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anti phospho gab1  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc anti phospho gab1
    Anti Phospho Gab1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phospho+gab1/Phospho-Gab1+(Tyr627)+Antibody/bio_rxiv__64898__2025__12__11__693497-233-17-38
    Average 93 stars, based on 50 article reviews
    anti phospho gab1 - by Bioz Stars, 2026-08
    93/100 stars

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    Fig. 7 PI3K-dependent <t>GAB1/Erk</t> phosphorylation rendered HNSCC cells sensitive to CYH33. A proposed scheme representing the mechanism of CYH33 executed its anti-HNSCC effect. CYH33 inhibited the proliferation of HNSCC cells via attenuating PI3K-dependent <t>GAB1</t> membrane localization and phosphorylation, which resulted in reduced activity of PI3K and MAPK pathway. Further inhibition of GAB1 phosphorylation independent of PI3K potentiated the activity of CYH33 against HNSCC.
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    Fig. 7 PI3K-dependent <t>GAB1/Erk</t> phosphorylation rendered HNSCC cells sensitive to CYH33. A proposed scheme representing the mechanism of CYH33 executed its anti-HNSCC effect. CYH33 inhibited the proliferation of HNSCC cells via attenuating PI3K-dependent <t>GAB1</t> membrane localization and phosphorylation, which resulted in reduced activity of PI3K and MAPK pathway. Further inhibition of GAB1 phosphorylation independent of PI3K potentiated the activity of CYH33 against HNSCC.
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    Image Search Results


    Fig. 7 PI3K-dependent GAB1/Erk phosphorylation rendered HNSCC cells sensitive to CYH33. A proposed scheme representing the mechanism of CYH33 executed its anti-HNSCC effect. CYH33 inhibited the proliferation of HNSCC cells via attenuating PI3K-dependent GAB1 membrane localization and phosphorylation, which resulted in reduced activity of PI3K and MAPK pathway. Further inhibition of GAB1 phosphorylation independent of PI3K potentiated the activity of CYH33 against HNSCC.

    Journal: Cell death & disease

    Article Title: PI3K-dependent GAB1/Erk phosphorylation renders head and neck squamous cell carcinoma sensitive to PI3Kα inhibitors.

    doi: 10.1038/s41419-025-07767-x

    Figure Lengend Snippet: Fig. 7 PI3K-dependent GAB1/Erk phosphorylation rendered HNSCC cells sensitive to CYH33. A proposed scheme representing the mechanism of CYH33 executed its anti-HNSCC effect. CYH33 inhibited the proliferation of HNSCC cells via attenuating PI3K-dependent GAB1 membrane localization and phosphorylation, which resulted in reduced activity of PI3K and MAPK pathway. Further inhibition of GAB1 phosphorylation independent of PI3K potentiated the activity of CYH33 against HNSCC.

    Article Snippet: Standard Western blotting was performed with antibodies against Akt (#4691), phospho-Akt (Ser473; #4060), S6K (#5707), phospho-S6K (Thr389; #9205), Erk (#4695), phospho-Erk (Thr185/Tyr187; #4370), GAB1 (#93804), phospho-GAB1 (Tyr 659; #12745), PI3Kα (#4249), PI3Kβ (#3011), PTEN (#9559) (Cell Signaling Technology, Danvers, USA) and GAPDH (#G8795) (Sigma, St. Louis, USA).

    Techniques: Phospho-proteomics, Membrane, Activity Assay, Inhibition