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phospho c jun s63  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc phospho c jun s63
    A) schematic diagram displaying enrichment of regulated kinase identified motifs which modified the reported phospho-sites. B) The upset plot overlapped the kinase regulated known phospho-sites with either mock or BPA unique phospho-signatures. The intersection of phospho-c-JUN <t>(S63)</t> and phospho-GSK3A (Y279) along their target kinases are graphically represented. C) The western blot analysis is performed with three biological replicates of mock or BPA treated samples probed with GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK. GAPDH is used as loading control. D) The relative expression is normalized using intensity of either GAPDH or total non-phospho form and represented as mean ± SEM (N=3). The evaluation of statistical significance was performed by Student’s t-test. p-value of less than 0.05 is considered as significant.
    Phospho C Jun S63, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 426 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phospho+c+jun+s63/Phospho-c-Jun+(Ser63)+Rabbit+mAb/bio_rxiv__64898__2026__03__04__709712-138-36-39
    Average 96 stars, based on 426 article reviews
    phospho c jun s63 - by Bioz Stars, 2026-09
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    Images

    1) Product Images from "Integrated proteomic and phosphoproteomic profiling reveals mechanisms of Bisphenol-A induced placental toxicity"

    Article Title: Integrated proteomic and phosphoproteomic profiling reveals mechanisms of Bisphenol-A induced placental toxicity

    Journal: bioRxiv

    doi: 10.64898/2026.03.04.709712

    A) schematic diagram displaying enrichment of regulated kinase identified motifs which modified the reported phospho-sites. B) The upset plot overlapped the kinase regulated known phospho-sites with either mock or BPA unique phospho-signatures. The intersection of phospho-c-JUN (S63) and phospho-GSK3A (Y279) along their target kinases are graphically represented. C) The western blot analysis is performed with three biological replicates of mock or BPA treated samples probed with GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK. GAPDH is used as loading control. D) The relative expression is normalized using intensity of either GAPDH or total non-phospho form and represented as mean ± SEM (N=3). The evaluation of statistical significance was performed by Student’s t-test. p-value of less than 0.05 is considered as significant.
    Figure Legend Snippet: A) schematic diagram displaying enrichment of regulated kinase identified motifs which modified the reported phospho-sites. B) The upset plot overlapped the kinase regulated known phospho-sites with either mock or BPA unique phospho-signatures. The intersection of phospho-c-JUN (S63) and phospho-GSK3A (Y279) along their target kinases are graphically represented. C) The western blot analysis is performed with three biological replicates of mock or BPA treated samples probed with GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK. GAPDH is used as loading control. D) The relative expression is normalized using intensity of either GAPDH or total non-phospho form and represented as mean ± SEM (N=3). The evaluation of statistical significance was performed by Student’s t-test. p-value of less than 0.05 is considered as significant.

    Techniques Used: Modification, Western Blot, Control, Expressing

    A) The workflow followed for generating BPA exposed pregnancy model in mice. The uterine horn showing the embryos with fetus and placenta inside were collected from either B) mock or C) BPA exposed mice post euthanization and then imaged. D) The western blot analysis of GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK is performed using placentas (N=6) from mock and BPA exposed mice. Here also, equal loading is indicated using GAPDH. E) The densitometric analysis of the blots are displayed as mean ± SEM (N=6). The p-value of <0.05, calculated using Student’s t-test, is considered statistically significant.
    Figure Legend Snippet: A) The workflow followed for generating BPA exposed pregnancy model in mice. The uterine horn showing the embryos with fetus and placenta inside were collected from either B) mock or C) BPA exposed mice post euthanization and then imaged. D) The western blot analysis of GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK is performed using placentas (N=6) from mock and BPA exposed mice. Here also, equal loading is indicated using GAPDH. E) The densitometric analysis of the blots are displayed as mean ± SEM (N=6). The p-value of <0.05, calculated using Student’s t-test, is considered statistically significant.

    Techniques Used: Western Blot

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    Article Snippet: Phospho- c -JUN (S63) , Cell Signaling Technology , 3270; RRID: AB_2129575.

    Produced:

    Article Title: Desmoglein-3 induces YAP phosphorylation and inactivation during collective migration of oral carcinoma cells.
    Article Snippet: .. The following mouse and rabbit monoclonal/polyclonal antibodies (Abs) were used: D8H1X, rabbit Ab to YAP (14074; Cell Signalling Technology, Leiden, Netherlands); EP1675Y, rabbit Ab to YAP1 (phospho S127) (ab76252; Abcam, Cambridge, UK); D24E4, rabbit Ab to YAP/TAZ (8418; Cell Signalling Technology); LATS1/2, rabbit Ab (9153; Cell Signalling Technology); 5H10, mouse Ab against the N-terminus of Dsg3 (sc23912; Santa Cruz, Dallas, TX, USA); 33–3D, mouse IgM against Dsg2 (gift from Professor Garrod); PG 5.1, mouse Ab to Plakoglobin (65015; Progen, Heidelberg, Germany); H-300, rabbit Ab to Desmoplakin (sc-33555; Santa Cruz); 5C2, mouse Ab to PKP1 (Progen); PKP3, mouse Ab (ab151401; Abcam); HECD-1, mouse anti-N terminus of E-Cadherin (ab1416; Abcam); rabbit Ab to a-Catenin (C2081; Sigma); 6F9, mouse Ab to b-Catenin (C7082; Sigma); mouse Ab to K14 (gift from Professor Leigh); C-20, rabbit Ab to FAK (sc-558; Santa Cruz); Anti-phospho-FAK (pTyr397) rabbit Ab (SAB4504403; Sigma); D38B1, rabbit Ab to EGF Receptor (4267; Cell Signalling Technology); D7A5, rabbit Ab to PhosphoEGF Receptor (Y1068) (3777; Cell Signalling Technology); Phospho-EGFR (S695), rabbit Ab (PA5-104725; Thermo Fisher Scientific); Phospho-EGFR (Y1086), rat Ab (MAB89671; R&D Systems, Minneapolis, MN, USA); 60A8, rabbit Ab to c-Jun (9165; Cell Signalling Technology); 54B3, rabbit Ab to Phospho-c-Jun (S63) (2361; Cell Signalling Technology); G31, mouse Ab to HSP27 (2402; Cell Signalling Technology); PhosphoHSP27 (S78), rabbit Ab (2405; Cell Signalling Technology); Phospho-HSP27 (S82), rabbit Ab (2401; Cell Signalling Technology); Alexa Fluor 488 conjugated phalloidin for F-Actin (A12379; Thermo Fisher Scientific); C-20, rabbit Ab to FOXM1 (sc-502; Santa Cruz); H-432, rabbit Ab to Cyclin A (sc-751; Santa Cruz); PC10, mouse Ab to PCNA (sc-56; Santa Cruz); Y69, rabbit Ab to c-Myc (ab32072; Abcam); MIB-1, mouse Ab to Ki-67 (GA626; Agilent, Santa Clara, CA, USA); 14C10, rabbit Ab to GAPDH (2118; Cell Signalling Technology); B-6, mouse Ab to HSC 70 (sc-7298; Santa Cruz); Secondary Abs were anti-mouse/rabbit IgG peroxidase antibody produced in goat (A0168/A6667; Sigma); Alexa Fluor 488 goat anti-mouse/rabbit IgG (A11029/A11034; Thermo Fisher Scientific), and Alexa Fluor 568 goat anti-mouse/rabbit IgG (A11031/A11036; Thermo Fisher Scientific). ..

    Blocking Assay:

    Article Title: Integrated proteomic and phosphoproteomic profiling reveals mechanisms of Bisphenol-A induced placental toxicity
    Article Snippet: 40 μg protein from each sample were loaded in 10% sodium dodecyl sulphate-polyacrylamide gel (SDS-PAGE) gel for electrophoretic separation and then subsequently transferred to a 0.45 μ polyvinylidene fluoride (PVDF) membrane (IPVH00010, Millipore, Merk). .. After 1 hour blocking in 5% (W/V) skimmed milk (GRM1254, Himedia) the respective blots were incubated overnight at 4 °C with primary antibodies against GSK3α (1:2000, A19060, ABclonal), phospho-GSK3α-Y279 (1:2000, AP0261, ABclonal), c-JUN (1:1000, 9165, CST), phospho-c-JUN-S63 (1:1000, 2361, CST), PBK (1:1000, 4942, CST) and GAPDH (1:10000, A19056, ABclonal). ..

    Incubation:

    Article Title: Integrated proteomic and phosphoproteomic profiling reveals mechanisms of Bisphenol-A induced placental toxicity
    Article Snippet: 40 μg protein from each sample were loaded in 10% sodium dodecyl sulphate-polyacrylamide gel (SDS-PAGE) gel for electrophoretic separation and then subsequently transferred to a 0.45 μ polyvinylidene fluoride (PVDF) membrane (IPVH00010, Millipore, Merk). .. After 1 hour blocking in 5% (W/V) skimmed milk (GRM1254, Himedia) the respective blots were incubated overnight at 4 °C with primary antibodies against GSK3α (1:2000, A19060, ABclonal), phospho-GSK3α-Y279 (1:2000, AP0261, ABclonal), c-JUN (1:1000, 9165, CST), phospho-c-JUN-S63 (1:1000, 2361, CST), PBK (1:1000, 4942, CST) and GAPDH (1:10000, A19056, ABclonal). ..



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    Image Search Results


    A) schematic diagram displaying enrichment of regulated kinase identified motifs which modified the reported phospho-sites. B) The upset plot overlapped the kinase regulated known phospho-sites with either mock or BPA unique phospho-signatures. The intersection of phospho-c-JUN (S63) and phospho-GSK3A (Y279) along their target kinases are graphically represented. C) The western blot analysis is performed with three biological replicates of mock or BPA treated samples probed with GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK. GAPDH is used as loading control. D) The relative expression is normalized using intensity of either GAPDH or total non-phospho form and represented as mean ± SEM (N=3). The evaluation of statistical significance was performed by Student’s t-test. p-value of less than 0.05 is considered as significant.

    Journal: bioRxiv

    Article Title: Integrated proteomic and phosphoproteomic profiling reveals mechanisms of Bisphenol-A induced placental toxicity

    doi: 10.64898/2026.03.04.709712

    Figure Lengend Snippet: A) schematic diagram displaying enrichment of regulated kinase identified motifs which modified the reported phospho-sites. B) The upset plot overlapped the kinase regulated known phospho-sites with either mock or BPA unique phospho-signatures. The intersection of phospho-c-JUN (S63) and phospho-GSK3A (Y279) along their target kinases are graphically represented. C) The western blot analysis is performed with three biological replicates of mock or BPA treated samples probed with GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK. GAPDH is used as loading control. D) The relative expression is normalized using intensity of either GAPDH or total non-phospho form and represented as mean ± SEM (N=3). The evaluation of statistical significance was performed by Student’s t-test. p-value of less than 0.05 is considered as significant.

    Article Snippet: After 1 hour blocking in 5% (W/V) skimmed milk (GRM1254, Himedia) the respective blots were incubated overnight at 4 °C with primary antibodies against GSK3α (1:2000, A19060, ABclonal), phospho-GSK3α-Y279 (1:2000, AP0261, ABclonal), c-JUN (1:1000, 9165, CST), phospho-c-JUN-S63 (1:1000, 2361, CST), PBK (1:1000, 4942, CST) and GAPDH (1:10000, A19056, ABclonal).

    Techniques: Modification, Western Blot, Control, Expressing

    A) The workflow followed for generating BPA exposed pregnancy model in mice. The uterine horn showing the embryos with fetus and placenta inside were collected from either B) mock or C) BPA exposed mice post euthanization and then imaged. D) The western blot analysis of GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK is performed using placentas (N=6) from mock and BPA exposed mice. Here also, equal loading is indicated using GAPDH. E) The densitometric analysis of the blots are displayed as mean ± SEM (N=6). The p-value of <0.05, calculated using Student’s t-test, is considered statistically significant.

    Journal: bioRxiv

    Article Title: Integrated proteomic and phosphoproteomic profiling reveals mechanisms of Bisphenol-A induced placental toxicity

    doi: 10.64898/2026.03.04.709712

    Figure Lengend Snippet: A) The workflow followed for generating BPA exposed pregnancy model in mice. The uterine horn showing the embryos with fetus and placenta inside were collected from either B) mock or C) BPA exposed mice post euthanization and then imaged. D) The western blot analysis of GSK3α, phospho-GSK3α (Y279), c-JUN, phospho-c-JUN (S63), and PBK is performed using placentas (N=6) from mock and BPA exposed mice. Here also, equal loading is indicated using GAPDH. E) The densitometric analysis of the blots are displayed as mean ± SEM (N=6). The p-value of <0.05, calculated using Student’s t-test, is considered statistically significant.

    Article Snippet: After 1 hour blocking in 5% (W/V) skimmed milk (GRM1254, Himedia) the respective blots were incubated overnight at 4 °C with primary antibodies against GSK3α (1:2000, A19060, ABclonal), phospho-GSK3α-Y279 (1:2000, AP0261, ABclonal), c-JUN (1:1000, 9165, CST), phospho-c-JUN-S63 (1:1000, 2361, CST), PBK (1:1000, 4942, CST) and GAPDH (1:10000, A19056, ABclonal).

    Techniques: Western Blot