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human pdgf bb  (MedChemExpress)


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    MedChemExpress human pdgf bb
    p.V665A mutant preferentially activates STAT1. (A) Human PDGF receptor β expression in transduced NIH3T3 cells was tested by flow cytometry (blue) and compared to cells transduced with the empty vector (red). The average percentage of positive cells was calculated from three experiments with SEM. The receptor expression levels of the other cell lines used in the study are shown in Figure . (B) PDGF receptor β phosphorylation and expression levels. Transduced NIH3T3 cells were starved for 7 h. As a positive control, cells expressing WT receptors were stimulated <t>with</t> <t>PDGF‐BB</t> (25 ng/ml) for 15 min before lysis. The receptor was isolated by immunoprecipitation and analysed by Western blot using anti‐phospho‐tyrosine and anti‐PDGFRB antibodies. One representative blot out of three is shown. (C) NIH3T3 cells were treated as in (B). Total cell lysates were analysed by Western blot with the indicated antibodies ( n = 3)
    Human Pdgf Bb, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human pdgf bb/product/MedChemExpress
    Average 93 stars, based on 3 article reviews
    human pdgf bb - by Bioz Stars, 2026-03
    93/100 stars

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    1) Product Images from "Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling"

    Article Title: Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/jcmm.17427

    p.V665A mutant preferentially activates STAT1. (A) Human PDGF receptor β expression in transduced NIH3T3 cells was tested by flow cytometry (blue) and compared to cells transduced with the empty vector (red). The average percentage of positive cells was calculated from three experiments with SEM. The receptor expression levels of the other cell lines used in the study are shown in Figure . (B) PDGF receptor β phosphorylation and expression levels. Transduced NIH3T3 cells were starved for 7 h. As a positive control, cells expressing WT receptors were stimulated with PDGF‐BB (25 ng/ml) for 15 min before lysis. The receptor was isolated by immunoprecipitation and analysed by Western blot using anti‐phospho‐tyrosine and anti‐PDGFRB antibodies. One representative blot out of three is shown. (C) NIH3T3 cells were treated as in (B). Total cell lysates were analysed by Western blot with the indicated antibodies ( n = 3)
    Figure Legend Snippet: p.V665A mutant preferentially activates STAT1. (A) Human PDGF receptor β expression in transduced NIH3T3 cells was tested by flow cytometry (blue) and compared to cells transduced with the empty vector (red). The average percentage of positive cells was calculated from three experiments with SEM. The receptor expression levels of the other cell lines used in the study are shown in Figure . (B) PDGF receptor β phosphorylation and expression levels. Transduced NIH3T3 cells were starved for 7 h. As a positive control, cells expressing WT receptors were stimulated with PDGF‐BB (25 ng/ml) for 15 min before lysis. The receptor was isolated by immunoprecipitation and analysed by Western blot using anti‐phospho‐tyrosine and anti‐PDGFRB antibodies. One representative blot out of three is shown. (C) NIH3T3 cells were treated as in (B). Total cell lysates were analysed by Western blot with the indicated antibodies ( n = 3)

    Techniques Used: Mutagenesis, Expressing, Flow Cytometry, Transduction, Plasmid Preparation, Phospho-proteomics, Positive Control, Lysis, Isolation, Immunoprecipitation, Western Blot

    STAT1 activation by βV665A is JAK2‐independent. (A) γ2A cells were transiently transfected with PDGFRB (WT or V665A) and JAK2, as indicated. After transfection, cells were starved for 7 h and lysed. The total lysates were analysed by Western blotting. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 7 h and treated with different concentrations of ruxolitinib as indicated. As positive controls, cells expressing the WT receptor were stimulated with PDGF‐BB or IFNγ for 15 min. The total lysates were analysed by Western blotting
    Figure Legend Snippet: STAT1 activation by βV665A is JAK2‐independent. (A) γ2A cells were transiently transfected with PDGFRB (WT or V665A) and JAK2, as indicated. After transfection, cells were starved for 7 h and lysed. The total lysates were analysed by Western blotting. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 7 h and treated with different concentrations of ruxolitinib as indicated. As positive controls, cells expressing the WT receptor were stimulated with PDGF‐BB or IFNγ for 15 min. The total lysates were analysed by Western blotting

    Techniques Used: Activation Assay, Transfection, Western Blot, Expressing, Produced

    PDGFRB p.V665A mutant is constitutively active. The activity of the mutants was analysed in a dual‐luciferase reporter assay. γ2A (A) or HEK293T (B) cells were co‐transfected with wild‐type (WT) or mutant PDGFRB and a firefly luciferase reporter controlled by STAT‐response elements (A) or serum‐response elements (B), respectively. Results were normalized using a renilla luciferase control reporter. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB. The mean of four independent experiments is shown with SEM. Statistical analysis was performed using an anova one‐way test with Dunnett correction to compare mutant to wild‐type conditions. (C) HEK293T cells were transfected with WT or mutant PDGFRB or the empty vector and starved for 7 h before lysis. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. Total cell lysates were analysed by Western blotting. The receptor phosphorylation was probed with an anti‐phospho‐tyrosine antibody. Membranes were re‐probed with anti‐PDGFRB and anti‐Actin antibodies. Representative blots are shown ( n = 4)
    Figure Legend Snippet: PDGFRB p.V665A mutant is constitutively active. The activity of the mutants was analysed in a dual‐luciferase reporter assay. γ2A (A) or HEK293T (B) cells were co‐transfected with wild‐type (WT) or mutant PDGFRB and a firefly luciferase reporter controlled by STAT‐response elements (A) or serum‐response elements (B), respectively. Results were normalized using a renilla luciferase control reporter. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB. The mean of four independent experiments is shown with SEM. Statistical analysis was performed using an anova one‐way test with Dunnett correction to compare mutant to wild‐type conditions. (C) HEK293T cells were transfected with WT or mutant PDGFRB or the empty vector and starved for 7 h before lysis. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. Total cell lysates were analysed by Western blotting. The receptor phosphorylation was probed with an anti‐phospho‐tyrosine antibody. Membranes were re‐probed with anti‐PDGFRB and anti‐Actin antibodies. Representative blots are shown ( n = 4)

    Techniques Used: Mutagenesis, Activity Assay, Luciferase, Reporter Assay, Transfection, Control, Positive Control, Expressing, Plasmid Preparation, Lysis, Western Blot, Phospho-proteomics

    p.V665A mutant receptor does not stimulate cell proliferation. (A) Ba/F3 cells were electroporated with PDGFRB (WT, V665A or N666K) or an empty vector. Cells were selected in the presence of G418 and sorted. The receptor cell surface expression was assessed by flow cytometry with a human PDGFRB‐specific antibody. (B) Transfected Ba/F3 cell lysates were analysed by Western blotting using anti‐PDGFRB antibodies. Membranes were re‐probed with an anti‐calnexin antibody as loading control. (C) Transfected Ba/F3 cells were stimulated with control medium, PDGF‐BB or IL‐3. After 20 h, [ 3 H]‐thymidine was added to each well for 4 h. Incorporation of radiolabelled thymidine into cell DNA was quantified. Results were normalized using the stimulated wild‐type condition as reference. The average of five independent experiments is shown with SEM. All cell lines responded similarly to IL‐3 (not shown). (D) NIH3T3 cells were transfected in triplicates with PDGFRB (WT, V665A or N666K). Three weeks after transfection, foci were stained with crystal violet and quantified. The mean of three independent experiments is shown with SEM
    Figure Legend Snippet: p.V665A mutant receptor does not stimulate cell proliferation. (A) Ba/F3 cells were electroporated with PDGFRB (WT, V665A or N666K) or an empty vector. Cells were selected in the presence of G418 and sorted. The receptor cell surface expression was assessed by flow cytometry with a human PDGFRB‐specific antibody. (B) Transfected Ba/F3 cell lysates were analysed by Western blotting using anti‐PDGFRB antibodies. Membranes were re‐probed with an anti‐calnexin antibody as loading control. (C) Transfected Ba/F3 cells were stimulated with control medium, PDGF‐BB or IL‐3. After 20 h, [ 3 H]‐thymidine was added to each well for 4 h. Incorporation of radiolabelled thymidine into cell DNA was quantified. Results were normalized using the stimulated wild‐type condition as reference. The average of five independent experiments is shown with SEM. All cell lines responded similarly to IL‐3 (not shown). (D) NIH3T3 cells were transfected in triplicates with PDGFRB (WT, V665A or N666K). Three weeks after transfection, foci were stained with crystal violet and quantified. The mean of three independent experiments is shown with SEM

    Techniques Used: Mutagenesis, Plasmid Preparation, Expressing, Flow Cytometry, Transfection, Western Blot, Control, Staining

    p.V665A mutation decreases the sensitivity to imatinib. (A) Position equivalent to valine 665 (blue), in the catalytic cleft of the PDGFRA kinase domain (green) co‐crystalized with imatinib (pink). The Asp‐Phe‐Gly (DFG) motif, which plays an important role in the regulation of kinase activity, is shown in orange. The alpha‐C helix is on the left. Drawn using PyMol based on structure #6JOL from Protein Data Bank. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 4 h and treated with different concentrations of imatinib as indicated. As a positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. The total lysates were analysed by Western blotting. (C) Ba/F3 cells expressing WT PDGFRB or βV665A were produced as described in Figure . Cells were stimulated with PDGF‐BB for 24 h in the presence of the indicated concentration of imatinib. Four hours before harvest, [ H]‐thymidine was added to each well. Radiolabelled thymidine incorporation was quantified and compared to cells that were not treated with imatinib. The average of three independent experiments is shown with SEM and statistical analysis ( anova test, p < 0.01)
    Figure Legend Snippet: p.V665A mutation decreases the sensitivity to imatinib. (A) Position equivalent to valine 665 (blue), in the catalytic cleft of the PDGFRA kinase domain (green) co‐crystalized with imatinib (pink). The Asp‐Phe‐Gly (DFG) motif, which plays an important role in the regulation of kinase activity, is shown in orange. The alpha‐C helix is on the left. Drawn using PyMol based on structure #6JOL from Protein Data Bank. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 4 h and treated with different concentrations of imatinib as indicated. As a positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. The total lysates were analysed by Western blotting. (C) Ba/F3 cells expressing WT PDGFRB or βV665A were produced as described in Figure . Cells were stimulated with PDGF‐BB for 24 h in the presence of the indicated concentration of imatinib. Four hours before harvest, [ H]‐thymidine was added to each well. Radiolabelled thymidine incorporation was quantified and compared to cells that were not treated with imatinib. The average of three independent experiments is shown with SEM and statistical analysis ( anova test, p < 0.01)

    Techniques Used: Mutagenesis, Activity Assay, Expressing, Produced, Positive Control, Western Blot, Concentration Assay



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    human pdgf bb  (MedChemExpress)
    93
    MedChemExpress human pdgf bb
    p.V665A mutant preferentially activates STAT1. (A) Human PDGF receptor β expression in transduced NIH3T3 cells was tested by flow cytometry (blue) and compared to cells transduced with the empty vector (red). The average percentage of positive cells was calculated from three experiments with SEM. The receptor expression levels of the other cell lines used in the study are shown in Figure . (B) PDGF receptor β phosphorylation and expression levels. Transduced NIH3T3 cells were starved for 7 h. As a positive control, cells expressing WT receptors were stimulated <t>with</t> <t>PDGF‐BB</t> (25 ng/ml) for 15 min before lysis. The receptor was isolated by immunoprecipitation and analysed by Western blot using anti‐phospho‐tyrosine and anti‐PDGFRB antibodies. One representative blot out of three is shown. (C) NIH3T3 cells were treated as in (B). Total cell lysates were analysed by Western blot with the indicated antibodies ( n = 3)
    Human Pdgf Bb, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human pdgf bb/product/MedChemExpress
    Average 93 stars, based on 1 article reviews
    human pdgf bb - by Bioz Stars, 2026-03
    93/100 stars
    		  Buy from Supplier

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    p.V665A mutant preferentially activates STAT1. (A) Human PDGF receptor β expression in transduced NIH3T3 cells was tested by flow cytometry (blue) and compared to cells transduced with the empty vector (red). The average percentage of positive cells was calculated from three experiments with SEM. The receptor expression levels of the other cell lines used in the study are shown in Figure . (B) PDGF receptor β phosphorylation and expression levels. Transduced NIH3T3 cells were starved for 7 h. As a positive control, cells expressing WT receptors were stimulated with PDGF‐BB (25 ng/ml) for 15 min before lysis. The receptor was isolated by immunoprecipitation and analysed by Western blot using anti‐phospho‐tyrosine and anti‐PDGFRB antibodies. One representative blot out of three is shown. (C) NIH3T3 cells were treated as in (B). Total cell lysates were analysed by Western blot with the indicated antibodies ( n = 3)

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling

    doi: 10.1111/jcmm.17427

    Figure Lengend Snippet: p.V665A mutant preferentially activates STAT1. (A) Human PDGF receptor β expression in transduced NIH3T3 cells was tested by flow cytometry (blue) and compared to cells transduced with the empty vector (red). The average percentage of positive cells was calculated from three experiments with SEM. The receptor expression levels of the other cell lines used in the study are shown in Figure . (B) PDGF receptor β phosphorylation and expression levels. Transduced NIH3T3 cells were starved for 7 h. As a positive control, cells expressing WT receptors were stimulated with PDGF‐BB (25 ng/ml) for 15 min before lysis. The receptor was isolated by immunoprecipitation and analysed by Western blot using anti‐phospho‐tyrosine and anti‐PDGFRB antibodies. One representative blot out of three is shown. (C) NIH3T3 cells were treated as in (B). Total cell lysates were analysed by Western blot with the indicated antibodies ( n = 3)

    Article Snippet: Cells were treated with human PDGF‐BB (25 ng/ml), IFNγ (25 ng/ml, both from PeproTech), imatinib (LC laboratories) or ruxolitinib (INCB18424, MedChemExpress) as indicated.

    Techniques: Mutagenesis, Expressing, Flow Cytometry, Transduction, Plasmid Preparation, Phospho-proteomics, Positive Control, Lysis, Isolation, Immunoprecipitation, Western Blot

    STAT1 activation by βV665A is JAK2‐independent. (A) γ2A cells were transiently transfected with PDGFRB (WT or V665A) and JAK2, as indicated. After transfection, cells were starved for 7 h and lysed. The total lysates were analysed by Western blotting. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 7 h and treated with different concentrations of ruxolitinib as indicated. As positive controls, cells expressing the WT receptor were stimulated with PDGF‐BB or IFNγ for 15 min. The total lysates were analysed by Western blotting

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling

    doi: 10.1111/jcmm.17427

    Figure Lengend Snippet: STAT1 activation by βV665A is JAK2‐independent. (A) γ2A cells were transiently transfected with PDGFRB (WT or V665A) and JAK2, as indicated. After transfection, cells were starved for 7 h and lysed. The total lysates were analysed by Western blotting. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 7 h and treated with different concentrations of ruxolitinib as indicated. As positive controls, cells expressing the WT receptor were stimulated with PDGF‐BB or IFNγ for 15 min. The total lysates were analysed by Western blotting

    Article Snippet: Cells were treated with human PDGF‐BB (25 ng/ml), IFNγ (25 ng/ml, both from PeproTech), imatinib (LC laboratories) or ruxolitinib (INCB18424, MedChemExpress) as indicated.

    Techniques: Activation Assay, Transfection, Western Blot, Expressing, Produced

    PDGFRB p.V665A mutant is constitutively active. The activity of the mutants was analysed in a dual‐luciferase reporter assay. γ2A (A) or HEK293T (B) cells were co‐transfected with wild‐type (WT) or mutant PDGFRB and a firefly luciferase reporter controlled by STAT‐response elements (A) or serum‐response elements (B), respectively. Results were normalized using a renilla luciferase control reporter. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB. The mean of four independent experiments is shown with SEM. Statistical analysis was performed using an anova one‐way test with Dunnett correction to compare mutant to wild‐type conditions. (C) HEK293T cells were transfected with WT or mutant PDGFRB or the empty vector and starved for 7 h before lysis. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. Total cell lysates were analysed by Western blotting. The receptor phosphorylation was probed with an anti‐phospho‐tyrosine antibody. Membranes were re‐probed with anti‐PDGFRB and anti‐Actin antibodies. Representative blots are shown ( n = 4)

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling

    doi: 10.1111/jcmm.17427

    Figure Lengend Snippet: PDGFRB p.V665A mutant is constitutively active. The activity of the mutants was analysed in a dual‐luciferase reporter assay. γ2A (A) or HEK293T (B) cells were co‐transfected with wild‐type (WT) or mutant PDGFRB and a firefly luciferase reporter controlled by STAT‐response elements (A) or serum‐response elements (B), respectively. Results were normalized using a renilla luciferase control reporter. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB. The mean of four independent experiments is shown with SEM. Statistical analysis was performed using an anova one‐way test with Dunnett correction to compare mutant to wild‐type conditions. (C) HEK293T cells were transfected with WT or mutant PDGFRB or the empty vector and starved for 7 h before lysis. As positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. Total cell lysates were analysed by Western blotting. The receptor phosphorylation was probed with an anti‐phospho‐tyrosine antibody. Membranes were re‐probed with anti‐PDGFRB and anti‐Actin antibodies. Representative blots are shown ( n = 4)

    Article Snippet: Cells were treated with human PDGF‐BB (25 ng/ml), IFNγ (25 ng/ml, both from PeproTech), imatinib (LC laboratories) or ruxolitinib (INCB18424, MedChemExpress) as indicated.

    Techniques: Mutagenesis, Activity Assay, Luciferase, Reporter Assay, Transfection, Control, Positive Control, Expressing, Plasmid Preparation, Lysis, Western Blot, Phospho-proteomics

    p.V665A mutant receptor does not stimulate cell proliferation. (A) Ba/F3 cells were electroporated with PDGFRB (WT, V665A or N666K) or an empty vector. Cells were selected in the presence of G418 and sorted. The receptor cell surface expression was assessed by flow cytometry with a human PDGFRB‐specific antibody. (B) Transfected Ba/F3 cell lysates were analysed by Western blotting using anti‐PDGFRB antibodies. Membranes were re‐probed with an anti‐calnexin antibody as loading control. (C) Transfected Ba/F3 cells were stimulated with control medium, PDGF‐BB or IL‐3. After 20 h, [ 3 H]‐thymidine was added to each well for 4 h. Incorporation of radiolabelled thymidine into cell DNA was quantified. Results were normalized using the stimulated wild‐type condition as reference. The average of five independent experiments is shown with SEM. All cell lines responded similarly to IL‐3 (not shown). (D) NIH3T3 cells were transfected in triplicates with PDGFRB (WT, V665A or N666K). Three weeks after transfection, foci were stained with crystal violet and quantified. The mean of three independent experiments is shown with SEM

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling

    doi: 10.1111/jcmm.17427

    Figure Lengend Snippet: p.V665A mutant receptor does not stimulate cell proliferation. (A) Ba/F3 cells were electroporated with PDGFRB (WT, V665A or N666K) or an empty vector. Cells were selected in the presence of G418 and sorted. The receptor cell surface expression was assessed by flow cytometry with a human PDGFRB‐specific antibody. (B) Transfected Ba/F3 cell lysates were analysed by Western blotting using anti‐PDGFRB antibodies. Membranes were re‐probed with an anti‐calnexin antibody as loading control. (C) Transfected Ba/F3 cells were stimulated with control medium, PDGF‐BB or IL‐3. After 20 h, [ 3 H]‐thymidine was added to each well for 4 h. Incorporation of radiolabelled thymidine into cell DNA was quantified. Results were normalized using the stimulated wild‐type condition as reference. The average of five independent experiments is shown with SEM. All cell lines responded similarly to IL‐3 (not shown). (D) NIH3T3 cells were transfected in triplicates with PDGFRB (WT, V665A or N666K). Three weeks after transfection, foci were stained with crystal violet and quantified. The mean of three independent experiments is shown with SEM

    Article Snippet: Cells were treated with human PDGF‐BB (25 ng/ml), IFNγ (25 ng/ml, both from PeproTech), imatinib (LC laboratories) or ruxolitinib (INCB18424, MedChemExpress) as indicated.

    Techniques: Mutagenesis, Plasmid Preparation, Expressing, Flow Cytometry, Transfection, Western Blot, Control, Staining

    p.V665A mutation decreases the sensitivity to imatinib. (A) Position equivalent to valine 665 (blue), in the catalytic cleft of the PDGFRA kinase domain (green) co‐crystalized with imatinib (pink). The Asp‐Phe‐Gly (DFG) motif, which plays an important role in the regulation of kinase activity, is shown in orange. The alpha‐C helix is on the left. Drawn using PyMol based on structure #6JOL from Protein Data Bank. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 4 h and treated with different concentrations of imatinib as indicated. As a positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. The total lysates were analysed by Western blotting. (C) Ba/F3 cells expressing WT PDGFRB or βV665A were produced as described in Figure . Cells were stimulated with PDGF‐BB for 24 h in the presence of the indicated concentration of imatinib. Four hours before harvest, [ H]‐thymidine was added to each well. Radiolabelled thymidine incorporation was quantified and compared to cells that were not treated with imatinib. The average of three independent experiments is shown with SEM and statistical analysis ( anova test, p < 0.01)

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signalling

    doi: 10.1111/jcmm.17427

    Figure Lengend Snippet: p.V665A mutation decreases the sensitivity to imatinib. (A) Position equivalent to valine 665 (blue), in the catalytic cleft of the PDGFRA kinase domain (green) co‐crystalized with imatinib (pink). The Asp‐Phe‐Gly (DFG) motif, which plays an important role in the regulation of kinase activity, is shown in orange. The alpha‐C helix is on the left. Drawn using PyMol based on structure #6JOL from Protein Data Bank. (B) NIH3T3 cell lines expressing the indicated receptor were produced as shown in Figure . Cells were starved for 4 h and treated with different concentrations of imatinib as indicated. As a positive control, cells expressing the WT receptor were stimulated with PDGF‐BB for 15 min. The total lysates were analysed by Western blotting. (C) Ba/F3 cells expressing WT PDGFRB or βV665A were produced as described in Figure . Cells were stimulated with PDGF‐BB for 24 h in the presence of the indicated concentration of imatinib. Four hours before harvest, [ H]‐thymidine was added to each well. Radiolabelled thymidine incorporation was quantified and compared to cells that were not treated with imatinib. The average of three independent experiments is shown with SEM and statistical analysis ( anova test, p < 0.01)

    Article Snippet: Cells were treated with human PDGF‐BB (25 ng/ml), IFNγ (25 ng/ml, both from PeproTech), imatinib (LC laboratories) or ruxolitinib (INCB18424, MedChemExpress) as indicated.

    Techniques: Mutagenesis, Activity Assay, Expressing, Produced, Positive Control, Western Blot, Concentration Assay