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su5402  (MedChemExpress)


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    MedChemExpress su5402
    NECA promotes AKT phosphorylation in ChEC, which is dependent on PI3K but not <t>VEGFR2</t> activity. ( A ). The expression levels of phosphorylated AKT, total AKT, and β-actin were detected by Western blot following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) treatment. ( B ) Relative expression of p AKT and t AKT (total AKT) was quantified using ImageJ and Prism software (* p < 0.05; ** p < 0.01; NS: not significant). NECA-mediated enhanced AKT phosphorylation was independent of VEFGR2 activity. ( C ) The expression of phosphorylated AKT, total AKT, and β-actin was detected by Western blot after DMSO (Con), NECA (N), or <t>SU5402</t> + NECA (SU + N) treatment. ( D ) Relative expression of p AKT and t AKT was quantified using ImageJ and Prism software (* p < 0.05; NS: not significant, n = 5). NECA promotes the migration of ChEC, which is mitigated by incubation with the PI3K inhibitor. ( E ) Phalloidin (green) and DAPI (blue) staining were used to detect migrated ChEC following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) within Transwells. ( F ) The cells that were transferred through the Transwell were counted using ImageJ, and data were analyzed using the Prism software (* p < 0.05, n = 8).
    Su5402, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/su5402/product/MedChemExpress
    Average 94 stars, based on 27 article reviews
    su5402 - by Bioz Stars, 2026-05
    94/100 stars

    Images

    1) Product Images from "Caffeine Mitigates Adenosine-Mediated Angiogenic Properties of Choroidal Endothelial Cells Through Antagonism of A 1 Adenosine Receptor and PI3K-AKT Axis"

    Article Title: Caffeine Mitigates Adenosine-Mediated Angiogenic Properties of Choroidal Endothelial Cells Through Antagonism of A 1 Adenosine Receptor and PI3K-AKT Axis

    Journal: Cells

    doi: 10.3390/cells15010087

    NECA promotes AKT phosphorylation in ChEC, which is dependent on PI3K but not VEGFR2 activity. ( A ). The expression levels of phosphorylated AKT, total AKT, and β-actin were detected by Western blot following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) treatment. ( B ) Relative expression of p AKT and t AKT (total AKT) was quantified using ImageJ and Prism software (* p < 0.05; ** p < 0.01; NS: not significant). NECA-mediated enhanced AKT phosphorylation was independent of VEFGR2 activity. ( C ) The expression of phosphorylated AKT, total AKT, and β-actin was detected by Western blot after DMSO (Con), NECA (N), or SU5402 + NECA (SU + N) treatment. ( D ) Relative expression of p AKT and t AKT was quantified using ImageJ and Prism software (* p < 0.05; NS: not significant, n = 5). NECA promotes the migration of ChEC, which is mitigated by incubation with the PI3K inhibitor. ( E ) Phalloidin (green) and DAPI (blue) staining were used to detect migrated ChEC following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) within Transwells. ( F ) The cells that were transferred through the Transwell were counted using ImageJ, and data were analyzed using the Prism software (* p < 0.05, n = 8).
    Figure Legend Snippet: NECA promotes AKT phosphorylation in ChEC, which is dependent on PI3K but not VEGFR2 activity. ( A ). The expression levels of phosphorylated AKT, total AKT, and β-actin were detected by Western blot following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) treatment. ( B ) Relative expression of p AKT and t AKT (total AKT) was quantified using ImageJ and Prism software (* p < 0.05; ** p < 0.01; NS: not significant). NECA-mediated enhanced AKT phosphorylation was independent of VEFGR2 activity. ( C ) The expression of phosphorylated AKT, total AKT, and β-actin was detected by Western blot after DMSO (Con), NECA (N), or SU5402 + NECA (SU + N) treatment. ( D ) Relative expression of p AKT and t AKT was quantified using ImageJ and Prism software (* p < 0.05; NS: not significant, n = 5). NECA promotes the migration of ChEC, which is mitigated by incubation with the PI3K inhibitor. ( E ) Phalloidin (green) and DAPI (blue) staining were used to detect migrated ChEC following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) within Transwells. ( F ) The cells that were transferred through the Transwell were counted using ImageJ, and data were analyzed using the Prism software (* p < 0.05, n = 8).

    Techniques Used: Phospho-proteomics, Activity Assay, Expressing, Western Blot, Incubation, Software, Migration, Staining



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    NECA promotes AKT phosphorylation in ChEC, which is dependent on PI3K but not <t>VEGFR2</t> activity. ( A ). The expression levels of phosphorylated AKT, total AKT, and β-actin were detected by Western blot following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) treatment. ( B ) Relative expression of p AKT and t AKT (total AKT) was quantified using ImageJ and Prism software (* p < 0.05; ** p < 0.01; NS: not significant). NECA-mediated enhanced AKT phosphorylation was independent of VEFGR2 activity. ( C ) The expression of phosphorylated AKT, total AKT, and β-actin was detected by Western blot after DMSO (Con), NECA (N), or <t>SU5402</t> + NECA (SU + N) treatment. ( D ) Relative expression of p AKT and t AKT was quantified using ImageJ and Prism software (* p < 0.05; NS: not significant, n = 5). NECA promotes the migration of ChEC, which is mitigated by incubation with the PI3K inhibitor. ( E ) Phalloidin (green) and DAPI (blue) staining were used to detect migrated ChEC following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) within Transwells. ( F ) The cells that were transferred through the Transwell were counted using ImageJ, and data were analyzed using the Prism software (* p < 0.05, n = 8).
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    Image Search Results


    NECA promotes AKT phosphorylation in ChEC, which is dependent on PI3K but not VEGFR2 activity. ( A ). The expression levels of phosphorylated AKT, total AKT, and β-actin were detected by Western blot following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) treatment. ( B ) Relative expression of p AKT and t AKT (total AKT) was quantified using ImageJ and Prism software (* p < 0.05; ** p < 0.01; NS: not significant). NECA-mediated enhanced AKT phosphorylation was independent of VEFGR2 activity. ( C ) The expression of phosphorylated AKT, total AKT, and β-actin was detected by Western blot after DMSO (Con), NECA (N), or SU5402 + NECA (SU + N) treatment. ( D ) Relative expression of p AKT and t AKT was quantified using ImageJ and Prism software (* p < 0.05; NS: not significant, n = 5). NECA promotes the migration of ChEC, which is mitigated by incubation with the PI3K inhibitor. ( E ) Phalloidin (green) and DAPI (blue) staining were used to detect migrated ChEC following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) within Transwells. ( F ) The cells that were transferred through the Transwell were counted using ImageJ, and data were analyzed using the Prism software (* p < 0.05, n = 8).

    Journal: Cells

    Article Title: Caffeine Mitigates Adenosine-Mediated Angiogenic Properties of Choroidal Endothelial Cells Through Antagonism of A 1 Adenosine Receptor and PI3K-AKT Axis

    doi: 10.3390/cells15010087

    Figure Lengend Snippet: NECA promotes AKT phosphorylation in ChEC, which is dependent on PI3K but not VEGFR2 activity. ( A ). The expression levels of phosphorylated AKT, total AKT, and β-actin were detected by Western blot following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) treatment. ( B ) Relative expression of p AKT and t AKT (total AKT) was quantified using ImageJ and Prism software (* p < 0.05; ** p < 0.01; NS: not significant). NECA-mediated enhanced AKT phosphorylation was independent of VEFGR2 activity. ( C ) The expression of phosphorylated AKT, total AKT, and β-actin was detected by Western blot after DMSO (Con), NECA (N), or SU5402 + NECA (SU + N) treatment. ( D ) Relative expression of p AKT and t AKT was quantified using ImageJ and Prism software (* p < 0.05; NS: not significant, n = 5). NECA promotes the migration of ChEC, which is mitigated by incubation with the PI3K inhibitor. ( E ) Phalloidin (green) and DAPI (blue) staining were used to detect migrated ChEC following incubation with DMSO (con), NECA (N), or LY294002 + NECA (Ly + N) within Transwells. ( F ) The cells that were transferred through the Transwell were counted using ImageJ, and data were analyzed using the Prism software (* p < 0.05, n = 8).

    Article Snippet: Caffeine citrate (51754-0500-1; Exela Pharma Sciences, Lenoir, NC, USA), Bz-ATP (2′(3′)-O-(4-benzoylbenzoyl) adenosine -5ʹ -triphosphate, tri(triethylammonium) salt (HY-136254), NECA (5′-N-ethylcarboxamidoadenosine, HY-103173), DPCPX (A 1 AR antagonist, HY-100937), Istradefylline (A 2A AR antagonist, HY-10888), MRS1754 (A 2B AR antagonist, HY-14121), MRS1523 (A 3 AR antagonist, HY-121119), SU5402 (VEGFR2 inhibitor, HY-10407) (Med Chem Express, Monmouth Junction, NJ, USA), LY294002 (PI3K inhibitor, L9908; Sigma), and AZ 11645373 (P2X7 receptor antagonist, 3317; R&D Systems, Minneapolis, MN, USA) were prepared with the desired concentration in EC growth medium.

    Techniques: Phospho-proteomics, Activity Assay, Expressing, Western Blot, Incubation, Software, Migration, Staining