active pkc alpha Search Results


pkc alpha  (Sino Biological)
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vitro pkcα kinase assay  (Sino Biological)
92
Sino Biological vitro pkcα kinase assay
Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by <t>PKC</t> α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP <t>or</t> <t>GST</t> ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).
Vitro Pkcα Kinase Assay, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pkcα  (Sino Biological)
90
Sino Biological pkcα
Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by <t>PKC</t> α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP <t>or</t> <t>GST</t> ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).
Pkcα, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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protein kinase cα pkcα  (Santa Cruz Biotechnology)
86
Santa Cruz Biotechnology protein kinase cα pkcα
Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by <t>PKC</t> α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP <t>or</t> <t>GST</t> ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).
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pkc activity assays  (Alpha Diagnostics)
90
Alpha Diagnostics pkc activity assays
Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by <t>PKC</t> α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP <t>or</t> <t>GST</t> ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).
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pkc alpha, active  (Sino Biological)
90
Sino Biological pkc alpha, active
Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by <t>PKC</t> α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP <t>or</t> <t>GST</t> ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).
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Image Search Results


Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by PKC α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP or GST ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).

Journal: FEBS Open Bio

Article Title: Protein kinase C regulates AMPA receptor auxiliary protein Shisa9/ CKAMP 44 through interactions with neuronal scaffold PICK 1

doi: 10.1002/2211-5463.12261

Figure Lengend Snippet: Shisa9/ CKAMP 44 interacts with PICK 1 and is phosphorylated by PKC α. (A) Schematic overview of Shisa9/ CKAMP 44 constructs used in this study (including the location of the respective tag): in CKAMP 44‐ FL (full length), the tag is C‐terminal to the signal peptide in the extracellular domain ( TM , yellow). Constructs with only the cytoplasmic tail of Shisa9/ CKAMP 44 are N‐terminally tagged (with either EGFP or GST ). PDZ ligand sequences are shown in red and are deleted in constructs labelled with ΔC ( PDZ ‐binding‐deficient variant). A conserved region of Shisa9/ CKAMP 44 (blue; N‐terminal region of the cytoplasmic tail) is deleted in the construct CKAMP 44‐ΔNΔC. Constructs are drawn to scale. (B) Comparative coimmunoprecipitation experiments of PICK 1 ( FLAG ‐ PICK 1) with Shisa9/ CKAMP 44 C‐terminal variants EGFP ‐ CKAMP 44, −ΔC, or −ΔNΔC). Proteins were precipitated using GFP antibody or mIgG (negative control) and detected using the antibodies indicated. Inputs are shown on the left. (C) Full‐length Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ), expressed in COS ‐7 cells, is phosphorylated following induction by PMA (1 μ m , 30 min). Phosphorylated proteins (indicated) are separated from nonphosphorylated proteins (indicated) via Phos‐tag‐ SDS / PAGE and observed via WB; phosphatase treatment with alkaline phosphatase is used as a negative control, thereby highlighting the phosphorylation dependence of the mobility shift. (D) Phosphorylation of Shisa9/ CKAMP 44 ( FLAG ‐ CKAMP 44‐ FL ) is induced with PMA and inhibited by application of the PKC inhibitor GF 109203X in COS ‐7 cells. Again phosphorylated proteins are observable via Phos‐tag‐ SDS / PAGE . PKC inhibitor concentrations are indicated above. (E) An in vitro PKC α kinase assay followed by Phos‐tag SDS / PAGE analysis highlights a PKC α‐dependent mobility shift of the phosphorylated substrate GST ‐ CKAMP 44 (top panel, Phos‐tag SDS / PAGE ). Presence of PKC α and kinase substrate present in the same samples is shown below (lower panel, standard Laemmli SDS / PAGE and WB; antibodies indicated).

Article Snippet: Purified and desalted GST‐CKAMP44 protein was used for an in vitro PKCα kinase assay (SignalChem, Richmond, Canada; #P61–18G) according to the manufacturer's instructions.

Techniques: Construct, Binding Assay, Variant Assay, Negative Control, SDS Page, Phospho-proteomics, Mobility Shift, In Vitro, Kinase Assay