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human fkbp12  (Addgene inc)


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    Structured Review

    Addgene inc human fkbp12
    Human Fkbp12, supplied by Addgene inc, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+fkbp12/FKBP-NTEVp(WT)+(Plasmid+%23137831)/pm41922352-158-46-51
    Average 94 stars, based on 2 article reviews
    human fkbp12 - by Bioz Stars, 2026-11
    94/100 stars

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    Plasmid Preparation:

    Article Title: The genetic architecture of an allosteric hormone receptor.
    Article Snippet: .. For the other tested yeast GluePCA plasmids, we replaced PYL1 with Arabidopsis thaliana GID1A (residues 2-345; from an IDT gBlock) or the human FRB domain of mTOR (residues 2025-2114; from Addgene plasmid #130812), and ABI1 with Arabidopsis thaliana GAI (residues 2-92; from an IDT gBlock) or human FKBP12 (residues 2-108; from Addgene plasmid #137831) (Supplementary Fig. 1; Supplementary Data 1B). ..

    Article Title: The genetic architecture of an allosteric hormone receptor.
    Article Snippet: .. For the other tested yeast GluePCA plasmids, we replaced PYL1 with Arabidopsis thaliana GID1A (residues 2-34557; from an IDT gBlock) or the human FRB domain of mTOR (residues 2025-211458; from Addgene plasmid #13081282), and ABI1 with Arabidopsis thaliana GAI (residues 2-9283; from an IDT gBlock) or human FKBP12 (residues 2-10858; from Addgene plasmid #13783182) (Supplementary Fig. 1; Supplementary Data 1B). ..



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    (A) Western-blot analysis of the in-vitro dephosphorylation assay using mouse brain extracts. The “Control” sample (lane 1) was not subject to the dephosphorylation assay. (B) Quantification of dephosphorylation in vitro (pS295/PSD-95) incubated with calcium (Ca 2+ (+)) or without calcium (Ca 2+ (-)), relative to no-incubation (Control) conditions. The data are represented as the mean ± standard deviation (n = 3 from three independent experiments). *** P < 0.001 by the unpaired Student’s t -test; n.s., not significant. (C, D) Western-blot analysis (C) and quantification (D) of the efficiency of suppression by different doses of FK506 on the Ca 2+ -dependent dephosphorylation of pS295 in vitro . (E, F) Western-blot analysis (E) and quantification (F) showing that coapplication of FK506 and <t>FKBP12</t> efficiently suppressed the Ca 2+ -dependent dephosphorylation of pS295 in vitro . The data are represented as the mean ± standard deviation overlaid with individual data points (n = 3 from three independent experiments). *** P < 0.001 by two-way ANOVA with the post-hoc Tukey’s multiple comparison test; n.s., not significant. F (1,16) = 383.3, P < 0.0001 for FKBP12+FK506, F (3,16) = 48.44, P < 0.0001 for Ca 2+ , and F (3,16) = 47.06, P < 0.0001 for interaction.
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    (A) Western-blot analysis of the in-vitro dephosphorylation assay using mouse brain extracts. The “Control” sample (lane 1) was not subject to the dephosphorylation assay. (B) Quantification of dephosphorylation in vitro (pS295/PSD-95) incubated with calcium (Ca 2+ (+)) or without calcium (Ca 2+ (-)), relative to no-incubation (Control) conditions. The data are represented as the mean ± standard deviation (n = 3 from three independent experiments). *** P < 0.001 by the unpaired Student’s t -test; n.s., not significant. (C, D) Western-blot analysis (C) and quantification (D) of the efficiency of suppression by different doses of FK506 on the Ca 2+ -dependent dephosphorylation of pS295 in vitro . (E, F) Western-blot analysis (E) and quantification (F) showing that coapplication of FK506 and <t>FKBP12</t> efficiently suppressed the Ca 2+ -dependent dephosphorylation of pS295 in vitro . The data are represented as the mean ± standard deviation overlaid with individual data points (n = 3 from three independent experiments). *** P < 0.001 by two-way ANOVA with the post-hoc Tukey’s multiple comparison test; n.s., not significant. F (1,16) = 383.3, P < 0.0001 for FKBP12+FK506, F (3,16) = 48.44, P < 0.0001 for Ca 2+ , and F (3,16) = 47.06, P < 0.0001 for interaction.
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    (A) Western-blot analysis of the in-vitro dephosphorylation assay using mouse brain extracts. The “Control” sample (lane 1) was not subject to the dephosphorylation assay. (B) Quantification of dephosphorylation in vitro (pS295/PSD-95) incubated with calcium (Ca 2+ (+)) or without calcium (Ca 2+ (-)), relative to no-incubation (Control) conditions. The data are represented as the mean ± standard deviation (n = 3 from three independent experiments). *** P < 0.001 by the unpaired Student’s t -test; n.s., not significant. (C, D) Western-blot analysis (C) and quantification (D) of the efficiency of suppression by different doses of FK506 on the Ca 2+ -dependent dephosphorylation of pS295 in vitro . (E, F) Western-blot analysis (E) and quantification (F) showing that coapplication of FK506 and <t>FKBP12</t> efficiently suppressed the Ca 2+ -dependent dephosphorylation of pS295 in vitro . The data are represented as the mean ± standard deviation overlaid with individual data points (n = 3 from three independent experiments). *** P < 0.001 by two-way ANOVA with the post-hoc Tukey’s multiple comparison test; n.s., not significant. F (1,16) = 383.3, P < 0.0001 for FKBP12+FK506, F (3,16) = 48.44, P < 0.0001 for Ca 2+ , and F (3,16) = 47.06, P < 0.0001 for interaction.
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    Image Search Results


    (A) Western-blot analysis of the in-vitro dephosphorylation assay using mouse brain extracts. The “Control” sample (lane 1) was not subject to the dephosphorylation assay. (B) Quantification of dephosphorylation in vitro (pS295/PSD-95) incubated with calcium (Ca 2+ (+)) or without calcium (Ca 2+ (-)), relative to no-incubation (Control) conditions. The data are represented as the mean ± standard deviation (n = 3 from three independent experiments). *** P < 0.001 by the unpaired Student’s t -test; n.s., not significant. (C, D) Western-blot analysis (C) and quantification (D) of the efficiency of suppression by different doses of FK506 on the Ca 2+ -dependent dephosphorylation of pS295 in vitro . (E, F) Western-blot analysis (E) and quantification (F) showing that coapplication of FK506 and FKBP12 efficiently suppressed the Ca 2+ -dependent dephosphorylation of pS295 in vitro . The data are represented as the mean ± standard deviation overlaid with individual data points (n = 3 from three independent experiments). *** P < 0.001 by two-way ANOVA with the post-hoc Tukey’s multiple comparison test; n.s., not significant. F (1,16) = 383.3, P < 0.0001 for FKBP12+FK506, F (3,16) = 48.44, P < 0.0001 for Ca 2+ , and F (3,16) = 47.06, P < 0.0001 for interaction.

    Journal: PLOS ONE

    Article Title: Ca 2+ -PP2B-PSD-95 axis: A novel regulatory mechanism of the phosphorylation state of Serine 295 of PSD-95

    doi: 10.1371/journal.pone.0313441

    Figure Lengend Snippet: (A) Western-blot analysis of the in-vitro dephosphorylation assay using mouse brain extracts. The “Control” sample (lane 1) was not subject to the dephosphorylation assay. (B) Quantification of dephosphorylation in vitro (pS295/PSD-95) incubated with calcium (Ca 2+ (+)) or without calcium (Ca 2+ (-)), relative to no-incubation (Control) conditions. The data are represented as the mean ± standard deviation (n = 3 from three independent experiments). *** P < 0.001 by the unpaired Student’s t -test; n.s., not significant. (C, D) Western-blot analysis (C) and quantification (D) of the efficiency of suppression by different doses of FK506 on the Ca 2+ -dependent dephosphorylation of pS295 in vitro . (E, F) Western-blot analysis (E) and quantification (F) showing that coapplication of FK506 and FKBP12 efficiently suppressed the Ca 2+ -dependent dephosphorylation of pS295 in vitro . The data are represented as the mean ± standard deviation overlaid with individual data points (n = 3 from three independent experiments). *** P < 0.001 by two-way ANOVA with the post-hoc Tukey’s multiple comparison test; n.s., not significant. F (1,16) = 383.3, P < 0.0001 for FKBP12+FK506, F (3,16) = 48.44, P < 0.0001 for Ca 2+ , and F (3,16) = 47.06, P < 0.0001 for interaction.

    Article Snippet: NMDA was obtained from Sigma-Aldrich (St. Louis, MO, USA), EGTA from Wako Chemicals (Osaka, Japan), FK506 from ChemScene (Monmouth Junction, NJ, USA), ascomycin from Cayman Chemical (Ann Arbor, MI, USA), cyclosporine A from Nacalai Tesque (Kyoto, Japan), calyculin A from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and recombinant FKBP12 from R&D Systems (Minneapolis, MN, USA).

    Techniques: Western Blot, In Vitro, De-Phosphorylation Assay, Control, Incubation, Standard Deviation, Comparison