F54271 Search Results


total fgfr1 f5421  (Millipore)
86
Millipore total fgfr1 f5421
(a) Ligand interaction diagram of quinacrine with <t>FGFR1</t> kinase domain. Here the amino acids are characterized as negatively charged (rusty red),hydrophobic (lime), polar (cerulean), H-bonding is shown is purple and pi-pi stacking is shown with green lines. (b) Diagram representing the bar plot of physical contacts of drug QC with residues of FGFR1 kinase domain throughout the 100ns long MD trajectory. (c) Root mean square deviation plot for all MD simulations i.e FGFR1 kinase in apo state (shown in red), complexed with and complex with quinacrine (shown in blue) The RMSD trajectories in all the MDs converged around 20 nanoseconds (ns).
Total Fgfr1 F5421, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/total fgfr1 f5421/product/Millipore
Average 86 stars, based on 1 article reviews
total fgfr1 f5421 - by Bioz Stars, 2025-06
86/100 stars
  Buy from Supplier
fgfr1  (Millipore)
86
Millipore fgfr1
(a) Ligand interaction diagram of quinacrine with <t>FGFR1</t> kinase domain. Here the amino acids are characterized as negatively charged (rusty red),hydrophobic (lime), polar (cerulean), H-bonding is shown is purple and pi-pi stacking is shown with green lines. (b) Diagram representing the bar plot of physical contacts of drug QC with residues of FGFR1 kinase domain throughout the 100ns long MD trajectory. (c) Root mean square deviation plot for all MD simulations i.e FGFR1 kinase in apo state (shown in red), complexed with and complex with quinacrine (shown in blue) The RMSD trajectories in all the MDs converged around 20 nanoseconds (ns).
Fgfr1, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/fgfr1/product/Millipore
Average 86 stars, based on 1 article reviews
fgfr1 - by Bioz Stars, 2025-06
86/100 stars
  Buy from Supplier
tgf β2  (Millipore)
86
Millipore tgf β2
(a) Ligand interaction diagram of quinacrine with <t>FGFR1</t> kinase domain. Here the amino acids are characterized as negatively charged (rusty red),hydrophobic (lime), polar (cerulean), H-bonding is shown is purple and pi-pi stacking is shown with green lines. (b) Diagram representing the bar plot of physical contacts of drug QC with residues of FGFR1 kinase domain throughout the 100ns long MD trajectory. (c) Root mean square deviation plot for all MD simulations i.e FGFR1 kinase in apo state (shown in red), complexed with and complex with quinacrine (shown in blue) The RMSD trajectories in all the MDs converged around 20 nanoseconds (ns).
Tgf β2, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/tgf β2/product/Millipore
Average 86 stars, based on 1 article reviews
tgf β2 - by Bioz Stars, 2025-06
86/100 stars
  Buy from Supplier
rabbit monoclonal anti fgfr1  (Millipore)
86
Millipore rabbit monoclonal anti fgfr1
(a) Ligand interaction diagram of quinacrine with <t>FGFR1</t> kinase domain. Here the amino acids are characterized as negatively charged (rusty red),hydrophobic (lime), polar (cerulean), H-bonding is shown is purple and pi-pi stacking is shown with green lines. (b) Diagram representing the bar plot of physical contacts of drug QC with residues of FGFR1 kinase domain throughout the 100ns long MD trajectory. (c) Root mean square deviation plot for all MD simulations i.e FGFR1 kinase in apo state (shown in red), complexed with and complex with quinacrine (shown in blue) The RMSD trajectories in all the MDs converged around 20 nanoseconds (ns).
Rabbit Monoclonal Anti Fgfr1, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit monoclonal anti fgfr1/product/Millipore
Average 86 stars, based on 1 article reviews
rabbit monoclonal anti fgfr1 - by Bioz Stars, 2025-06
86/100 stars
  Buy from Supplier

Image Search Results


(a) Ligand interaction diagram of quinacrine with FGFR1 kinase domain. Here the amino acids are characterized as negatively charged (rusty red),hydrophobic (lime), polar (cerulean), H-bonding is shown is purple and pi-pi stacking is shown with green lines. (b) Diagram representing the bar plot of physical contacts of drug QC with residues of FGFR1 kinase domain throughout the 100ns long MD trajectory. (c) Root mean square deviation plot for all MD simulations i.e FGFR1 kinase in apo state (shown in red), complexed with and complex with quinacrine (shown in blue) The RMSD trajectories in all the MDs converged around 20 nanoseconds (ns).

Journal: bioRxiv

Article Title: Quinacrine binds to the kinase domain of FGFR1 and inhibits its activity

doi: 10.1101/2021.12.02.470934

Figure Lengend Snippet: (a) Ligand interaction diagram of quinacrine with FGFR1 kinase domain. Here the amino acids are characterized as negatively charged (rusty red),hydrophobic (lime), polar (cerulean), H-bonding is shown is purple and pi-pi stacking is shown with green lines. (b) Diagram representing the bar plot of physical contacts of drug QC with residues of FGFR1 kinase domain throughout the 100ns long MD trajectory. (c) Root mean square deviation plot for all MD simulations i.e FGFR1 kinase in apo state (shown in red), complexed with and complex with quinacrine (shown in blue) The RMSD trajectories in all the MDs converged around 20 nanoseconds (ns).

Article Snippet: Primary antibodies against β-actin (A5441), phosphor-FGFR1 Tyr 653/654 (06-1433-25 μg), and total FGFR1 (F5421) were purchased from Sigma Life Sciences.

Techniques:

(a) Root mean square fluctuation analysis for all MD simulations i.e FGFR1 kinase in apo state (shown in red and in complex with quinacrine (shown in blue). (b) From top to bottom, the ligand’s root mean square deviation, radius of gyration, intramolecular hydrogen bonds, molecular surface area, solvent accessible surface area and polar surface area are shown. (c) and (d) Dihedral angle plots for QC-FGFR1 complex MD simulations.

Journal: bioRxiv

Article Title: Quinacrine binds to the kinase domain of FGFR1 and inhibits its activity

doi: 10.1101/2021.12.02.470934

Figure Lengend Snippet: (a) Root mean square fluctuation analysis for all MD simulations i.e FGFR1 kinase in apo state (shown in red and in complex with quinacrine (shown in blue). (b) From top to bottom, the ligand’s root mean square deviation, radius of gyration, intramolecular hydrogen bonds, molecular surface area, solvent accessible surface area and polar surface area are shown. (c) and (d) Dihedral angle plots for QC-FGFR1 complex MD simulations.

Article Snippet: Primary antibodies against β-actin (A5441), phosphor-FGFR1 Tyr 653/654 (06-1433-25 μg), and total FGFR1 (F5421) were purchased from Sigma Life Sciences.

Techniques:

(a) Graph representing luminescence-based kinase activity inhibition of the FGFR1 protein by quinacrine. (b) Graph representing the aFGF and bFGF induced proliferation assay with exposure to different concentrations of quinacrine. Cells were seeded in 6-well plate and treated with various concentrations of QC as described in materials and methods section for 24 h. *=P value<0.05, **=P value<0.001, ***=P value<0.0001 versus control group. (c) Image panel showing western blots of total and phoshopylated FGFR1 in QC treated cells stimulated with 10ng/ml of aFGF and bFGF.

Journal: bioRxiv

Article Title: Quinacrine binds to the kinase domain of FGFR1 and inhibits its activity

doi: 10.1101/2021.12.02.470934

Figure Lengend Snippet: (a) Graph representing luminescence-based kinase activity inhibition of the FGFR1 protein by quinacrine. (b) Graph representing the aFGF and bFGF induced proliferation assay with exposure to different concentrations of quinacrine. Cells were seeded in 6-well plate and treated with various concentrations of QC as described in materials and methods section for 24 h. *=P value<0.05, **=P value<0.001, ***=P value<0.0001 versus control group. (c) Image panel showing western blots of total and phoshopylated FGFR1 in QC treated cells stimulated with 10ng/ml of aFGF and bFGF.

Article Snippet: Primary antibodies against β-actin (A5441), phosphor-FGFR1 Tyr 653/654 (06-1433-25 μg), and total FGFR1 (F5421) were purchased from Sigma Life Sciences.

Techniques: Activity Assay, Inhibition, Proliferation Assay, Western Blot