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alphascreen signal  (Tecan Systems)


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    Tecan Systems alphascreen signal
    Alphascreen Signal, supplied by Tecan Systems, used in various techniques. Bioz Stars score: 99/100, based on 16796 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/alphascreen+signal/Spark/pm35384315-41-4-13
    Average 99 stars, based on 16796 article reviews
    alphascreen signal - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Incubation:

    Article Title: Discovery of two novel ALKBH5 selective inhibitors that exhibit uncompetitive or competitive type and suppress the growth activity of glioblastoma multiforme.
    Article Snippet: In recent years, among the many different RNA modifications known as the ‘epitranscriptome’, a group of enzymes related to RNA methylation (Cantara et al., 2011; Czerwoniec et al., 2009) has been attracting attention as a new target for anticancer activity.. The N6methyladenosine (m6A) modification of RNA is known to be the most common and has an important role in the regulation of gene expression based on the epigenetic control of transcripts (Dominissini et al., 2012; Meyer et al., 2012).. Recently, the m6A modification was found to play an important role in regulating mRNA stability (Wang et al., 2014) and protein translation (Meyer et al., 2015).

    Amplified Luminescent Proximity Homogenous Assay:

    Article Title: Discovery of two novel ALKBH5 selective inhibitors that exhibit uncompetitive or competitive type and suppress the growth activity of glioblastoma multiforme.
    Article Snippet: In recent years, among the many different RNA modifications known as the ‘epitranscriptome’, a group of enzymes related to RNA methylation (Cantara et al., 2011; Czerwoniec et al., 2009) has been attracting attention as a new target for anticancer activity.. The N6methyladenosine (m6A) modification of RNA is known to be the most common and has an important role in the regulation of gene expression based on the epigenetic control of transcripts (Dominissini et al., 2012; Meyer et al., 2012).. Recently, the m6A modification was found to play an important role in regulating mRNA stability (Wang et al., 2014) and protein translation (Meyer et al., 2015).



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    Figure 1. Pirh2 and KLHDC10 directly bind to Ala-tails (A) Domain arrangement of human Pirh2: NTM, N-terminal module; RING, really interesting new gene domain; CTD, C-terminal domain. (B) In vitro GST pull-down assay using the specified GST-Pirh2 truncation constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (C) <t>AlphaScreen</t> assay to assess Pirh2-Ala-tail binding. Reactants were GST fusions with Pirh2 fragments containing both the NTM and RING domains (Pirh21–195) or the NTM alone (Pirh21–137) and a biotinylated Ala-tail peptide (MDELYKAAAAAA). Proximity-induced fluorescence signal (see STAR Methods) was monitored in the presence of increasing amounts of a competing, non-biotinylated Ala-tail peptide to determine IC50 values from the dose-response curve. Each data point is a technical triplicate, and error bars represent ± SD. The y axis presents the normalized AlphaScreen signal as arbitrary fluorescence units (AFUs). (D) Domain arrangement of human KLHDC10. (E) In vitro GST pull-down assay using the GST-KLHDC10 and GST-KLHDC2 constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (F) AlphaScreen assay to assess KLHDC10-Ala-tail binding. As in (C) but using GST-KLHDC10 and GST-KLHDC10b1-88–442 instead. See also Figures S1, S2, S10, and S11.
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    Figure 1. Pirh2 and KLHDC10 directly bind to Ala-tails (A) Domain arrangement of human Pirh2: NTM, N-terminal module; RING, really interesting new gene domain; CTD, C-terminal domain. (B) In vitro GST pull-down assay using the specified GST-Pirh2 truncation constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (C) <t>AlphaScreen</t> assay to assess Pirh2-Ala-tail binding. Reactants were GST fusions with Pirh2 fragments containing both the NTM and RING domains (Pirh21–195) or the NTM alone (Pirh21–137) and a biotinylated Ala-tail peptide (MDELYKAAAAAA). Proximity-induced fluorescence signal (see STAR Methods) was monitored in the presence of increasing amounts of a competing, non-biotinylated Ala-tail peptide to determine IC50 values from the dose-response curve. Each data point is a technical triplicate, and error bars represent ± SD. The y axis presents the normalized AlphaScreen signal as arbitrary fluorescence units (AFUs). (D) Domain arrangement of human KLHDC10. (E) In vitro GST pull-down assay using the GST-KLHDC10 and GST-KLHDC2 constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (F) AlphaScreen assay to assess KLHDC10-Ala-tail binding. As in (C) but using GST-KLHDC10 and GST-KLHDC10b1-88–442 instead. See also Figures S1, S2, S10, and S11.
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    Figure 1. Pirh2 and KLHDC10 directly bind to Ala-tails (A) Domain arrangement of human Pirh2: NTM, N-terminal module; RING, really interesting new gene domain; CTD, C-terminal domain. (B) In vitro GST pull-down assay using the specified GST-Pirh2 truncation constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (C) <t>AlphaScreen</t> assay to assess Pirh2-Ala-tail binding. Reactants were GST fusions with Pirh2 fragments containing both the NTM and RING domains (Pirh21–195) or the NTM alone (Pirh21–137) and a biotinylated Ala-tail peptide (MDELYKAAAAAA). Proximity-induced fluorescence signal (see STAR Methods) was monitored in the presence of increasing amounts of a competing, non-biotinylated Ala-tail peptide to determine IC50 values from the dose-response curve. Each data point is a technical triplicate, and error bars represent ± SD. The y axis presents the normalized AlphaScreen signal as arbitrary fluorescence units (AFUs). (D) Domain arrangement of human KLHDC10. (E) In vitro GST pull-down assay using the GST-KLHDC10 and GST-KLHDC2 constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (F) AlphaScreen assay to assess KLHDC10-Ala-tail binding. As in (C) but using GST-KLHDC10 and GST-KLHDC10b1-88–442 instead. See also Figures S1, S2, S10, and S11.
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    Figure 1. Pirh2 and KLHDC10 directly bind to Ala-tails (A) Domain arrangement of human Pirh2: NTM, N-terminal module; RING, really interesting new gene domain; CTD, C-terminal domain. (B) In vitro GST pull-down assay using the specified GST-Pirh2 truncation constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (C) <t>AlphaScreen</t> assay to assess Pirh2-Ala-tail binding. Reactants were GST fusions with Pirh2 fragments containing both the NTM and RING domains (Pirh21–195) or the NTM alone (Pirh21–137) and a biotinylated Ala-tail peptide (MDELYKAAAAAA). Proximity-induced fluorescence signal (see STAR Methods) was monitored in the presence of increasing amounts of a competing, non-biotinylated Ala-tail peptide to determine IC50 values from the dose-response curve. Each data point is a technical triplicate, and error bars represent ± SD. The y axis presents the normalized AlphaScreen signal as arbitrary fluorescence units (AFUs). (D) Domain arrangement of human KLHDC10. (E) In vitro GST pull-down assay using the GST-KLHDC10 and GST-KLHDC2 constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (F) AlphaScreen assay to assess KLHDC10-Ala-tail binding. As in (C) but using GST-KLHDC10 and GST-KLHDC10b1-88–442 instead. See also Figures S1, S2, S10, and S11.
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    Image Search Results


    Figure 1. Pirh2 and KLHDC10 directly bind to Ala-tails (A) Domain arrangement of human Pirh2: NTM, N-terminal module; RING, really interesting new gene domain; CTD, C-terminal domain. (B) In vitro GST pull-down assay using the specified GST-Pirh2 truncation constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (C) AlphaScreen assay to assess Pirh2-Ala-tail binding. Reactants were GST fusions with Pirh2 fragments containing both the NTM and RING domains (Pirh21–195) or the NTM alone (Pirh21–137) and a biotinylated Ala-tail peptide (MDELYKAAAAAA). Proximity-induced fluorescence signal (see STAR Methods) was monitored in the presence of increasing amounts of a competing, non-biotinylated Ala-tail peptide to determine IC50 values from the dose-response curve. Each data point is a technical triplicate, and error bars represent ± SD. The y axis presents the normalized AlphaScreen signal as arbitrary fluorescence units (AFUs). (D) Domain arrangement of human KLHDC10. (E) In vitro GST pull-down assay using the GST-KLHDC10 and GST-KLHDC2 constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (F) AlphaScreen assay to assess KLHDC10-Ala-tail binding. As in (C) but using GST-KLHDC10 and GST-KLHDC10b1-88–442 instead. See also Figures S1, S2, S10, and S11.

    Journal: Cell reports

    Article Title: Mechanism and evolutionary origins of alanine-tail C-degron recognition by E3 ligases Pirh2 and CRL2-KLHDC10.

    doi: 10.1016/j.celrep.2023.113100

    Figure Lengend Snippet: Figure 1. Pirh2 and KLHDC10 directly bind to Ala-tails (A) Domain arrangement of human Pirh2: NTM, N-terminal module; RING, really interesting new gene domain; CTD, C-terminal domain. (B) In vitro GST pull-down assay using the specified GST-Pirh2 truncation constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (C) AlphaScreen assay to assess Pirh2-Ala-tail binding. Reactants were GST fusions with Pirh2 fragments containing both the NTM and RING domains (Pirh21–195) or the NTM alone (Pirh21–137) and a biotinylated Ala-tail peptide (MDELYKAAAAAA). Proximity-induced fluorescence signal (see STAR Methods) was monitored in the presence of increasing amounts of a competing, non-biotinylated Ala-tail peptide to determine IC50 values from the dose-response curve. Each data point is a technical triplicate, and error bars represent ± SD. The y axis presents the normalized AlphaScreen signal as arbitrary fluorescence units (AFUs). (D) Domain arrangement of human KLHDC10. (E) In vitro GST pull-down assay using the GST-KLHDC10 and GST-KLHDC2 constructs and recombinantly purified GFP or GFP-Ala6. Anti-GST and anti-GFP immunoblots are indicated. (F) AlphaScreen assay to assess KLHDC10-Ala-tail binding. As in (C) but using GST-KLHDC10 and GST-KLHDC10b1-88–442 instead. See also Figures S1, S2, S10, and S11.

    Article Snippet: AlphaScreen signal was measured using PHERAstar microplate reader (BMG Labtech) at RT.

    Techniques: In Vitro, Pull Down Assay, Construct, Western Blot, Amplified Luminescent Proximity Homogenous Assay, Binding Assay