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anti eb3  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology anti eb3
    Anti Eb3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+eb3/CLIP-170+Antibody/pmc10469336__pnas__2301457120__sapp-197-26-34
    Average 93 stars, based on 52 article reviews
    anti eb3 - by Bioz Stars, 2026-10
    93/100 stars

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    Related Articles

    other:

    Article Title: Microtubule Targeting Agents Eribulin and Paclitaxel Differentially Affect Neuronal Cell Bodies in Chemotherapy Induced Peripheral Neuropathy
    Article Snippet: Primary antibodies used in this study include: Anti-βIII tubulin (abcam, ab107216, 1:1000 dilution)( Rinkevich et al. 2014 )), anti-ATF3 (C-19), (Santa Cruz SC-188, 1:1000 dilution, ( Carozzi et al. 2013 )), anti-α-tubulin (Millipore, 04-1117, 1:100 dilution ( Zhang et al. 2011 )), anti-acetylated tubulin(Cell Signal, 5335, 1:800 dilution, ( Creppe et al. 2009 )), anti-EB1 (Millipore, AB6057, 1:500 dilution, ( Vitre et al. 2008 )), anti-EB3 (Santa Cruz, SC-101475, 1:200 dilution, ( Levy et al. 1994 )) and anti-phosphoneurofilament (Covance, SMI-31R, 1:2000 dilution, ( Choi et al. 2008 )).

    Article Title: Phase separation of +TIP-networks regulates microtubule dynamics
    Article Snippet: The following day, unbound 846 antibodies were washed off with TBS-Tween 1%, and membranes were incubated with secondary 847 antibodies conjugated to horseradish peroxidase (anti-mouse or anti-rabbit; GE Healthcare 848 17097199 and 16951542, 1:5000 dilution) for 1 hour at room temperature.

    Incubation:

    Article Title: A liquid +TIP-network regulates microtubule dynamics through tubulin condensation
    Article Snippet: Cell lysates were boiled run on SDS-PAGE gels (10% acrylamide) and subsequently transferred to a nitrocellulose membrane using an iBLOT 2 Gel Transfer Device (ThermoFisher Scientific, IB21001). .. Nitrocellulose membranes were blocked for 1 h with 5 % dried milk resuspended in TBS-Tween 1 %, then incubated over-night with primary antibodies: anti-beta-tubulin (Sigma, T6074, 1:1000 dilution) anti-EB3 (ATLAS anti-MAPRE3, HPA-009263, 1:500 dilution), or anti-CLIP-170 (Santa Cruz Biotechnology, SC-28325, 1:1000 dilution). .. The following day, unbound antibodies were washed off with TBS-Tween 1%, and membranes were incubated with secondary antibodies conjugated to horseradish peroxidase (anti-mouse or anti-rabbit; GE Healthcare 17097199 and 16951542, 1:5000 dilution) for 1 hour at room temperature.

    Article Title:
    Article Snippet: Cell lysates were boiled run on SDS-PAGE gels (10% acrylamide) and subsequently transferred to a nitrocellulose membrane using an iBLOT 2 Gel Transfer Device (ThermoFisher Scientific, IB21001). .. Nitrocellulose membranes were blocked for 1 h with 5% dried milk resuspended in TBS-Tween 1%, then incubated over-night with primary antibodies: anti-beta-tubulin (Sigma, T6074, 1:1000 dilution) anti-EB3 (ATLAS anti-MAPRE3, HPA-009263, 1:500 dilution), or antiCLIP-170 (Santa Cruz Biotechnology, SC-28325, 1:1000 dilution). .. The following day, unbound antibodies were washed off with TBS-Tween 1%, and membranes were incubated with secondary antibodies conjugated to horseradish peroxidase (anti-mouse or anti-rabbit; GE Healthcare 17097199 and 16951542, 1:5000 dilution) for 1 hour at room temperature.

    Transcranial Magnetic Stimulation:

    Article Title:
    Article Snippet: Cell lysates were boiled run on SDS-PAGE gels (10% acrylamide) and subsequently transferred to a nitrocellulose membrane using an iBLOT 2 Gel Transfer Device (ThermoFisher Scientific, IB21001). .. Nitrocellulose membranes were blocked for 1 h with 5% dried milk resuspended in TBS-Tween 1%, then incubated over-night with primary antibodies: anti-beta-tubulin (Sigma, T6074, 1:1000 dilution) anti-EB3 (ATLAS anti-MAPRE3, HPA-009263, 1:500 dilution), or antiCLIP-170 (Santa Cruz Biotechnology, SC-28325, 1:1000 dilution). .. The following day, unbound antibodies were washed off with TBS-Tween 1%, and membranes were incubated with secondary antibodies conjugated to horseradish peroxidase (anti-mouse or anti-rabbit; GE Healthcare 17097199 and 16951542, 1:5000 dilution) for 1 hour at room temperature.



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    eb3  (Santa Cruz Biotechnology)
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    ADNP indirectly interacts with the histone deacetylase enzyme SIRT1 through the microtubule end-binding proteins <t>EB1/EB3.</t> ( A ) Adnp and Sirt1 immunostaining (red Cy3 fluorescence) in cryosections of the murine cerebellum was assessed by confocal scanning microscopy. Adnp was mainly observed in the nucleus and Sirt1 was mostly located in the cytoplasm. ( B ) Co-IP assay of Adnp and Sirt1 in the murine cerebellum. IP-competent EB1 and <t>EB3</t> antibodies were crosslinked to agarose beads and sequentially eluted in fractions (input, In; flow-through, Ft; three consecutive washes, w1-w3; and elution, E). All fractions were analyzed by western blotting for Adnp, Sirt1, EB1, and EB3. IgG non-reactive beads were used as a negative control. GAPDH has been used as loading control for all western blots, and critical assessment of the accuracy of the Co-IP method. ( C ) ELM analysis identified shared motif sequences of Adnp and Sirt, including 14–3–3 motifs (green), SxIP motif (blue), SH3 domains (orange), and the SSIP motif (violet). ( D ) In silico 3D-molecular docking of Adnp (SxIP motif) to EB1/3, left (purple) and right (pink) respectively to Sirt1 in the panel below (SSIP motif) to EB1/3, left (purple) and right (pink)
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    ADNP indirectly interacts with the histone deacetylase enzyme SIRT1 through the microtubule end-binding proteins <t>EB1/EB3.</t> ( A ) Adnp and Sirt1 immunostaining (red Cy3 fluorescence) in cryosections of the murine cerebellum was assessed by confocal scanning microscopy. Adnp was mainly observed in the nucleus and Sirt1 was mostly located in the cytoplasm. ( B ) Co-IP assay of Adnp and Sirt1 in the murine cerebellum. IP-competent EB1 and <t>EB3</t> antibodies were crosslinked to agarose beads and sequentially eluted in fractions (input, In; flow-through, Ft; three consecutive washes, w1-w3; and elution, E). All fractions were analyzed by western blotting for Adnp, Sirt1, EB1, and EB3. IgG non-reactive beads were used as a negative control. GAPDH has been used as loading control for all western blots, and critical assessment of the accuracy of the Co-IP method. ( C ) ELM analysis identified shared motif sequences of Adnp and Sirt, including 14–3–3 motifs (green), SxIP motif (blue), SH3 domains (orange), and the SSIP motif (violet). ( D ) In silico 3D-molecular docking of Adnp (SxIP motif) to EB1/3, left (purple) and right (pink) respectively to Sirt1 in the panel below (SSIP motif) to EB1/3, left (purple) and right (pink)
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    Image Search Results


    ADNP indirectly interacts with the histone deacetylase enzyme SIRT1 through the microtubule end-binding proteins EB1/EB3. ( A ) Adnp and Sirt1 immunostaining (red Cy3 fluorescence) in cryosections of the murine cerebellum was assessed by confocal scanning microscopy. Adnp was mainly observed in the nucleus and Sirt1 was mostly located in the cytoplasm. ( B ) Co-IP assay of Adnp and Sirt1 in the murine cerebellum. IP-competent EB1 and EB3 antibodies were crosslinked to agarose beads and sequentially eluted in fractions (input, In; flow-through, Ft; three consecutive washes, w1-w3; and elution, E). All fractions were analyzed by western blotting for Adnp, Sirt1, EB1, and EB3. IgG non-reactive beads were used as a negative control. GAPDH has been used as loading control for all western blots, and critical assessment of the accuracy of the Co-IP method. ( C ) ELM analysis identified shared motif sequences of Adnp and Sirt, including 14–3–3 motifs (green), SxIP motif (blue), SH3 domains (orange), and the SSIP motif (violet). ( D ) In silico 3D-molecular docking of Adnp (SxIP motif) to EB1/3, left (purple) and right (pink) respectively to Sirt1 in the panel below (SSIP motif) to EB1/3, left (purple) and right (pink)

    Journal: Acta Neuropathologica Communications

    Article Title: ADNP dysregulates methylation and mitochondrial gene expression in the cerebellum of a Helsmoortel–Van der Aa syndrome autopsy case

    doi: 10.1186/s40478-024-01743-w

    Figure Lengend Snippet: ADNP indirectly interacts with the histone deacetylase enzyme SIRT1 through the microtubule end-binding proteins EB1/EB3. ( A ) Adnp and Sirt1 immunostaining (red Cy3 fluorescence) in cryosections of the murine cerebellum was assessed by confocal scanning microscopy. Adnp was mainly observed in the nucleus and Sirt1 was mostly located in the cytoplasm. ( B ) Co-IP assay of Adnp and Sirt1 in the murine cerebellum. IP-competent EB1 and EB3 antibodies were crosslinked to agarose beads and sequentially eluted in fractions (input, In; flow-through, Ft; three consecutive washes, w1-w3; and elution, E). All fractions were analyzed by western blotting for Adnp, Sirt1, EB1, and EB3. IgG non-reactive beads were used as a negative control. GAPDH has been used as loading control for all western blots, and critical assessment of the accuracy of the Co-IP method. ( C ) ELM analysis identified shared motif sequences of Adnp and Sirt, including 14–3–3 motifs (green), SxIP motif (blue), SH3 domains (orange), and the SSIP motif (violet). ( D ) In silico 3D-molecular docking of Adnp (SxIP motif) to EB1/3, left (purple) and right (pink) respectively to Sirt1 in the panel below (SSIP motif) to EB1/3, left (purple) and right (pink)

    Article Snippet: The immunoprecipitated materials were subsequently investigated by immunoblotting using the following primary antibodies (Additional file : Table S2): rat monoclonal EB1 (Abcam; ab53358 ), rabbit monoclonal EB3 (Abcam; ab157217 ), rabbit monoclonal ADNP antibody (Abcam; ab300114 ) and SIRT1 (Abcam; ab189494 ).

    Techniques: Histone Deacetylase Assay, Binding Assay, Immunostaining, Fluorescence, Microscopy, Co-Immunoprecipitation Assay, Western Blot, Negative Control, In Silico