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    • anti phospho ck2 substrate  (Cell Signaling Technology Inc)
    94
    Cell Signaling Technology Inc anti phospho ck2 substrate
    Anti Phospho Ck2 Substrate, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ck2 substrate/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho ck2 substrate - by Bioz Stars, 2023-12
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    anti ck2 phospho substrate  (Cell Signaling Technology Inc)
    86
    Cell Signaling Technology Inc anti ck2 phospho substrate
    Motif analysis of phosphorylation changes in iKras PDAC cells in response to Kras G12D induction. Phospho to total proteomic changes from Fig were annotated for different kinase target linear phospho‐motifs in Perseus (Tyanova et al , ), and subjected to 1D annotation enrichment test (FDR < 0.02). Kras G12D ‐induced median shift in the phosphorylation intensity was plotted against the total number of the sites for each indicated motif (Dataset ). Colors indicate the major kinase family groups (red: Proline‐directed kinases; blue: Casein kinases; orange: AGC kinases; black: Ca 2+ /Calmodulin‐dependent kinases; green: STE kinases). In addition to the ERK1/2 substrate motif, motifs for substrates of several other kinases such as CDKs, CK1, <t>CK2,</t> and GPRK/β‐ARK kinases were significantly enriched among the Kras G12D ‐induced phosphorylations. A CK2 phospho‐substrate antibody mix can be used as an indicator of CK2 activity. IKras PDAC cells grown in the presence of Dox were treated overnight with the indicated concentrations of Silmitasertib, a specific CK2 inhibitor (Chon et al , ), before being subjected to lysis and immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (B), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD. Significance was calculated relative to untreated control (* P < 0.05—calculated from unpaired t ‐test). Kras G12D induction enhances CK2 activity in an Erk1/2‐dependent manner. IKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells, with or without Trametinib (10 nM), for a further 24 h. Cells were then lysed and analyzed by immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (D), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD (** P < 0.01; * P < 0.05; n.s.: not significant—calculated from unpaired t ‐test). Kras G12D induction slows the migration of myc‐Ncl through the Phos‐tag gel in an Erk1/2‐ and CK2‐dependent manner. Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for a further 24 h, with or without Trametinib (10 nM) or Silmitasertib (10 μM). Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from three independent biological replicate experiments. Kras G12D ‐induced retardation of myc‐Ncl migration through the Phos‐tag gel is dependent on S28, S34, S40, and S41. Control, wild‐type (WT), and phospho‐defective (S4A) mutant Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for 24 h. Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from two independent biological replicate experiments.
    Anti Ck2 Phospho Substrate, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti ck2 phospho substrate/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti ck2 phospho substrate - by Bioz Stars, 2023-12
    86/100 stars
    		  Buy from Supplier
    anti phospho ck2 substrate antibody  (Cell Signaling Technology Inc)
    86
    Cell Signaling Technology Inc anti phospho ck2 substrate antibody
    Motif analysis of phosphorylation changes in iKras PDAC cells in response to Kras G12D induction. Phospho to total proteomic changes from Fig were annotated for different kinase target linear phospho‐motifs in Perseus (Tyanova et al , ), and subjected to 1D annotation enrichment test (FDR < 0.02). Kras G12D ‐induced median shift in the phosphorylation intensity was plotted against the total number of the sites for each indicated motif (Dataset ). Colors indicate the major kinase family groups (red: Proline‐directed kinases; blue: Casein kinases; orange: AGC kinases; black: Ca 2+ /Calmodulin‐dependent kinases; green: STE kinases). In addition to the ERK1/2 substrate motif, motifs for substrates of several other kinases such as CDKs, CK1, <t>CK2,</t> and GPRK/β‐ARK kinases were significantly enriched among the Kras G12D ‐induced phosphorylations. A CK2 phospho‐substrate antibody mix can be used as an indicator of CK2 activity. IKras PDAC cells grown in the presence of Dox were treated overnight with the indicated concentrations of Silmitasertib, a specific CK2 inhibitor (Chon et al , ), before being subjected to lysis and immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (B), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD. Significance was calculated relative to untreated control (* P < 0.05—calculated from unpaired t ‐test). Kras G12D induction enhances CK2 activity in an Erk1/2‐dependent manner. IKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells, with or without Trametinib (10 nM), for a further 24 h. Cells were then lysed and analyzed by immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (D), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD (** P < 0.01; * P < 0.05; n.s.: not significant—calculated from unpaired t ‐test). Kras G12D induction slows the migration of myc‐Ncl through the Phos‐tag gel in an Erk1/2‐ and CK2‐dependent manner. Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for a further 24 h, with or without Trametinib (10 nM) or Silmitasertib (10 μM). Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from three independent biological replicate experiments. Kras G12D ‐induced retardation of myc‐Ncl migration through the Phos‐tag gel is dependent on S28, S34, S40, and S41. Control, wild‐type (WT), and phospho‐defective (S4A) mutant Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for 24 h. Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from two independent biological replicate experiments.
    Anti Phospho Ck2 Substrate Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ck2 substrate antibody/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho ck2 substrate antibody - by Bioz Stars, 2023-12
    86/100 stars
    		  Buy from Supplier

    Image Search Results


    Motif analysis of phosphorylation changes in iKras PDAC cells in response to Kras G12D induction. Phospho to total proteomic changes from Fig were annotated for different kinase target linear phospho‐motifs in Perseus (Tyanova et al , ), and subjected to 1D annotation enrichment test (FDR < 0.02). Kras G12D ‐induced median shift in the phosphorylation intensity was plotted against the total number of the sites for each indicated motif (Dataset ). Colors indicate the major kinase family groups (red: Proline‐directed kinases; blue: Casein kinases; orange: AGC kinases; black: Ca 2+ /Calmodulin‐dependent kinases; green: STE kinases). In addition to the ERK1/2 substrate motif, motifs for substrates of several other kinases such as CDKs, CK1, CK2, and GPRK/β‐ARK kinases were significantly enriched among the Kras G12D ‐induced phosphorylations. A CK2 phospho‐substrate antibody mix can be used as an indicator of CK2 activity. IKras PDAC cells grown in the presence of Dox were treated overnight with the indicated concentrations of Silmitasertib, a specific CK2 inhibitor (Chon et al , ), before being subjected to lysis and immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (B), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD. Significance was calculated relative to untreated control (* P < 0.05—calculated from unpaired t ‐test). Kras G12D induction enhances CK2 activity in an Erk1/2‐dependent manner. IKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells, with or without Trametinib (10 nM), for a further 24 h. Cells were then lysed and analyzed by immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (D), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD (** P < 0.01; * P < 0.05; n.s.: not significant—calculated from unpaired t ‐test). Kras G12D induction slows the migration of myc‐Ncl through the Phos‐tag gel in an Erk1/2‐ and CK2‐dependent manner. Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for a further 24 h, with or without Trametinib (10 nM) or Silmitasertib (10 μM). Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from three independent biological replicate experiments. Kras G12D ‐induced retardation of myc‐Ncl migration through the Phos‐tag gel is dependent on S28, S34, S40, and S41. Control, wild‐type (WT), and phospho‐defective (S4A) mutant Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for 24 h. Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from two independent biological replicate experiments.

    Journal: The EMBO Journal

    Article Title: An ERK1/2‐driven RNA‐binding switch in nucleolin drives ribosome biogenesis and pancreatic tumorigenesis downstream of RAS oncogene

    doi: 10.15252/embj.2022110902

    Figure Lengend Snippet: Motif analysis of phosphorylation changes in iKras PDAC cells in response to Kras G12D induction. Phospho to total proteomic changes from Fig were annotated for different kinase target linear phospho‐motifs in Perseus (Tyanova et al , ), and subjected to 1D annotation enrichment test (FDR < 0.02). Kras G12D ‐induced median shift in the phosphorylation intensity was plotted against the total number of the sites for each indicated motif (Dataset ). Colors indicate the major kinase family groups (red: Proline‐directed kinases; blue: Casein kinases; orange: AGC kinases; black: Ca 2+ /Calmodulin‐dependent kinases; green: STE kinases). In addition to the ERK1/2 substrate motif, motifs for substrates of several other kinases such as CDKs, CK1, CK2, and GPRK/β‐ARK kinases were significantly enriched among the Kras G12D ‐induced phosphorylations. A CK2 phospho‐substrate antibody mix can be used as an indicator of CK2 activity. IKras PDAC cells grown in the presence of Dox were treated overnight with the indicated concentrations of Silmitasertib, a specific CK2 inhibitor (Chon et al , ), before being subjected to lysis and immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (B), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD. Significance was calculated relative to untreated control (* P < 0.05—calculated from unpaired t ‐test). Kras G12D induction enhances CK2 activity in an Erk1/2‐dependent manner. IKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells, with or without Trametinib (10 nM), for a further 24 h. Cells were then lysed and analyzed by immunoblotting with the indicated antibodies. Quantification of normalized CK2 phospho‐substrate levels from (D), as a measure of CK2 kinase activity. A total of three independent biological replicate experiments were quantified. Error bars depict SD (** P < 0.01; * P < 0.05; n.s.: not significant—calculated from unpaired t ‐test). Kras G12D induction slows the migration of myc‐Ncl through the Phos‐tag gel in an Erk1/2‐ and CK2‐dependent manner. Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for a further 24 h, with or without Trametinib (10 nM) or Silmitasertib (10 μM). Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from three independent biological replicate experiments. Kras G12D ‐induced retardation of myc‐Ncl migration through the Phos‐tag gel is dependent on S28, S34, S40, and S41. Control, wild‐type (WT), and phospho‐defective (S4A) mutant Myc‐Ncl transfected iKras PDAC cells were grown in the absence of Dox for 48 h, before its addition to the indicated cells for 24 h. Cells were lysed and subjected to immunoprecipitation with anti‐Myc tag antibody, and the immunoprecipitates were resolved by Phos‐tag SDS–PAGE, followed by immunoblotting with the anti‐Myc antibody. In parallel, input lysates were resolved using standard SDS–PAGE, and immunoblotted with the indicated antibodies. The blots are representative results from two independent biological replicate experiments.

    Article Snippet: Anti‐CK2 phospho‐Substrate [(pS/pT)DXE] mAb mix , Cell Signaling , 8738S.

    Techniques: Activity Assay, Lysis, Western Blot, Migration, Transfection, Immunoprecipitation, SDS Page, Mutagenesis

    Journal: The EMBO Journal

    Article Title: An ERK1/2‐driven RNA‐binding switch in nucleolin drives ribosome biogenesis and pancreatic tumorigenesis downstream of RAS oncogene

    doi: 10.15252/embj.2022110902

    Figure Lengend Snippet:

    Article Snippet: Anti‐CK2 phospho‐Substrate [(pS/pT)DXE] mAb mix , Cell Signaling , 8738S.

    Techniques: Mutagenesis, Western Blot, Methylation, Transfection, Peptide Fractionation, Viability Assay, Bicinchoninic Acid Protein Assay, SYBR Green Assay, Generated, Software