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human grb2 sequence  (Addgene inc)


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    Addgene inc human grb2 sequence
    Recruitment of the GBA motif of GIV to activated EGFR is sufficient to induce G protein activation. A, diagram depicting how <t>Grb2</t> fused to the GBA motif (aa 1660–1705) of GIV (Grb2-GBA) is recruited from the cytosol to tyrosine phosphorylated EGFR at the plasma membrane upon activation. Grb2-mediated binding to EGFR brings the GBA motif close to membrane-bound Gi3. B and C, HEK293T cells were transfected with plasmids for all the components required BRET-based G protein activity measurements as described for Fig. 3, Grb2-GBA (WT or FA) and EGFR. EGF (50 ng/μl) was added at the indicated time (arrow in B). BRET results (B) are the averages of three or four independent experiments, and the error bars are the S.E. (shown only at 5-s intervals for clarity). Representative immunoblots of the cells used in these experiments are shown in C.
    Human Grb2 Sequence, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human grb2 sequence/product/Addgene inc
    Average 90 stars, based on 1 article reviews
    human grb2 sequence - by Bioz Stars, 2026-02
    90/100 stars

    Images

    1) Product Images from "Membrane Recruitment of the Non-receptor Protein GIV/Girdin (Gα-interacting, Vesicle-associated Protein/Girdin) Is Sufficient for Activating Heterotrimeric G Protein Signaling * "

    Article Title: Membrane Recruitment of the Non-receptor Protein GIV/Girdin (Gα-interacting, Vesicle-associated Protein/Girdin) Is Sufficient for Activating Heterotrimeric G Protein Signaling *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M116.764431

    Recruitment of the GBA motif of GIV to activated EGFR is sufficient to induce G protein activation. A, diagram depicting how Grb2 fused to the GBA motif (aa 1660–1705) of GIV (Grb2-GBA) is recruited from the cytosol to tyrosine phosphorylated EGFR at the plasma membrane upon activation. Grb2-mediated binding to EGFR brings the GBA motif close to membrane-bound Gi3. B and C, HEK293T cells were transfected with plasmids for all the components required BRET-based G protein activity measurements as described for Fig. 3, Grb2-GBA (WT or FA) and EGFR. EGF (50 ng/μl) was added at the indicated time (arrow in B). BRET results (B) are the averages of three or four independent experiments, and the error bars are the S.E. (shown only at 5-s intervals for clarity). Representative immunoblots of the cells used in these experiments are shown in C.
    Figure Legend Snippet: Recruitment of the GBA motif of GIV to activated EGFR is sufficient to induce G protein activation. A, diagram depicting how Grb2 fused to the GBA motif (aa 1660–1705) of GIV (Grb2-GBA) is recruited from the cytosol to tyrosine phosphorylated EGFR at the plasma membrane upon activation. Grb2-mediated binding to EGFR brings the GBA motif close to membrane-bound Gi3. B and C, HEK293T cells were transfected with plasmids for all the components required BRET-based G protein activity measurements as described for Fig. 3, Grb2-GBA (WT or FA) and EGFR. EGF (50 ng/μl) was added at the indicated time (arrow in B). BRET results (B) are the averages of three or four independent experiments, and the error bars are the S.E. (shown only at 5-s intervals for clarity). Representative immunoblots of the cells used in these experiments are shown in C.

    Techniques Used: Activation Assay, Clinical Proteomics, Membrane, Binding Assay, Transfection, Activity Assay, Western Blot

    Model depicting the parallelism between the mechanisms of activation of Gαi and Ras by their respective cytoplasmic GEFs, GIV, and SOS, upon RTK stimulation. A, under resting conditions, SOS is primarily located in the cytosol along with Grb2, whereas its substrate G protein Ras is constitutively anchored to the plasma membrane, thereby precluding SOS action. Upon RTK stimulation, Grb2-SOS complexes translocate to the plasma membrane via binding of Grb2 SH2 domains to tyrosine phosphorylated EGFR. This change of localization brings SOS in physical proximity to Ras, thereby promoting G protein activation. B, under resting conditions, GIV is primarily located in the cytosol, whereas its substrate G protein Gαi is constitutively anchored to the plasma membrane, thereby precluding GIV action. Upon RTK stimulation, GIV translocates to the plasma membrane via binding of its SH2-like domain to tyrosine phosphorylated EGFR. This change of localization brings GIV in physical proximity to Gαi, thereby promoting G protein activation.
    Figure Legend Snippet: Model depicting the parallelism between the mechanisms of activation of Gαi and Ras by their respective cytoplasmic GEFs, GIV, and SOS, upon RTK stimulation. A, under resting conditions, SOS is primarily located in the cytosol along with Grb2, whereas its substrate G protein Ras is constitutively anchored to the plasma membrane, thereby precluding SOS action. Upon RTK stimulation, Grb2-SOS complexes translocate to the plasma membrane via binding of Grb2 SH2 domains to tyrosine phosphorylated EGFR. This change of localization brings SOS in physical proximity to Ras, thereby promoting G protein activation. B, under resting conditions, GIV is primarily located in the cytosol, whereas its substrate G protein Gαi is constitutively anchored to the plasma membrane, thereby precluding GIV action. Upon RTK stimulation, GIV translocates to the plasma membrane via binding of its SH2-like domain to tyrosine phosphorylated EGFR. This change of localization brings GIV in physical proximity to Gαi, thereby promoting G protein activation.

    Techniques Used: Activation Assay, Clinical Proteomics, Membrane, Binding Assay



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    human grb2 sequence  (Addgene inc)
    90
    Addgene inc human grb2 sequence
    Recruitment of the GBA motif of GIV to activated EGFR is sufficient to induce G protein activation. A, diagram depicting how <t>Grb2</t> fused to the GBA motif (aa 1660–1705) of GIV (Grb2-GBA) is recruited from the cytosol to tyrosine phosphorylated EGFR at the plasma membrane upon activation. Grb2-mediated binding to EGFR brings the GBA motif close to membrane-bound Gi3. B and C, HEK293T cells were transfected with plasmids for all the components required BRET-based G protein activity measurements as described for Fig. 3, Grb2-GBA (WT or FA) and EGFR. EGF (50 ng/μl) was added at the indicated time (arrow in B). BRET results (B) are the averages of three or four independent experiments, and the error bars are the S.E. (shown only at 5-s intervals for clarity). Representative immunoblots of the cells used in these experiments are shown in C.
    Human Grb2 Sequence, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human grb2 sequence/product/Addgene inc
    Average 90 stars, based on 1 article reviews
    human grb2 sequence - by Bioz Stars, 2026-02
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Recruitment of the GBA motif of GIV to activated EGFR is sufficient to induce G protein activation. A, diagram depicting how Grb2 fused to the GBA motif (aa 1660–1705) of GIV (Grb2-GBA) is recruited from the cytosol to tyrosine phosphorylated EGFR at the plasma membrane upon activation. Grb2-mediated binding to EGFR brings the GBA motif close to membrane-bound Gi3. B and C, HEK293T cells were transfected with plasmids for all the components required BRET-based G protein activity measurements as described for Fig. 3, Grb2-GBA (WT or FA) and EGFR. EGF (50 ng/μl) was added at the indicated time (arrow in B). BRET results (B) are the averages of three or four independent experiments, and the error bars are the S.E. (shown only at 5-s intervals for clarity). Representative immunoblots of the cells used in these experiments are shown in C.

    Journal: The Journal of Biological Chemistry

    Article Title: Membrane Recruitment of the Non-receptor Protein GIV/Girdin (Gα-interacting, Vesicle-associated Protein/Girdin) Is Sufficient for Activating Heterotrimeric G Protein Signaling *

    doi: 10.1074/jbc.M116.764431

    Figure Lengend Snippet: Recruitment of the GBA motif of GIV to activated EGFR is sufficient to induce G protein activation. A, diagram depicting how Grb2 fused to the GBA motif (aa 1660–1705) of GIV (Grb2-GBA) is recruited from the cytosol to tyrosine phosphorylated EGFR at the plasma membrane upon activation. Grb2-mediated binding to EGFR brings the GBA motif close to membrane-bound Gi3. B and C, HEK293T cells were transfected with plasmids for all the components required BRET-based G protein activity measurements as described for Fig. 3, Grb2-GBA (WT or FA) and EGFR. EGF (50 ng/μl) was added at the indicated time (arrow in B). BRET results (B) are the averages of three or four independent experiments, and the error bars are the S.E. (shown only at 5-s intervals for clarity). Representative immunoblots of the cells used in these experiments are shown in C.

    Article Snippet: Grb2-GBA was generated by replacing the mRFP and FKBP sequences of FKBP-GIV-GBA (1660–1705) with the human Grb2 sequence (amplified from Addgene plasmid catalog no. 70383) preceded by a Myc tag (NheI/NruI sites). pcDNA6A-EGFR was obtained from Addgene (catalog no. 42665).

    Techniques: Activation Assay, Clinical Proteomics, Membrane, Binding Assay, Transfection, Activity Assay, Western Blot

    Model depicting the parallelism between the mechanisms of activation of Gαi and Ras by their respective cytoplasmic GEFs, GIV, and SOS, upon RTK stimulation. A, under resting conditions, SOS is primarily located in the cytosol along with Grb2, whereas its substrate G protein Ras is constitutively anchored to the plasma membrane, thereby precluding SOS action. Upon RTK stimulation, Grb2-SOS complexes translocate to the plasma membrane via binding of Grb2 SH2 domains to tyrosine phosphorylated EGFR. This change of localization brings SOS in physical proximity to Ras, thereby promoting G protein activation. B, under resting conditions, GIV is primarily located in the cytosol, whereas its substrate G protein Gαi is constitutively anchored to the plasma membrane, thereby precluding GIV action. Upon RTK stimulation, GIV translocates to the plasma membrane via binding of its SH2-like domain to tyrosine phosphorylated EGFR. This change of localization brings GIV in physical proximity to Gαi, thereby promoting G protein activation.

    Journal: The Journal of Biological Chemistry

    Article Title: Membrane Recruitment of the Non-receptor Protein GIV/Girdin (Gα-interacting, Vesicle-associated Protein/Girdin) Is Sufficient for Activating Heterotrimeric G Protein Signaling *

    doi: 10.1074/jbc.M116.764431

    Figure Lengend Snippet: Model depicting the parallelism between the mechanisms of activation of Gαi and Ras by their respective cytoplasmic GEFs, GIV, and SOS, upon RTK stimulation. A, under resting conditions, SOS is primarily located in the cytosol along with Grb2, whereas its substrate G protein Ras is constitutively anchored to the plasma membrane, thereby precluding SOS action. Upon RTK stimulation, Grb2-SOS complexes translocate to the plasma membrane via binding of Grb2 SH2 domains to tyrosine phosphorylated EGFR. This change of localization brings SOS in physical proximity to Ras, thereby promoting G protein activation. B, under resting conditions, GIV is primarily located in the cytosol, whereas its substrate G protein Gαi is constitutively anchored to the plasma membrane, thereby precluding GIV action. Upon RTK stimulation, GIV translocates to the plasma membrane via binding of its SH2-like domain to tyrosine phosphorylated EGFR. This change of localization brings GIV in physical proximity to Gαi, thereby promoting G protein activation.

    Article Snippet: Grb2-GBA was generated by replacing the mRFP and FKBP sequences of FKBP-GIV-GBA (1660–1705) with the human Grb2 sequence (amplified from Addgene plasmid catalog no. 70383) preceded by a Myc tag (NheI/NruI sites). pcDNA6A-EGFR was obtained from Addgene (catalog no. 42665).

    Techniques: Activation Assay, Clinical Proteomics, Membrane, Binding Assay