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    Addgene inc pcag gphn fingr egfp ccr5tc
    Development of anti-GluN1 intrabody (A) Schematic diagram illustrating GluN1 domain structure and the anti-GluN1 intrabody target region (834–863 amino acids). (B) Illustration of <t>CCR5TC-mediated</t> transcriptional regulation. To avoid overproduction and subsequent random diffusion of intrabodies, intrabody candidates were fused with mCherry and CCR5TC. If the interaction is unsaturated, protein expression continues for further GluN1 binding. If 100% of GluN1 binds to the intrabody, then the newly synthesized intrabodies move to the nucleus and bind to a zinc-finger binding site (zfbs) upstream of a promoter to discontinue protein expression. (C–F) Colocalization and interaction of Clone#31, but not Clone#2, with GluN1 in heterologous cells. Intrabody candidates (Clone#31 and #2) were fused with mCherry and CCR5TC and expressed in HeLa cells with or without SEP-fused GluN1. In the absence of SEP-GluN1, both Clone#31 and #2 localized in the nucleus due to the nuclear localization signal of CCR5TC (C and D, left panels). When co-expressed with SEP-GluN1 (green), Clone#31 (magenta), but not Clone#2, colocalized with SEP-GluN1, depicting an ER-like structure (C and D, right panels). GFP-Trap pull-down (PD) revealed the specific binding of Clone#31-mCherry-CCR5TC, but not Clone#2, to SEP-GluN1 (E and F). Scale bars, 10 μm.
    Pcag Gphn Fingr Egfp Ccr5tc, supplied by Addgene inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pcag gphn fingr egfp ccr5tc/product/Addgene inc
    Average 94 stars, based on 1 article reviews
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    86
    Thermo Fisher pa1 46 296 rrid ab 2223196
    Development of anti-GluN1 intrabody (A) Schematic diagram illustrating GluN1 domain structure and the anti-GluN1 intrabody target region (834–863 amino acids). (B) Illustration of <t>CCR5TC-mediated</t> transcriptional regulation. To avoid overproduction and subsequent random diffusion of intrabodies, intrabody candidates were fused with mCherry and CCR5TC. If the interaction is unsaturated, protein expression continues for further GluN1 binding. If 100% of GluN1 binds to the intrabody, then the newly synthesized intrabodies move to the nucleus and bind to a zinc-finger binding site (zfbs) upstream of a promoter to discontinue protein expression. (C–F) Colocalization and interaction of Clone#31, but not Clone#2, with GluN1 in heterologous cells. Intrabody candidates (Clone#31 and #2) were fused with mCherry and CCR5TC and expressed in HeLa cells with or without SEP-fused GluN1. In the absence of SEP-GluN1, both Clone#31 and #2 localized in the nucleus due to the nuclear localization signal of CCR5TC (C and D, left panels). When co-expressed with SEP-GluN1 (green), Clone#31 (magenta), but not Clone#2, colocalized with SEP-GluN1, depicting an ER-like structure (C and D, right panels). GFP-Trap pull-down (PD) revealed the specific binding of Clone#31-mCherry-CCR5TC, but not Clone#2, to SEP-GluN1 (E and F). Scale bars, 10 μm.
    Pa1 46 296 Rrid Ab 2223196, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pa1 46 296 rrid ab 2223196/product/Thermo Fisher
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pa1 46 296 rrid ab 2223196 - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    Image Search Results


    Development of anti-GluN1 intrabody (A) Schematic diagram illustrating GluN1 domain structure and the anti-GluN1 intrabody target region (834–863 amino acids). (B) Illustration of CCR5TC-mediated transcriptional regulation. To avoid overproduction and subsequent random diffusion of intrabodies, intrabody candidates were fused with mCherry and CCR5TC. If the interaction is unsaturated, protein expression continues for further GluN1 binding. If 100% of GluN1 binds to the intrabody, then the newly synthesized intrabodies move to the nucleus and bind to a zinc-finger binding site (zfbs) upstream of a promoter to discontinue protein expression. (C–F) Colocalization and interaction of Clone#31, but not Clone#2, with GluN1 in heterologous cells. Intrabody candidates (Clone#31 and #2) were fused with mCherry and CCR5TC and expressed in HeLa cells with or without SEP-fused GluN1. In the absence of SEP-GluN1, both Clone#31 and #2 localized in the nucleus due to the nuclear localization signal of CCR5TC (C and D, left panels). When co-expressed with SEP-GluN1 (green), Clone#31 (magenta), but not Clone#2, colocalized with SEP-GluN1, depicting an ER-like structure (C and D, right panels). GFP-Trap pull-down (PD) revealed the specific binding of Clone#31-mCherry-CCR5TC, but not Clone#2, to SEP-GluN1 (E and F). Scale bars, 10 μm.

    Journal: iScience

    Article Title: NMDA receptor-targeted enrichment of CaMKIIα improves fear memory

    doi: 10.1016/j.isci.2022.104864

    Figure Lengend Snippet: Development of anti-GluN1 intrabody (A) Schematic diagram illustrating GluN1 domain structure and the anti-GluN1 intrabody target region (834–863 amino acids). (B) Illustration of CCR5TC-mediated transcriptional regulation. To avoid overproduction and subsequent random diffusion of intrabodies, intrabody candidates were fused with mCherry and CCR5TC. If the interaction is unsaturated, protein expression continues for further GluN1 binding. If 100% of GluN1 binds to the intrabody, then the newly synthesized intrabodies move to the nucleus and bind to a zinc-finger binding site (zfbs) upstream of a promoter to discontinue protein expression. (C–F) Colocalization and interaction of Clone#31, but not Clone#2, with GluN1 in heterologous cells. Intrabody candidates (Clone#31 and #2) were fused with mCherry and CCR5TC and expressed in HeLa cells with or without SEP-fused GluN1. In the absence of SEP-GluN1, both Clone#31 and #2 localized in the nucleus due to the nuclear localization signal of CCR5TC (C and D, left panels). When co-expressed with SEP-GluN1 (green), Clone#31 (magenta), but not Clone#2, colocalized with SEP-GluN1, depicting an ER-like structure (C and D, right panels). GFP-Trap pull-down (PD) revealed the specific binding of Clone#31-mCherry-CCR5TC, but not Clone#2, to SEP-GluN1 (E and F). Scale bars, 10 μm.

    Article Snippet: The amplified fragments were inserted using KpnI and MluI sites into the pCAG vector backbone containing a zinc-finger binding site upstream of a CAG promoter prepared from pCAG-GPHN.FingR-EGFP-CCR5TC (Addgene #46296) ( ).

    Techniques: Diffusion-based Assay, Expressing, Binding Assay, Synthesized

    VHHAN1 associates with endogenous GluN1 in the mouse hippocampus (A) Illustration of the AAV expressing EGFP- and CCR5TC-fused VHHAN1 (AAV-EF1α-DIO-VHHAN1-EGFP). (B–F) Comparison of EGFP and VHHAN1-EGFP distribution in the mouse hippocampal dentate gyrus. Anti-GFP immunostaining visualized expression and localization of EGFP (left) and VHHAN1-EGFP (right) (B). OML, outer molecular layer; IML, inner molecular layer; GCL, granule cell layer. Scale bars, 10 μm. The molecular layer regions are shown in (C) as indicated by the dashed boxes in (B). Scale bars, 10 μm. High-magnification confocal images of hippocampal dentate gyrus co-stained with anti-GFP and anti-GluN1 antibodies showed postsynaptic puncta of VHHAN1 (green) that colocalized with endogenous GluN1 puncta (magenta) in the dentate gyrus (D and E). Scale bars, 2 μm. Quantitative analysis of the colocalization of GFP signals with endogenous GluN1 (F). Data are shown as mean ± SEM; AU, arbitrary unit; 9 randomly chosen images from 3 animals; ∗∗∗p < 0.0001; Mann-Whitney test. (G) The binding of VHHAN1 to the endogenous NMDAR complex was validated by anti-GFP co-immunoprecipitation.

    Journal: iScience

    Article Title: NMDA receptor-targeted enrichment of CaMKIIα improves fear memory

    doi: 10.1016/j.isci.2022.104864

    Figure Lengend Snippet: VHHAN1 associates with endogenous GluN1 in the mouse hippocampus (A) Illustration of the AAV expressing EGFP- and CCR5TC-fused VHHAN1 (AAV-EF1α-DIO-VHHAN1-EGFP). (B–F) Comparison of EGFP and VHHAN1-EGFP distribution in the mouse hippocampal dentate gyrus. Anti-GFP immunostaining visualized expression and localization of EGFP (left) and VHHAN1-EGFP (right) (B). OML, outer molecular layer; IML, inner molecular layer; GCL, granule cell layer. Scale bars, 10 μm. The molecular layer regions are shown in (C) as indicated by the dashed boxes in (B). Scale bars, 10 μm. High-magnification confocal images of hippocampal dentate gyrus co-stained with anti-GFP and anti-GluN1 antibodies showed postsynaptic puncta of VHHAN1 (green) that colocalized with endogenous GluN1 puncta (magenta) in the dentate gyrus (D and E). Scale bars, 2 μm. Quantitative analysis of the colocalization of GFP signals with endogenous GluN1 (F). Data are shown as mean ± SEM; AU, arbitrary unit; 9 randomly chosen images from 3 animals; ∗∗∗p < 0.0001; Mann-Whitney test. (G) The binding of VHHAN1 to the endogenous NMDAR complex was validated by anti-GFP co-immunoprecipitation.

    Article Snippet: The amplified fragments were inserted using KpnI and MluI sites into the pCAG vector backbone containing a zinc-finger binding site upstream of a CAG promoter prepared from pCAG-GPHN.FingR-EGFP-CCR5TC (Addgene #46296) ( ).

    Techniques: Expressing, Immunostaining, Staining, MANN-WHITNEY, Binding Assay, Immunoprecipitation

    Journal: iScience

    Article Title: NMDA receptor-targeted enrichment of CaMKIIα improves fear memory

    doi: 10.1016/j.isci.2022.104864

    Figure Lengend Snippet:

    Article Snippet: The amplified fragments were inserted using KpnI and MluI sites into the pCAG vector backbone containing a zinc-finger binding site upstream of a CAG promoter prepared from pCAG-GPHN.FingR-EGFP-CCR5TC (Addgene #46296) ( ).

    Techniques: Recombinant, Transfection, Blocking Assay, Plasmid Preparation, Construct, Software