Review



rabbit antibodies against syndig4  (Proteintech)


Bioz Verified Symbol Proteintech is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 92

    Structured Review

    Proteintech rabbit antibodies against syndig4
    Synapse composition is unaltered in SynDIG1-deficient synapses. A , Representative immunoblots of biochemical fractions isolated from WT and SynDIG1 β-gal homozygous mutant P14 mouse brain tissue showing levels of GluA1, GluA2, GluN1, GluN2B, PSD-93, PSD-95, synaptophysin (Synapto), SynDIG1, <t>SynDIG4,</t> and PICK-1 present in the S1-, P2-, Syn-, and PSD-enriched fractions. Loading controls are provided by β-actin and β-tubulin immunoreactivity. B–D , Graphs depict the ratio of SynDIG1 β-gal homozygous mutant protein relative to WT levels of AMPA receptor subunits ( B ), NMDA receptor subunits ( C ), and PSD-93 and PSD-95 ( D ) in the PSD-enriched fractions. Data are the average of three independent biochemical fractionation experiments; each experiment used four to six mouse brains of each genotype. Error bars represent ±SEM.
    Rabbit Antibodies Against Syndig4, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+antibodies+against+syndig4/pmc05073248-72-54-61?v=Proteintech
    Average 92 stars, based on 5 article reviews
    rabbit antibodies against syndig4 - by Bioz Stars, 2026-07
    92/100 stars

    Images

    1) Product Images from "Loss of SynDIG1 Reduces Excitatory Synapse Maturation But Not Formation In Vivo"

    Article Title: Loss of SynDIG1 Reduces Excitatory Synapse Maturation But Not Formation In Vivo

    Journal: eNeuro

    doi: 10.1523/ENEURO.0130-16.2016

    Synapse composition is unaltered in SynDIG1-deficient synapses. A , Representative immunoblots of biochemical fractions isolated from WT and SynDIG1 β-gal homozygous mutant P14 mouse brain tissue showing levels of GluA1, GluA2, GluN1, GluN2B, PSD-93, PSD-95, synaptophysin (Synapto), SynDIG1, SynDIG4, and PICK-1 present in the S1-, P2-, Syn-, and PSD-enriched fractions. Loading controls are provided by β-actin and β-tubulin immunoreactivity. B–D , Graphs depict the ratio of SynDIG1 β-gal homozygous mutant protein relative to WT levels of AMPA receptor subunits ( B ), NMDA receptor subunits ( C ), and PSD-93 and PSD-95 ( D ) in the PSD-enriched fractions. Data are the average of three independent biochemical fractionation experiments; each experiment used four to six mouse brains of each genotype. Error bars represent ±SEM.
    Figure Legend Snippet: Synapse composition is unaltered in SynDIG1-deficient synapses. A , Representative immunoblots of biochemical fractions isolated from WT and SynDIG1 β-gal homozygous mutant P14 mouse brain tissue showing levels of GluA1, GluA2, GluN1, GluN2B, PSD-93, PSD-95, synaptophysin (Synapto), SynDIG1, SynDIG4, and PICK-1 present in the S1-, P2-, Syn-, and PSD-enriched fractions. Loading controls are provided by β-actin and β-tubulin immunoreactivity. B–D , Graphs depict the ratio of SynDIG1 β-gal homozygous mutant protein relative to WT levels of AMPA receptor subunits ( B ), NMDA receptor subunits ( C ), and PSD-93 and PSD-95 ( D ) in the PSD-enriched fractions. Data are the average of three independent biochemical fractionation experiments; each experiment used four to six mouse brains of each genotype. Error bars represent ±SEM.

    Techniques Used: Western Blot, Isolation, Mutagenesis, Fractionation



    Similar Products

    92
    Proteintech rabbit antibodies against syndig4
    Synapse composition is unaltered in SynDIG1-deficient synapses. A , Representative immunoblots of biochemical fractions isolated from WT and SynDIG1 β-gal homozygous mutant P14 mouse brain tissue showing levels of GluA1, GluA2, GluN1, GluN2B, PSD-93, PSD-95, synaptophysin (Synapto), SynDIG1, <t>SynDIG4,</t> and PICK-1 present in the S1-, P2-, Syn-, and PSD-enriched fractions. Loading controls are provided by β-actin and β-tubulin immunoreactivity. B–D , Graphs depict the ratio of SynDIG1 β-gal homozygous mutant protein relative to WT levels of AMPA receptor subunits ( B ), NMDA receptor subunits ( C ), and PSD-93 and PSD-95 ( D ) in the PSD-enriched fractions. Data are the average of three independent biochemical fractionation experiments; each experiment used four to six mouse brains of each genotype. Error bars represent ±SEM.
    Rabbit Antibodies Against Syndig4, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+antibodies+against+syndig4/pmc05073248-72-54-61?v=Proteintech
    Average 92 stars, based on 1 article reviews
    rabbit antibodies against syndig4 - by Bioz Stars, 2026-07
    92/100 stars
      Buy from Supplier

    Image Search Results


    Synapse composition is unaltered in SynDIG1-deficient synapses. A , Representative immunoblots of biochemical fractions isolated from WT and SynDIG1 β-gal homozygous mutant P14 mouse brain tissue showing levels of GluA1, GluA2, GluN1, GluN2B, PSD-93, PSD-95, synaptophysin (Synapto), SynDIG1, SynDIG4, and PICK-1 present in the S1-, P2-, Syn-, and PSD-enriched fractions. Loading controls are provided by β-actin and β-tubulin immunoreactivity. B–D , Graphs depict the ratio of SynDIG1 β-gal homozygous mutant protein relative to WT levels of AMPA receptor subunits ( B ), NMDA receptor subunits ( C ), and PSD-93 and PSD-95 ( D ) in the PSD-enriched fractions. Data are the average of three independent biochemical fractionation experiments; each experiment used four to six mouse brains of each genotype. Error bars represent ±SEM.

    Journal: eNeuro

    Article Title: Loss of SynDIG1 Reduces Excitatory Synapse Maturation But Not Formation In Vivo

    doi: 10.1523/ENEURO.0130-16.2016

    Figure Lengend Snippet: Synapse composition is unaltered in SynDIG1-deficient synapses. A , Representative immunoblots of biochemical fractions isolated from WT and SynDIG1 β-gal homozygous mutant P14 mouse brain tissue showing levels of GluA1, GluA2, GluN1, GluN2B, PSD-93, PSD-95, synaptophysin (Synapto), SynDIG1, SynDIG4, and PICK-1 present in the S1-, P2-, Syn-, and PSD-enriched fractions. Loading controls are provided by β-actin and β-tubulin immunoreactivity. B–D , Graphs depict the ratio of SynDIG1 β-gal homozygous mutant protein relative to WT levels of AMPA receptor subunits ( B ), NMDA receptor subunits ( C ), and PSD-93 and PSD-95 ( D ) in the PSD-enriched fractions. Data are the average of three independent biochemical fractionation experiments; each experiment used four to six mouse brains of each genotype. Error bars represent ±SEM.

    Article Snippet: Membranes were blotted with the following primary antibodies: mouse antibodies against PSD-95 [catalog #75-028, NeuroMab (RRID:AB_2292909)], synaptophysin [catalog #101011, Synaptic Systems (RRID:AB_887824)], SynDIG1 [catalog #75-251, NeuroMab (RRID:AB_10999753)], GluA2 [catalog #75-002, NeuroMab (RRID:AB_2232661)], PSD-93 [catalog #75-057, NeuroMab (RRID:AB_2277296)], β-tubulin [catalog #05-661, Millipore (RRID:AB_309885)], GluN1 [catalog #556308, BD Biosciences (RRID:AB_396353)], and Pick1 [catalog #73-040, NeuroMab (RRID:AB_10672986)]; rabbit antibodies against SynDIG4 (Anti-Prrt1, catalog #17261-1-AP, ProteinTech), β-actin [catalog #ab8224, Abcam (RRID:AB_449644)], GluA1 [catalog #AB1504, Millipore (RRID:AB_2113602)], and GluN2B (provided by J.W.H.

    Techniques: Western Blot, Isolation, Mutagenesis, Fractionation