objective 63× (scale bar 10µm) for the presence of co-localization; and ( C ) the Pearson’s correlation coefficient was determined; ( D ) HEK-293T cells were co-transfected with FLAG-STX17 and <t>GST-2BC</t> for 48 h. Lysates were collected for co-immunoprecipitation (IP) using glutathione (GST) <t>sepharose.</t> Western Blot was performed to detect FLAG-STX17 and GST fusion proteins; ( E ) RD cells were infected with EV-A71 for 8 hpi and lysates of infected cells were then harvested prior to co-immunoprecipitation (co-IP) assay using anti-STX17 and anti-SNAP29. The final IP eluates and discarded IP flow through were collected for WB to detect 2BC (anti-2C polyclonal antibody) and structural proteins (mAB979) of EV-A71. One-way ANOVA: * p
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    The 2BC non-structural protein of EV-A71 interacts with syntaxin-17 (STX17) and synaptosome-associated protein of 29 kDa (SNAP29). ( A ) Yeast two-hybrid assays of 2BC and STX17. Yeasts were transformed with pGBKT7 or pGBKT7-STX17 together with pACT2 or pACT2–2BC. Yeasts were then grown on selective medium without tryptophan (-W) or without leucine, tryptophan, and histidine (-LWH); ( B ) HeLa cells were transfected with pDEST27 or pDEST27–2BC in combination with pCherry-STX17 for 48 h. The transfected cells were examined under a confocal microscope with objective 63× (scale bar 10µm) for the presence of co-localization; and ( C ) the Pearson’s correlation coefficient was determined; ( D ) HEK-293T cells were co-transfected with FLAG-STX17 and <t>GST-2BC</t> for 48 h. Lysates were collected for co-immunoprecipitation (IP) using glutathione (GST) <t>sepharose.</t> Western Blot was performed to detect FLAG-STX17 and GST fusion proteins; ( E ) RD cells were infected with EV-A71 for 8 hpi and lysates of infected cells were then harvested prior to co-immunoprecipitation (co-IP) assay using anti-STX17 and anti-SNAP29. The final IP eluates and discarded IP flow through were collected for WB to detect 2BC (anti-2C polyclonal antibody) and structural proteins (mAB979) of EV-A71. One-way ANOVA: * p
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    TBK1 phosphorylates RKIP at serine 109 BMDM cells were infected with VSV (MOI 0.1) or HSV (MOI 5) for the indicated times. Cell lysates were analyzed by immunoblotting with the indicated antibodies. BMDM cells were transfected with control or TBK1 siRNA. 72 h after transfection, cells were analyzed by immunoblotting with antibodies for phospho‐RKIP or TBK1. Immunoblot analysis of RKIP phosphorylation in control or TBK1 −/− mouse embryonic fibroblasts after VSV (MOI 0.1) infection for the indicated times. Recombinant flag‐tagged TBK1 was immunoprecipitated with anti‐flag M2 beads in flag‐TBK1‐transfected 293T cells. Followed this, in vitro kinase assay was carried out in the reaction mixture containing 2 mM ATP, 100 μM GST‐RKIP, or 100 μM GST‐GFP together with 5 μM flag‐TBK1 at 30°C for 30 min. Assay mixtures were immunoblotted with the indicated antibodies for phospho‐RKIP, flag, GST, or his. Immunoblot analysis of extracts of RAW264.7 cells stably overexpressing flag‐RKIP, flag‐S109A, and flag‐S109D, and infected with VSV (MOI 0.1) for the indicated times, followed by immunoprecipitation with anti‐flag beads. BMDM cells were infected with VSV (MOI 0.1) for the indicated times. The cell lysates were immunoprecipitated with anti‐TBK1 (left) or anti‐RKIP (right). The immunoprecipitates were analyzed by immunoblot with anti‐RKIP or anti‐TBK1 antibody. The levels of the endogenous RKIP, TBK1, and p‐RKIP were detected by immunoblot analysis. Co‐immunoprecipitation and immunoblot analysis of 293T cells transfected with myc‐TBK1 alone or with flag‐RKIP, flag‐S109A, or flag‐S109D. GST pull‐down experiment was performed with 1 μg fusion protein GST‐GFP, GST‐his‐RKIP, or GST‐his‐S109D mixed with 20 μl pre‐cleared agarose beads in 800 μl reaction medium, followed by adding 1 μg flag‐TBK1 and incubating at 4°C for 3 h with gentle rotation. Pull‐down (lane 1–3) and input samples (lane 4) were separated by SDS–PAGE followed by immunoblotting with anti‐GST or anti‐flag antibody. Immunoprecipitation and immunoblot analysis of 293T cells transfected with indicated combinations of vector for myc‐TBK1, flag‐RKIP, flag‐S109A, flag‐S109D, HA‐GSK3β or flag‐GFP. In vitro assay was carried out in the reaction mixture containing 2 mM ATP, 50 μM GST‐TBK1 together with 100 μM GST‐his‐RKIP, 100 μM GST‐his‐S109D, 100 μM GST‐his‐S109A, or 100 μM GST, respectively, at 30°C for 30 min, followed by immunoblotting with anti‐p‐TBK1 or anti‐GST antibody. . Source data are available online for this figure.

    Journal: The EMBO Journal

    Article Title: RKIP and TBK1 form a positive feedback loop to promote type I interferon production in innate immunity

    doi: 10.15252/embj.201694060

    Figure Lengend Snippet: TBK1 phosphorylates RKIP at serine 109 BMDM cells were infected with VSV (MOI 0.1) or HSV (MOI 5) for the indicated times. Cell lysates were analyzed by immunoblotting with the indicated antibodies. BMDM cells were transfected with control or TBK1 siRNA. 72 h after transfection, cells were analyzed by immunoblotting with antibodies for phospho‐RKIP or TBK1. Immunoblot analysis of RKIP phosphorylation in control or TBK1 −/− mouse embryonic fibroblasts after VSV (MOI 0.1) infection for the indicated times. Recombinant flag‐tagged TBK1 was immunoprecipitated with anti‐flag M2 beads in flag‐TBK1‐transfected 293T cells. Followed this, in vitro kinase assay was carried out in the reaction mixture containing 2 mM ATP, 100 μM GST‐RKIP, or 100 μM GST‐GFP together with 5 μM flag‐TBK1 at 30°C for 30 min. Assay mixtures were immunoblotted with the indicated antibodies for phospho‐RKIP, flag, GST, or his. Immunoblot analysis of extracts of RAW264.7 cells stably overexpressing flag‐RKIP, flag‐S109A, and flag‐S109D, and infected with VSV (MOI 0.1) for the indicated times, followed by immunoprecipitation with anti‐flag beads. BMDM cells were infected with VSV (MOI 0.1) for the indicated times. The cell lysates were immunoprecipitated with anti‐TBK1 (left) or anti‐RKIP (right). The immunoprecipitates were analyzed by immunoblot with anti‐RKIP or anti‐TBK1 antibody. The levels of the endogenous RKIP, TBK1, and p‐RKIP were detected by immunoblot analysis. Co‐immunoprecipitation and immunoblot analysis of 293T cells transfected with myc‐TBK1 alone or with flag‐RKIP, flag‐S109A, or flag‐S109D. GST pull‐down experiment was performed with 1 μg fusion protein GST‐GFP, GST‐his‐RKIP, or GST‐his‐S109D mixed with 20 μl pre‐cleared agarose beads in 800 μl reaction medium, followed by adding 1 μg flag‐TBK1 and incubating at 4°C for 3 h with gentle rotation. Pull‐down (lane 1–3) and input samples (lane 4) were separated by SDS–PAGE followed by immunoblotting with anti‐GST or anti‐flag antibody. Immunoprecipitation and immunoblot analysis of 293T cells transfected with indicated combinations of vector for myc‐TBK1, flag‐RKIP, flag‐S109A, flag‐S109D, HA‐GSK3β or flag‐GFP. In vitro assay was carried out in the reaction mixture containing 2 mM ATP, 50 μM GST‐TBK1 together with 100 μM GST‐his‐RKIP, 100 μM GST‐his‐S109D, 100 μM GST‐his‐S109A, or 100 μM GST, respectively, at 30°C for 30 min, followed by immunoblotting with anti‐p‐TBK1 or anti‐GST antibody. . Source data are available online for this figure.

    Article Snippet: The fusion proteins of GST‐GFP, GST‐his‐RKIP, and GST‐his‐S109D were expressed in E. coli and purified according to standard protocols with pre‐equilibrated glutathione–Sepharose beads (GE Healthcare).

    Techniques: Infection, Transfection, Recombinant, Immunoprecipitation, In Vitro, Kinase Assay, Stable Transfection, SDS Page, Plasmid Preparation

    Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on GSH agarose beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.

    Journal: PLoS ONE

    Article Title: Investigating the Molecular Basis of Siah1 and Siah2 E3 Ubiquitin Ligase Substrate Specificity

    doi: 10.1371/journal.pone.0106547

    Figure Lengend Snippet: Interaction of Siah2 with PHD3. ( a ) HEK293 cells were transfected in 60-mm cell culture plates for 2 days with the indicated expression plasmids. The cells were lysed, and the lysates were subjected to FLAG immunoprecipitation (IP), as described under “ Materials and Methods ”. Aliquots of the cell lysates and immunoprecipitates were analyzed by western blotting with the anti-HA antibody. Both full length Siah2 and Siah2 SBD bind to PHD3 to the same extent. In the IP, the presence of the faint band in the empty vector lane is due to non-specific binding of PHD3. The same membrane was reblotted with FLAG antibody to detect FLAG tagged Siah2 proteins. ( b ) GST-Siah2 SBD pulldown of HA-PHD3. Cell lysate of HEK293 cells transfected with HA-PHD3 was incubated with GST-Siah2 SBD immobilized on GSH agarose beads and the reaction was performed as described under “ Material and Methods ”. The empty expression vector alone was expressed as a GST control for non-specific binding of HA PHD3. After the incubation, the lysate was removed, the GSH-agarose beads were washed, and bound HA-PHD3 was analyzed by Western blotting using anti HA antibody. The pull down assay confirmed the interaction of Siah2 SBD with PHD3.

    Article Snippet: GST pull down For GST pull down assay, GST-Siah2 SBD was allowed to bind to glutathione sepharose beads (GSH) (GE Healthcare) for 30 min at 4°C in binding buffer containing 50 mM Tris-HCl (pH 8), 150 mM NaCl, 1 mM DTT, 5% glycerol, 0.1% Triton X-100.

    Techniques: Transfection, Cell Culture, Expressing, Immunoprecipitation, Western Blot, Plasmid Preparation, Binding Assay, Incubation, Pull Down Assay

    Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on GTH beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native agarose gel. Position of Relaxed and Form U DNA is indicated.

    Journal: Nucleic Acids Research

    Article Title: Strand invasion by HLTF as a mechanism for template switch in fork rescue

    doi: 10.1093/nar/gkt1040

    Figure Lengend Snippet: Mechanism of D-loop formation by HLTF. ( A ) Self-association of HLTF. GST pull-down experiment was carried out using FLAG-HLTF and GST-HLTF or GST followed by immobilization on GTH beads. The beads were washed, bound proteins were eluted and reactions were analysed on 10% SDS–PAGE gels. ( B ) Western blot analyses of the GST pull-down experiment. We sequentially developed the filter by anti-FLAG, anti-GST and finally anti-HLTF antibodies as indicated on the bottom of the gels together with the bands corresponding to individual proteins. ( C ) HLTF mediates change in DNA conformation in ATP-dependent manner. Increasing amounts of HLTF (22, 66 and 200 nM) were incubated with topologically relaxed DNA and topoisomerase I with (lanes 2–5) or without (lanes 6–8) ATP as indicated. Lane 1 represents control reaction in the absence of topoisomerase I. All reactions were stopped by addition of SDS/proteinase K and reaction products resolved on 0.8% native agarose gel. Position of Relaxed and Form U DNA is indicated.

    Article Snippet: GST pull-down experiment Purified GST or GST-HLTF proteins (3 μg) were incubated with Glutathione-Sepharose (GTH) beads (GE Healthcare) for 4 h at 4°C with FLAG-HLTF (1 μg) in buffer E (40 mM Tris–HCl, pH 7.5, 100 mM NaCl, 0.1 mM DTT, 10% glycerol, 0.01% NP40).

    Techniques: SDS Page, Western Blot, Incubation, Agarose Gel Electrophoresis

    The 2BC non-structural protein of EV-A71 interacts with syntaxin-17 (STX17) and synaptosome-associated protein of 29 kDa (SNAP29). ( A ) Yeast two-hybrid assays of 2BC and STX17. Yeasts were transformed with pGBKT7 or pGBKT7-STX17 together with pACT2 or pACT2–2BC. Yeasts were then grown on selective medium without tryptophan (-W) or without leucine, tryptophan, and histidine (-LWH); ( B ) HeLa cells were transfected with pDEST27 or pDEST27–2BC in combination with pCherry-STX17 for 48 h. The transfected cells were examined under a confocal microscope with objective 63× (scale bar 10µm) for the presence of co-localization; and ( C ) the Pearson’s correlation coefficient was determined; ( D ) HEK-293T cells were co-transfected with FLAG-STX17 and GST-2BC for 48 h. Lysates were collected for co-immunoprecipitation (IP) using glutathione (GST) sepharose. Western Blot was performed to detect FLAG-STX17 and GST fusion proteins; ( E ) RD cells were infected with EV-A71 for 8 hpi and lysates of infected cells were then harvested prior to co-immunoprecipitation (co-IP) assay using anti-STX17 and anti-SNAP29. The final IP eluates and discarded IP flow through were collected for WB to detect 2BC (anti-2C polyclonal antibody) and structural proteins (mAB979) of EV-A71. One-way ANOVA: * p

    Journal: Viruses

    Article Title: 2BC Non-Structural Protein of Enterovirus A71 Interacts with SNARE Proteins to Trigger Autolysosome Formation

    doi: 10.3390/v9070169

    Figure Lengend Snippet: The 2BC non-structural protein of EV-A71 interacts with syntaxin-17 (STX17) and synaptosome-associated protein of 29 kDa (SNAP29). ( A ) Yeast two-hybrid assays of 2BC and STX17. Yeasts were transformed with pGBKT7 or pGBKT7-STX17 together with pACT2 or pACT2–2BC. Yeasts were then grown on selective medium without tryptophan (-W) or without leucine, tryptophan, and histidine (-LWH); ( B ) HeLa cells were transfected with pDEST27 or pDEST27–2BC in combination with pCherry-STX17 for 48 h. The transfected cells were examined under a confocal microscope with objective 63× (scale bar 10µm) for the presence of co-localization; and ( C ) the Pearson’s correlation coefficient was determined; ( D ) HEK-293T cells were co-transfected with FLAG-STX17 and GST-2BC for 48 h. Lysates were collected for co-immunoprecipitation (IP) using glutathione (GST) sepharose. Western Blot was performed to detect FLAG-STX17 and GST fusion proteins; ( E ) RD cells were infected with EV-A71 for 8 hpi and lysates of infected cells were then harvested prior to co-immunoprecipitation (co-IP) assay using anti-STX17 and anti-SNAP29. The final IP eluates and discarded IP flow through were collected for WB to detect 2BC (anti-2C polyclonal antibody) and structural proteins (mAB979) of EV-A71. One-way ANOVA: * p

    Article Snippet: Co-Affinity Purification (Co-AP) Each expression vector (1.5 µg) was transfected into HEK293T cells for 48 h. After cell lysis, Glutathione (GST)-sepharose 4B beads (GE Healthcare, Chalfont St Giles, UK) were used for the co-affinity purification (co-AP) [ ].

    Techniques: Transformation Assay, Transfection, Microscopy, Immunoprecipitation, Western Blot, Infection, Co-Immunoprecipitation Assay, Flow Cytometry