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mouse α-ap2  (Millipore)


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    Structured Review

    Millipore mouse α-ap2
    Domain-specific mutations in Amph1 disrupt its ability to form protein-protein complexes. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused N-BAR-lacking mutants either with or without the SH3 domain. Point mutations were introduced within the CLAP domain including FFE to SSR for the <t>α-AP2</t> binding site; and DLD to HSR and WD to SR for the CHC binding sites as indicated. (B) GST-pull-down experiments were performed using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR mutants. The binding affinity of purified endocytic proteins including endophilin A1, CHC, α-AP2 subunits, and Dyn1 was assessed by immunoblotting. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the GST-Amph1-ΔSH3 constructs which run at a similar molecular weight. (C-F) Quantification of the binding efficacy of CHC (C), α-AP2 subunits (D), Dyn1 (E), and endophilin A1 (F) by determining relative band intensities normalised to the level of the total GST-fused proteins and WT controls. Bars indicate mean ± SEM. ** p < 0.01, *** p < 0.001, and ****p < 0.0001 by one-way ANOVA followed by Tukey’s multiple comparison test. n = 4 synaptosomal lysates/condition from 4 rat brains.
    Mouse α Ap2, supplied by Millipore, 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/product/mouse+%CE%B1-ap2/bio_rxiv__2023__01__15__524101-80-29-32?v=Millipore
    Average 90 stars, based on 1 article reviews
    mouse α-ap2 - by Bioz Stars, 2026-07
    90/100 stars

    Images

    1) Product Images from "The phospho-regulated amphiphysin/endophilin interaction is required for synaptic vesicle endocytosis"

    Article Title: The phospho-regulated amphiphysin/endophilin interaction is required for synaptic vesicle endocytosis

    Journal: bioRxiv

    doi: 10.1101/2023.01.15.524101

    Domain-specific mutations in Amph1 disrupt its ability to form protein-protein complexes. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused N-BAR-lacking mutants either with or without the SH3 domain. Point mutations were introduced within the CLAP domain including FFE to SSR for the α-AP2 binding site; and DLD to HSR and WD to SR for the CHC binding sites as indicated. (B) GST-pull-down experiments were performed using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR mutants. The binding affinity of purified endocytic proteins including endophilin A1, CHC, α-AP2 subunits, and Dyn1 was assessed by immunoblotting. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the GST-Amph1-ΔSH3 constructs which run at a similar molecular weight. (C-F) Quantification of the binding efficacy of CHC (C), α-AP2 subunits (D), Dyn1 (E), and endophilin A1 (F) by determining relative band intensities normalised to the level of the total GST-fused proteins and WT controls. Bars indicate mean ± SEM. ** p < 0.01, *** p < 0.001, and ****p < 0.0001 by one-way ANOVA followed by Tukey’s multiple comparison test. n = 4 synaptosomal lysates/condition from 4 rat brains.
    Figure Legend Snippet: Domain-specific mutations in Amph1 disrupt its ability to form protein-protein complexes. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused N-BAR-lacking mutants either with or without the SH3 domain. Point mutations were introduced within the CLAP domain including FFE to SSR for the α-AP2 binding site; and DLD to HSR and WD to SR for the CHC binding sites as indicated. (B) GST-pull-down experiments were performed using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR mutants. The binding affinity of purified endocytic proteins including endophilin A1, CHC, α-AP2 subunits, and Dyn1 was assessed by immunoblotting. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the GST-Amph1-ΔSH3 constructs which run at a similar molecular weight. (C-F) Quantification of the binding efficacy of CHC (C), α-AP2 subunits (D), Dyn1 (E), and endophilin A1 (F) by determining relative band intensities normalised to the level of the total GST-fused proteins and WT controls. Bars indicate mean ± SEM. ** p < 0.01, *** p < 0.001, and ****p < 0.0001 by one-way ANOVA followed by Tukey’s multiple comparison test. n = 4 synaptosomal lysates/condition from 4 rat brains.

    Techniques Used: Binding Assay, Affinity Purification, Western Blot, Staining, Construct, Molecular Weight

    The Amph1-endophilin A1 complex is formed at the motif 301 PPVPP 305 within the PRD and is controlled by the phosphorylation status of Amph1-S293. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused ΔN-BAR- and ΔSH3 mutants. Point mutations were introduced within the PRD domain including substitutions of proline to alanine residues for AVRA, A 1 A 2 VA 3 A 4 , A1A2, and A3A4 mutants, and S293A and S293E respectively. (B) GST-pull-down experiments using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR-ΔSH3 mutants to assess binding affinity to endophilin A1 and other SH3-containing proteins, such as CHC, α-AP2, PSD95, and syndapin 1. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the Amph1-ΔNBAR-ΔSH3 constructs which run at a similar molecular weight. (C) Quantification of the endophilin binding efficacy by determining relative band intensities normalised to the level of the GST-fused proteins and WT Amph1-ΔNBAR-ΔSH3. Bars indicate mean ± SEM. n = 4 synaptosomal lysates/condition from 4 rat brains, * p < 0.05 by one-way ANOVA followed by Dunnett’s multiple comparison test.
    Figure Legend Snippet: The Amph1-endophilin A1 complex is formed at the motif 301 PPVPP 305 within the PRD and is controlled by the phosphorylation status of Amph1-S293. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused ΔN-BAR- and ΔSH3 mutants. Point mutations were introduced within the PRD domain including substitutions of proline to alanine residues for AVRA, A 1 A 2 VA 3 A 4 , A1A2, and A3A4 mutants, and S293A and S293E respectively. (B) GST-pull-down experiments using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR-ΔSH3 mutants to assess binding affinity to endophilin A1 and other SH3-containing proteins, such as CHC, α-AP2, PSD95, and syndapin 1. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the Amph1-ΔNBAR-ΔSH3 constructs which run at a similar molecular weight. (C) Quantification of the endophilin binding efficacy by determining relative band intensities normalised to the level of the GST-fused proteins and WT Amph1-ΔNBAR-ΔSH3. Bars indicate mean ± SEM. n = 4 synaptosomal lysates/condition from 4 rat brains, * p < 0.05 by one-way ANOVA followed by Dunnett’s multiple comparison test.

    Techniques Used: Binding Assay, Staining, Construct, Molecular Weight



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    Image Search Results


    Domain-specific mutations in Amph1 disrupt its ability to form protein-protein complexes. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused N-BAR-lacking mutants either with or without the SH3 domain. Point mutations were introduced within the CLAP domain including FFE to SSR for the α-AP2 binding site; and DLD to HSR and WD to SR for the CHC binding sites as indicated. (B) GST-pull-down experiments were performed using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR mutants. The binding affinity of purified endocytic proteins including endophilin A1, CHC, α-AP2 subunits, and Dyn1 was assessed by immunoblotting. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the GST-Amph1-ΔSH3 constructs which run at a similar molecular weight. (C-F) Quantification of the binding efficacy of CHC (C), α-AP2 subunits (D), Dyn1 (E), and endophilin A1 (F) by determining relative band intensities normalised to the level of the total GST-fused proteins and WT controls. Bars indicate mean ± SEM. ** p < 0.01, *** p < 0.001, and ****p < 0.0001 by one-way ANOVA followed by Tukey’s multiple comparison test. n = 4 synaptosomal lysates/condition from 4 rat brains.

    Journal: bioRxiv

    Article Title: The phospho-regulated amphiphysin/endophilin interaction is required for synaptic vesicle endocytosis

    doi: 10.1101/2023.01.15.524101

    Figure Lengend Snippet: Domain-specific mutations in Amph1 disrupt its ability to form protein-protein complexes. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused N-BAR-lacking mutants either with or without the SH3 domain. Point mutations were introduced within the CLAP domain including FFE to SSR for the α-AP2 binding site; and DLD to HSR and WD to SR for the CHC binding sites as indicated. (B) GST-pull-down experiments were performed using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR mutants. The binding affinity of purified endocytic proteins including endophilin A1, CHC, α-AP2 subunits, and Dyn1 was assessed by immunoblotting. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the GST-Amph1-ΔSH3 constructs which run at a similar molecular weight. (C-F) Quantification of the binding efficacy of CHC (C), α-AP2 subunits (D), Dyn1 (E), and endophilin A1 (F) by determining relative band intensities normalised to the level of the total GST-fused proteins and WT controls. Bars indicate mean ± SEM. ** p < 0.01, *** p < 0.001, and ****p < 0.0001 by one-way ANOVA followed by Tukey’s multiple comparison test. n = 4 synaptosomal lysates/condition from 4 rat brains.

    Article Snippet: The primary antibodies used in this study are as follows: goat endophilin A1 (1:1000; Santa Cruz Biotechnology, cat no. sc-10874), goat CHC (1:250: Santa Cruz Biotechnology, cat no. sc-6579), mouse α-AP2 (1:1000; Sigma Aldrich, cat no. A4325), goat Dyn1 (1:500; Santa Cruz Biotechnology, sc-6402), goat syndapin 1 (1:1000; Santa Cruz Biotechnology, sc-10412), and mouse PSD95 (1:1000; BioLegend, cat no. 810401).

    Techniques: Binding Assay, Affinity Purification, Western Blot, Staining, Construct, Molecular Weight

    The Amph1-endophilin A1 complex is formed at the motif 301 PPVPP 305 within the PRD and is controlled by the phosphorylation status of Amph1-S293. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused ΔN-BAR- and ΔSH3 mutants. Point mutations were introduced within the PRD domain including substitutions of proline to alanine residues for AVRA, A 1 A 2 VA 3 A 4 , A1A2, and A3A4 mutants, and S293A and S293E respectively. (B) GST-pull-down experiments using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR-ΔSH3 mutants to assess binding affinity to endophilin A1 and other SH3-containing proteins, such as CHC, α-AP2, PSD95, and syndapin 1. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the Amph1-ΔNBAR-ΔSH3 constructs which run at a similar molecular weight. (C) Quantification of the endophilin binding efficacy by determining relative band intensities normalised to the level of the GST-fused proteins and WT Amph1-ΔNBAR-ΔSH3. Bars indicate mean ± SEM. n = 4 synaptosomal lysates/condition from 4 rat brains, * p < 0.05 by one-way ANOVA followed by Dunnett’s multiple comparison test.

    Journal: bioRxiv

    Article Title: The phospho-regulated amphiphysin/endophilin interaction is required for synaptic vesicle endocytosis

    doi: 10.1101/2023.01.15.524101

    Figure Lengend Snippet: The Amph1-endophilin A1 complex is formed at the motif 301 PPVPP 305 within the PRD and is controlled by the phosphorylation status of Amph1-S293. (A) Schematic representation of the structural domains of Amph1 that were used for generating GST-fused ΔN-BAR- and ΔSH3 mutants. Point mutations were introduced within the PRD domain including substitutions of proline to alanine residues for AVRA, A 1 A 2 VA 3 A 4 , A1A2, and A3A4 mutants, and S293A and S293E respectively. (B) GST-pull-down experiments using synaptosomal lysates from rat brains and GST-fused Amph1-ΔNBAR-ΔSH3 mutants to assess binding affinity to endophilin A1 and other SH3-containing proteins, such as CHC, α-AP2, PSD95, and syndapin 1. CBB staining was performed in parallel to assess GST-fusion protein levels (arrows). Representative images are displayed. The abnormal separation of α-AP2 subunits may result from the high protein content of the Amph1-ΔNBAR-ΔSH3 constructs which run at a similar molecular weight. (C) Quantification of the endophilin binding efficacy by determining relative band intensities normalised to the level of the GST-fused proteins and WT Amph1-ΔNBAR-ΔSH3. Bars indicate mean ± SEM. n = 4 synaptosomal lysates/condition from 4 rat brains, * p < 0.05 by one-way ANOVA followed by Dunnett’s multiple comparison test.

    Article Snippet: The primary antibodies used in this study are as follows: goat endophilin A1 (1:1000; Santa Cruz Biotechnology, cat no. sc-10874), goat CHC (1:250: Santa Cruz Biotechnology, cat no. sc-6579), mouse α-AP2 (1:1000; Sigma Aldrich, cat no. A4325), goat Dyn1 (1:500; Santa Cruz Biotechnology, sc-6402), goat syndapin 1 (1:1000; Santa Cruz Biotechnology, sc-10412), and mouse PSD95 (1:1000; BioLegend, cat no. 810401).

    Techniques: Binding Assay, Staining, Construct, Molecular Weight