spr-binding experiments Search Results


spr binding experiments  (Biacore)
90
Biacore spr binding experiments
<t>(A)</t> <t>Biacore</t> <t>SPR</t> analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.
Spr Binding Experiments, supplied by Biacore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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spr binding experiments  (SACRI Antibody)
90
SACRI Antibody spr binding experiments
<t>(A)</t> <t>Biacore</t> <t>SPR</t> analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.
Spr Binding Experiments, supplied by SACRI Antibody, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
spr binding experiments - by Bioz Stars, 2026-03
90/100 stars
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spr binding experiments biacore 2000 instrument  (Biacore)
90
Biacore spr binding experiments biacore 2000 instrument
<t>(A)</t> <t>Biacore</t> <t>SPR</t> analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.
Spr Binding Experiments Biacore 2000 Instrument, supplied by Biacore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
spr binding experiments biacore 2000 instrument - by Bioz Stars, 2026-03
90/100 stars
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spr binding experiments with lead inhibitors 14ba and 14aa  (Biacore)
90
Biacore spr binding experiments with lead inhibitors 14ba and 14aa
<t>(A)</t> <t>Biacore</t> <t>SPR</t> analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.
Spr Binding Experiments With Lead Inhibitors 14ba And 14aa, supplied by Biacore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
spr binding experiments with lead inhibitors 14ba and 14aa - by Bioz Stars, 2026-03
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spr binding and molecular docking experiment  (Biacore)
90
Biacore spr binding and molecular docking experiment
<t>(A)</t> <t>Biacore</t> <t>SPR</t> analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.
Spr Binding And Molecular Docking Experiment, supplied by Biacore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
spr binding and molecular docking experiment - by Bioz Stars, 2026-03
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Image Search Results


(A) Biacore SPR analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.

Journal: Molecular cell

Article Title: Inhibition of Ras/Raf/MEK/ERK Pathway Signaling by a Stress-induced Phospho-regulatory Circuit

doi: 10.1016/j.molcel.2016.10.029

Figure Lengend Snippet: (A) Biacore SPR analysis of in vitro RafRBD binding: K-Ras-GTP or K-Ras-GDP (10 µM) were injected over WT- or R89L-RafRBD and binding responses were determined. (B) A 2-fold dilution series of Rigosertib (50 µM to 0.39 µM) was injected over WT-RafRBD and binding was determined by SPR. (C) 5 µM WT-RafRBD was mixed with increasing concentrations of Rigosertib (0.19 – 50 µM), following which binding to avi-K-RasGTP was measured (red lines) and compared to a RafRBD calibration series (black lines) (D) WT- or R89L-GST-RafRBD was incubated for 1 hr with increasing concentrations of Rigosertib and binding to GTP-loaded WTor G12V-K-Ras was determined by proximity based energy transfer. As a control for nonspecific inhibition, the effect of Rigosertib on Avi-GST was also monitored. (E) HeLa cells were treated as indicated with DMSO or 2 µM Rigosertib (Rig) prior to stimulation with EGF for 5 min (+) and lysis. Raf dimerization was monitored by probing Raf immunoprecipitates for the presence of other Raf family members. Lysates were examined for activated pMEK, pERK, and pAKT levels and for total B-Raf, C-Raf, A-Raf and tubulin (loading control) levels. (F) Depiction of the Raf domain structure and location of the Rigosertib-induced sites of S/TP phosphorylation. (G) The indicated cancer lines were treated with DMSO (−) or Rigosertib (+) for 18 hrs prior to lysis. Endogenous C-Raf was immunoprecipitated and probed for pS642P levels or B-Raf. Shifts in the electrophoretic mobility of B-Raf and C-Raf were also examined.

Article Snippet: SPR binding experiments were performed on a Biacore S200 instrument (GE).

Techniques: In Vitro, Binding Assay, Injection, Incubation, Control, Inhibition, Lysis, Phospho-proteomics, Immunoprecipitation