pierce ecl western blotting substrate Thermo Fisher Search Results


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  • 83
    Thermo Fisher pierce ecl western blotting substrate thermo fisher scientific
    Pierce Ecl Western Blotting Substrate Thermo Fisher Scientific, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 83/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific ecl western blotting substrate
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    Thermo Fisher pierce ecl western blotting substrate
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    Thermo Fisher ecl western blotting substrate kit
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    Thermo Fisher ecl substrate western blot detection system
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    Thermo Fisher pierce ecl western blotting substrate kit
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    Thermo Fisher chemiluminescent pierce ecl western blotting substrate
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    Thermo Fisher chemiluminescence western blotting substrate
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    Thermo Fisher ecl western blot system
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    Thermo Fisher supersignal west pico enhanced chemiluminescent ecl substrate
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    Thermo Fisher west femto enhanced chemiluminescent substrate system
    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. <t>SuperSignal</t> West Pico (Pico) or West <t>Femto</t> (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.
    West Femto Enhanced Chemiluminescent Substrate System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher super sensitive enhanced chemiluminescence substrate
    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. <t>SuperSignal</t> West Pico (Pico) or West <t>Femto</t> (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.
    Super Sensitive Enhanced Chemiluminescence Substrate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 76/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher ecl chemiluminiscent substrate
    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. <t>SuperSignal</t> West Pico (Pico) or West <t>Femto</t> (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.
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    Thermo Fisher ecl autoradiography
    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. <t>SuperSignal</t> West Pico (Pico) or West <t>Femto</t> (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.
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    Thermo Fisher chemiluminescence ecl
    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. <t>SuperSignal</t> West Pico (Pico) or West <t>Femto</t> (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.
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    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. <t>SuperSignal</t> West Pico (Pico) or West <t>Femto</t> (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.
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    In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. SuperSignal West Pico (Pico) or West Femto (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.

    Journal: Journal of Virology

    Article Title: Association of Simian Virus 40 Vp1 with 70-Kilodalton Heat Shock Proteins and Viral Tumor Antigens ▿

    doi: 10.1128/JVI.00844-08

    Figure Lengend Snippet: In vitro binding of recombinant Vp1 proteins with (co)chaperone proteins. (A) Schematic diagram of Vp1 amino acid residues of recombinant Vp1 proteins. Diagrams are shown for the Vp1ΔN20ΔC58-His6 pentamer (ΔNΔC; aa 22 to 303), the Vp1ΔC58-His6 pentamer (ΔC; aa 1 to 303), and GST-Vp1C69 (C69; aa 292 to 361). GST-Vp1 is full-length Vp1 (aa 1 to 361). (B) Vp1 interacts with (co)chaperones. GST or GST-Vp1 was immobilized onto glutathione-Sepharose resin and reacted with the Sol fraction of 4 × 10 7 293TT cells. The resin-bound proteins were eluted and probed for GST proteins, a unique region of LT, Hsc70, Hsp70, and Hsp40 by Western blotting. To detect GST in input, a 1/3 volume of input GST and GST-Vp1 was loaded (lanes 3 and 4, top row), and for LT, Hsc70, Hsp70, and Hsp40, a 1/160 dilution of input Sol was used (lanes 3 and 4, bottom four rows). An unlabeled arrowhead points to a degraded product of GST-Vp1. (C, D) Binding of recombinant Vp1 proteins to Hsc70 (C) or to Hsp70 (D). GST-Vp1C69 (C69), the Vp1ΔC58-His6 pentamer (ΔC), or the Vp1ΔN20ΔC58-His6 core pentamer (ΔNΔC) was mixed with the Sol fraction from 4 × 10 6 of 293TT cells or hs TC7 cells, with the 293TT Sol fraction that had been depleted of LT/ST (T/t), or with the lysis buffer in the presence of hexokinase (hex) or ATP, followed by hexokinase addition (ATP/hex). After incubation, chaperone-Vp1 binding was assessed by IP with an anti-Hsc70 antibody (C) or with an anti-Hsp70 antibody (D), followed by anti-Vp1 Western blotting. (E) GST-Vp1C69 was mixed with the 293TT Sol fraction and treated with hexokinase or ATP/hexokinase as described for panels C and D. After IP with an anti-β-Gal antibody, Vp1 was visualized by anti-Vp1 Western blots. (F) The Vp1 in 1/500 of input Vp1ΔC58-His6, GST-Vp1C69, or Vp1ΔN20ΔC58-His6 used for panels B, C, and D was visualized by anti-Vp1 Western blotting. (G) The Sol fraction from 2.4 × 10 6 293TT cells (lane 1), 6.0 × 10 5 293TT cells (lane 2), 6.0 × 10 5 LT/ST-depleted 293TT cells (lane 3), or 3.6 × 10 5 COS-7 cells (lane 4) was analyzed for LT and ST by using antibody to a common epitope of both LT and ST by Western blotting. SuperSignal West Pico (Pico) or West Femto (Femto) was used to visualize LT or ST. An arrow or arrowhead indicates LT or ST, respectively.

    Article Snippet: Western blot analysis was performed essentially according to the protocol recommended for the TrueBlot system (eBioscience) and detected using either SuperSignal West Pico or West Femto enhanced chemiluminescent substrate system (Pierce).

    Techniques: In Vitro, Binding Assay, Recombinant, Western Blot, Lysis, Incubation