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n 6 phenyl atp  (Jena Bioscience)


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    Jena Bioscience n 6 phenyl atp
    (A) In vitro kinase assay with the purified analog-sensitive (AS) variant of CaMKIIβ. CaMKII activity against a protein substrate (Syntide 2, fused to GST) was measured as a function of calmodulin concentration. Direct phosphorylation of the substrate by the analog-sensitive F89G variant was measured via 32 P incorporation. Samples were separated on an SDS–PAGE and detected using autoradiography. (A, B) Quantification of (A), normalized to the maximum activity at 400 nM calmodulin. Data for the wt variant of CaMKIIβΔ13 and CaMKIIβΔ13,16 are taken from . Error bars indicate SD (n = 3). (C) Inhibition of the AS variant of CaMKIIβ by various <t>N</t> <t>6</t> -modified <t>ATP</t> analogs. An in vitro kinase assay was performed at an optimal calmodulin concentration and supplemented with different non-radioactive ATP analogs. (A) Enzymatic activity was measured as described for (A). (C, D) Quantification of (C), normalized to the non-inhibited signal (n = 3). Note that the wt enzyme is not inhibited by N 6 -modified ATP analogs, whereas the AS variant is inhibited. (E) Western blot showing the labeling efficiency in permeabilized cells. N2A cells overexpressing Twin-Strep-CaMKIIIβΔ13,16-F89G were collected and permeabilized with nOG (n-octyl-β-D-glucopyranoside) or Tween-20 as indicated, or lysed by brief sonication. Reactions were performed with N 6 -benzyl-ATPγS in the presence–absence of stimulating conditions (calmodulin/Ca 2+ ) and/or an external substrate (Syntide 2, linked to GST). Samples were alkylated, run on an SDS–PAGE, and analyzed via Western blot with a thiophosphate ester–specific antibody. (F) Correlation matrix of the substrate spectra of different CaMKIIβ isoforms, as determined by an analog-sensitive kinase assay. The analysis was restricted to CaMKIIβ-specific targets. In addition, CaMKIIβ autophosphorylation targets were removed from the analysis. A Person correlation coefficient was calculated based on the intensity values of individual phosphorylation sites.
    N 6 Phenyl Atp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n 6 phenyl atp/product/Jena Bioscience
    Average 90 stars, based on 2 article reviews
    n 6 phenyl atp - by Bioz Stars, 2026-02
    90/100 stars

    Images

    1) Product Images from "Branch point strength controls species-specific CAMK2B alternative splicing and regulates LTP"

    Article Title: Branch point strength controls species-specific CAMK2B alternative splicing and regulates LTP

    Journal: Life Science Alliance

    doi: 10.26508/lsa.202201826

    (A) In vitro kinase assay with the purified analog-sensitive (AS) variant of CaMKIIβ. CaMKII activity against a protein substrate (Syntide 2, fused to GST) was measured as a function of calmodulin concentration. Direct phosphorylation of the substrate by the analog-sensitive F89G variant was measured via 32 P incorporation. Samples were separated on an SDS–PAGE and detected using autoradiography. (A, B) Quantification of (A), normalized to the maximum activity at 400 nM calmodulin. Data for the wt variant of CaMKIIβΔ13 and CaMKIIβΔ13,16 are taken from . Error bars indicate SD (n = 3). (C) Inhibition of the AS variant of CaMKIIβ by various N 6 -modified ATP analogs. An in vitro kinase assay was performed at an optimal calmodulin concentration and supplemented with different non-radioactive ATP analogs. (A) Enzymatic activity was measured as described for (A). (C, D) Quantification of (C), normalized to the non-inhibited signal (n = 3). Note that the wt enzyme is not inhibited by N 6 -modified ATP analogs, whereas the AS variant is inhibited. (E) Western blot showing the labeling efficiency in permeabilized cells. N2A cells overexpressing Twin-Strep-CaMKIIIβΔ13,16-F89G were collected and permeabilized with nOG (n-octyl-β-D-glucopyranoside) or Tween-20 as indicated, or lysed by brief sonication. Reactions were performed with N 6 -benzyl-ATPγS in the presence–absence of stimulating conditions (calmodulin/Ca 2+ ) and/or an external substrate (Syntide 2, linked to GST). Samples were alkylated, run on an SDS–PAGE, and analyzed via Western blot with a thiophosphate ester–specific antibody. (F) Correlation matrix of the substrate spectra of different CaMKIIβ isoforms, as determined by an analog-sensitive kinase assay. The analysis was restricted to CaMKIIβ-specific targets. In addition, CaMKIIβ autophosphorylation targets were removed from the analysis. A Person correlation coefficient was calculated based on the intensity values of individual phosphorylation sites.
    Figure Legend Snippet: (A) In vitro kinase assay with the purified analog-sensitive (AS) variant of CaMKIIβ. CaMKII activity against a protein substrate (Syntide 2, fused to GST) was measured as a function of calmodulin concentration. Direct phosphorylation of the substrate by the analog-sensitive F89G variant was measured via 32 P incorporation. Samples were separated on an SDS–PAGE and detected using autoradiography. (A, B) Quantification of (A), normalized to the maximum activity at 400 nM calmodulin. Data for the wt variant of CaMKIIβΔ13 and CaMKIIβΔ13,16 are taken from . Error bars indicate SD (n = 3). (C) Inhibition of the AS variant of CaMKIIβ by various N 6 -modified ATP analogs. An in vitro kinase assay was performed at an optimal calmodulin concentration and supplemented with different non-radioactive ATP analogs. (A) Enzymatic activity was measured as described for (A). (C, D) Quantification of (C), normalized to the non-inhibited signal (n = 3). Note that the wt enzyme is not inhibited by N 6 -modified ATP analogs, whereas the AS variant is inhibited. (E) Western blot showing the labeling efficiency in permeabilized cells. N2A cells overexpressing Twin-Strep-CaMKIIIβΔ13,16-F89G were collected and permeabilized with nOG (n-octyl-β-D-glucopyranoside) or Tween-20 as indicated, or lysed by brief sonication. Reactions were performed with N 6 -benzyl-ATPγS in the presence–absence of stimulating conditions (calmodulin/Ca 2+ ) and/or an external substrate (Syntide 2, linked to GST). Samples were alkylated, run on an SDS–PAGE, and analyzed via Western blot with a thiophosphate ester–specific antibody. (F) Correlation matrix of the substrate spectra of different CaMKIIβ isoforms, as determined by an analog-sensitive kinase assay. The analysis was restricted to CaMKIIβ-specific targets. In addition, CaMKIIβ autophosphorylation targets were removed from the analysis. A Person correlation coefficient was calculated based on the intensity values of individual phosphorylation sites.

    Techniques Used: In Vitro, Kinase Assay, Purification, Variant Assay, Activity Assay, Concentration Assay, SDS Page, Autoradiography, Inhibition, Modification, Western Blot, Labeling, Sonication



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    n 6 phenyl atp  (Jena Bioscience)
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    Jena Bioscience n 6 phenyl atp
    (A) In vitro kinase assay with the purified analog-sensitive (AS) variant of CaMKIIβ. CaMKII activity against a protein substrate (Syntide 2, fused to GST) was measured as a function of calmodulin concentration. Direct phosphorylation of the substrate by the analog-sensitive F89G variant was measured via 32 P incorporation. Samples were separated on an SDS–PAGE and detected using autoradiography. (A, B) Quantification of (A), normalized to the maximum activity at 400 nM calmodulin. Data for the wt variant of CaMKIIβΔ13 and CaMKIIβΔ13,16 are taken from . Error bars indicate SD (n = 3). (C) Inhibition of the AS variant of CaMKIIβ by various <t>N</t> <t>6</t> -modified <t>ATP</t> analogs. An in vitro kinase assay was performed at an optimal calmodulin concentration and supplemented with different non-radioactive ATP analogs. (A) Enzymatic activity was measured as described for (A). (C, D) Quantification of (C), normalized to the non-inhibited signal (n = 3). Note that the wt enzyme is not inhibited by N 6 -modified ATP analogs, whereas the AS variant is inhibited. (E) Western blot showing the labeling efficiency in permeabilized cells. N2A cells overexpressing Twin-Strep-CaMKIIIβΔ13,16-F89G were collected and permeabilized with nOG (n-octyl-β-D-glucopyranoside) or Tween-20 as indicated, or lysed by brief sonication. Reactions were performed with N 6 -benzyl-ATPγS in the presence–absence of stimulating conditions (calmodulin/Ca 2+ ) and/or an external substrate (Syntide 2, linked to GST). Samples were alkylated, run on an SDS–PAGE, and analyzed via Western blot with a thiophosphate ester–specific antibody. (F) Correlation matrix of the substrate spectra of different CaMKIIβ isoforms, as determined by an analog-sensitive kinase assay. The analysis was restricted to CaMKIIβ-specific targets. In addition, CaMKIIβ autophosphorylation targets were removed from the analysis. A Person correlation coefficient was calculated based on the intensity values of individual phosphorylation sites.
    N 6 Phenyl Atp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n 6 phenyl atp/product/Jena Bioscience
    Average 90 stars, based on 1 article reviews
    n 6 phenyl atp - by Bioz Stars, 2026-02
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) In vitro kinase assay with the purified analog-sensitive (AS) variant of CaMKIIβ. CaMKII activity against a protein substrate (Syntide 2, fused to GST) was measured as a function of calmodulin concentration. Direct phosphorylation of the substrate by the analog-sensitive F89G variant was measured via 32 P incorporation. Samples were separated on an SDS–PAGE and detected using autoradiography. (A, B) Quantification of (A), normalized to the maximum activity at 400 nM calmodulin. Data for the wt variant of CaMKIIβΔ13 and CaMKIIβΔ13,16 are taken from . Error bars indicate SD (n = 3). (C) Inhibition of the AS variant of CaMKIIβ by various N 6 -modified ATP analogs. An in vitro kinase assay was performed at an optimal calmodulin concentration and supplemented with different non-radioactive ATP analogs. (A) Enzymatic activity was measured as described for (A). (C, D) Quantification of (C), normalized to the non-inhibited signal (n = 3). Note that the wt enzyme is not inhibited by N 6 -modified ATP analogs, whereas the AS variant is inhibited. (E) Western blot showing the labeling efficiency in permeabilized cells. N2A cells overexpressing Twin-Strep-CaMKIIIβΔ13,16-F89G were collected and permeabilized with nOG (n-octyl-β-D-glucopyranoside) or Tween-20 as indicated, or lysed by brief sonication. Reactions were performed with N 6 -benzyl-ATPγS in the presence–absence of stimulating conditions (calmodulin/Ca 2+ ) and/or an external substrate (Syntide 2, linked to GST). Samples were alkylated, run on an SDS–PAGE, and analyzed via Western blot with a thiophosphate ester–specific antibody. (F) Correlation matrix of the substrate spectra of different CaMKIIβ isoforms, as determined by an analog-sensitive kinase assay. The analysis was restricted to CaMKIIβ-specific targets. In addition, CaMKIIβ autophosphorylation targets were removed from the analysis. A Person correlation coefficient was calculated based on the intensity values of individual phosphorylation sites.

    Journal: Life Science Alliance

    Article Title: Branch point strength controls species-specific CAMK2B alternative splicing and regulates LTP

    doi: 10.26508/lsa.202201826

    Figure Lengend Snippet: (A) In vitro kinase assay with the purified analog-sensitive (AS) variant of CaMKIIβ. CaMKII activity against a protein substrate (Syntide 2, fused to GST) was measured as a function of calmodulin concentration. Direct phosphorylation of the substrate by the analog-sensitive F89G variant was measured via 32 P incorporation. Samples were separated on an SDS–PAGE and detected using autoradiography. (A, B) Quantification of (A), normalized to the maximum activity at 400 nM calmodulin. Data for the wt variant of CaMKIIβΔ13 and CaMKIIβΔ13,16 are taken from . Error bars indicate SD (n = 3). (C) Inhibition of the AS variant of CaMKIIβ by various N 6 -modified ATP analogs. An in vitro kinase assay was performed at an optimal calmodulin concentration and supplemented with different non-radioactive ATP analogs. (A) Enzymatic activity was measured as described for (A). (C, D) Quantification of (C), normalized to the non-inhibited signal (n = 3). Note that the wt enzyme is not inhibited by N 6 -modified ATP analogs, whereas the AS variant is inhibited. (E) Western blot showing the labeling efficiency in permeabilized cells. N2A cells overexpressing Twin-Strep-CaMKIIIβΔ13,16-F89G were collected and permeabilized with nOG (n-octyl-β-D-glucopyranoside) or Tween-20 as indicated, or lysed by brief sonication. Reactions were performed with N 6 -benzyl-ATPγS in the presence–absence of stimulating conditions (calmodulin/Ca 2+ ) and/or an external substrate (Syntide 2, linked to GST). Samples were alkylated, run on an SDS–PAGE, and analyzed via Western blot with a thiophosphate ester–specific antibody. (F) Correlation matrix of the substrate spectra of different CaMKIIβ isoforms, as determined by an analog-sensitive kinase assay. The analysis was restricted to CaMKIIβ-specific targets. In addition, CaMKIIβ autophosphorylation targets were removed from the analysis. A Person correlation coefficient was calculated based on the intensity values of individual phosphorylation sites.

    Article Snippet: The reaction mixture contained varying concentrations of non-radioactive ATP (0–1 mM) or 0.5 mM of one of the following non-radioactive ATP analogs: N 6 -methyl-ATP, N 6 -etheno-ATP, N 6 -phenyl-ATP, and N 6 -benzyl-ATP (Jena Bioscience).

    Techniques: In Vitro, Kinase Assay, Purification, Variant Assay, Activity Assay, Concentration Assay, SDS Page, Autoradiography, Inhibition, Modification, Western Blot, Labeling, Sonication