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Santa Cruz Biotechnology atpase alpha3
Atpase Alpha3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/atpase alpha3/product/Santa Cruz Biotechnology
Average 93 stars, based on 2 article reviews
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atpase alpha3 - by Bioz Stars, 2020-05
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Article Title: Clustering of Tau fibrils impairs the synaptic composition of α3‐Na+/K+‐ ATPase and AMPA receptors
Article Snippet: .. Then, the pre‐cleared extracts (0.25 mg initial total proteins) were incubated overnight at 4°C under gentle agitation in the presence of 1 μg of goat polyclonal anti‐Na+ /K+ ‐ATPase alpha3 (C‐16, Santa Cruz, # sc‐16052), rabbit polyclonal anti‐GluA2 (Synaptic Systems, # 182103), or rabbit polyclonal anti‐GluN1 (Synaptic Systems, #114011). .. As controls, the same amounts of extracts were incubated with 1 μg of pre‐immune goat or rabbit control IgGs (Santa Cruz, # sc‐2028 and # sc‐2027, respectively).

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  • 85
    Santa Cruz Biotechnology goat anti sodium potassium atpase α3 subunit
    Elimination of CRFR1 causes abnormal afferent fiber innervation Afferent fibers and their most distal endings were visualized using antibodies directed against sodium-potassium <t>ATPase</t> <t>α3</t> subunit (NKA, green). IHCs were immunolabeled using antibodies against myosin VI (red). (A–D) Whole-mount sections of cochlear middle turns were imaged in CRFR1 +/+ (A, B) and CRFR1 −/− (C, D) mice. (A, C) Significant differences in hair cell width (modiolar (m) to pillar (p) along the y axis) are evident. (B, D) Afferent fiber endings were found on all sides of the IHCs in CRFR1 +/+ mice, and were decorated with immunoreactive puncta that outlined the termination of the fibers (arrows). These fibers appeared stunted in CRFR1 −/− mice, with few endings reaching toward the pillar side of the inner hair cell (above dashed line, arrows), and none exhibiting the immunoreactive puncta observed in (B). (E–G) An abnormal cluster of fibers was found on the modiolar side of the IHCs of CRFR1 −/− mice (F, dashed box) that is not present in CRFR1 +/+ mice (E). YZ projections highlight this abnormal clustering in CRFR1 −/− mice (G, boxed region). (H, I) YZ projections also revealed reduced innervation on the pillar surface of the IHC in CRFR1 −/− mice (I) compared to CRFR1 +/+ mice (H) (dashed ovals).
    Goat Anti Sodium Potassium Atpase α3 Subunit, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti sodium potassium atpase α3 subunit/product/Santa Cruz Biotechnology
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti sodium potassium atpase α3 subunit - by Bioz Stars, 2020-05
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    90
    Santa Cruz Biotechnology k atpase α3 monoclonal antibody
    Effect of arenobufagin (Arg) on Na, <t>K-ATPase</t> activity, intracellular Ca(2+) level and ROS level. ( A ) Quantitation of Na, K-ATPase activity in HeLa cells treated with arenobufagin(Arg) at different doses for 24h. (B) Western blotting results of Na, K-ATPase α1 and <t>α3</t> in HeLa cells treated with arenobufagin(Arg) at different doses for 24 h. ( C ) Quantitation of the intracellular Ca(2+) level in HeLa cells treated with 10 nM arenobufagin for different time periods. ( D ) Quantitation of the intracellular ROS level in HeLa cells treated with 10 nM arenobufagin for different time periods. ( E ) Quantitation of the intracellular ROS level in HeLa cells treated with arenobufagin at different doses for 3h. (F) The viability of HeLa cells treated with 10 nM arenobufagin for 72 h in the presence of ROS scavenger NAC (N-acetyl cysteine). Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P
    K Atpase α3 Monoclonal Antibody, supplied by Santa Cruz Biotechnology, 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/result/k atpase α3 monoclonal antibody/product/Santa Cruz Biotechnology
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    k atpase α3 monoclonal antibody - by Bioz Stars, 2020-05
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    86
    Santa Cruz Biotechnology na k atpase α3 subunit
    Identification of the functional role of Na + /K + <t>-ATPase</t> α 3 subunit. (A) The expression of Na + /K + -ATPase α 3 subunit was detected using Western blot analysis. The anti-proliferative IC 50 values were determined using SRB assays except for
    Na K Atpase α3 Subunit, supplied by Santa Cruz Biotechnology, 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/na k atpase α3 subunit/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    na k atpase α3 subunit - by Bioz Stars, 2020-05
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    90
    Santa Cruz Biotechnology goat anti na k atpase α3
    Visualizing IHC synapses in confocal z-stacks from immunostained cochlear whole mounts, acquired in the x - y plane ( A ) and re-projected into y - z ( B ) plane. A Pre- and post-synaptic elements in the IHC area are counted in cochlear whole mounts quadruple-immunostained for CtBP2 ( red ), GluA2 ( green ), <t>Na-K</t> <t>ATPase</t> ( blue ), and myosin VIIa ( white ). White arrows indicate several synapses, i.e., closely juxtaposed red and green puncta ; red-filled arrows indicate several terminal swellings of cochlear nerve fibers. B The size gradients in pre- and post-synaptic elements are quantified by defining a new set of axes in the y - z plane designed to (1) minimize the habenular-cuticular spread of synaptic distances from new modiolar-pillar axis while (2) keeping the new origin as close to the IHC midline as possible. This maximum projection in the y - z plane is from the same z -stack shown in the acquisition ( x - y ) plane in panel A .
    Goat Anti Na K Atpase α3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti na k atpase α3/product/Santa Cruz Biotechnology
    Average 90 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    goat anti na k atpase α3 - by Bioz Stars, 2020-05
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    Image Search Results


    Elimination of CRFR1 causes abnormal afferent fiber innervation Afferent fibers and their most distal endings were visualized using antibodies directed against sodium-potassium ATPase α3 subunit (NKA, green). IHCs were immunolabeled using antibodies against myosin VI (red). (A–D) Whole-mount sections of cochlear middle turns were imaged in CRFR1 +/+ (A, B) and CRFR1 −/− (C, D) mice. (A, C) Significant differences in hair cell width (modiolar (m) to pillar (p) along the y axis) are evident. (B, D) Afferent fiber endings were found on all sides of the IHCs in CRFR1 +/+ mice, and were decorated with immunoreactive puncta that outlined the termination of the fibers (arrows). These fibers appeared stunted in CRFR1 −/− mice, with few endings reaching toward the pillar side of the inner hair cell (above dashed line, arrows), and none exhibiting the immunoreactive puncta observed in (B). (E–G) An abnormal cluster of fibers was found on the modiolar side of the IHCs of CRFR1 −/− mice (F, dashed box) that is not present in CRFR1 +/+ mice (E). YZ projections highlight this abnormal clustering in CRFR1 −/− mice (G, boxed region). (H, I) YZ projections also revealed reduced innervation on the pillar surface of the IHC in CRFR1 −/− mice (I) compared to CRFR1 +/+ mice (H) (dashed ovals).

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: The mouse cochlea expresses a local hypothalamic-pituitary-adrenal equivalent signaling system and requires CRFR1 to establish normal hair cell innervation and cochlear sensitivity

    doi: 10.1523/JNEUROSCI.4545-10.2011

    Figure Lengend Snippet: Elimination of CRFR1 causes abnormal afferent fiber innervation Afferent fibers and their most distal endings were visualized using antibodies directed against sodium-potassium ATPase α3 subunit (NKA, green). IHCs were immunolabeled using antibodies against myosin VI (red). (A–D) Whole-mount sections of cochlear middle turns were imaged in CRFR1 +/+ (A, B) and CRFR1 −/− (C, D) mice. (A, C) Significant differences in hair cell width (modiolar (m) to pillar (p) along the y axis) are evident. (B, D) Afferent fiber endings were found on all sides of the IHCs in CRFR1 +/+ mice, and were decorated with immunoreactive puncta that outlined the termination of the fibers (arrows). These fibers appeared stunted in CRFR1 −/− mice, with few endings reaching toward the pillar side of the inner hair cell (above dashed line, arrows), and none exhibiting the immunoreactive puncta observed in (B). (E–G) An abnormal cluster of fibers was found on the modiolar side of the IHCs of CRFR1 −/− mice (F, dashed box) that is not present in CRFR1 +/+ mice (E). YZ projections highlight this abnormal clustering in CRFR1 −/− mice (G, boxed region). (H, I) YZ projections also revealed reduced innervation on the pillar surface of the IHC in CRFR1 −/− mice (I) compared to CRFR1 +/+ mice (H) (dashed ovals).

    Article Snippet: Immunofluorescence labeling was performed using goat anti-sodium-potassium ATPase α3 subunit (Santa Cruz, 1:100) in 1% normal donkey serum and 0.1% Triton X-100 at room temperature overnight.

    Techniques: Immunolabeling, Mouse Assay, Immunohistochemistry

    Effect of arenobufagin (Arg) on Na, K-ATPase activity, intracellular Ca(2+) level and ROS level. ( A ) Quantitation of Na, K-ATPase activity in HeLa cells treated with arenobufagin(Arg) at different doses for 24h. (B) Western blotting results of Na, K-ATPase α1 and α3 in HeLa cells treated with arenobufagin(Arg) at different doses for 24 h. ( C ) Quantitation of the intracellular Ca(2+) level in HeLa cells treated with 10 nM arenobufagin for different time periods. ( D ) Quantitation of the intracellular ROS level in HeLa cells treated with 10 nM arenobufagin for different time periods. ( E ) Quantitation of the intracellular ROS level in HeLa cells treated with arenobufagin at different doses for 3h. (F) The viability of HeLa cells treated with 10 nM arenobufagin for 72 h in the presence of ROS scavenger NAC (N-acetyl cysteine). Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P

    Journal: PLoS ONE

    Article Title: Proteasome Inhibition Contributed to the Cytotoxicity of Arenobufagin after Its Binding with Na, K-ATPase in Human Cervical Carcinoma HeLa Cells

    doi: 10.1371/journal.pone.0159034

    Figure Lengend Snippet: Effect of arenobufagin (Arg) on Na, K-ATPase activity, intracellular Ca(2+) level and ROS level. ( A ) Quantitation of Na, K-ATPase activity in HeLa cells treated with arenobufagin(Arg) at different doses for 24h. (B) Western blotting results of Na, K-ATPase α1 and α3 in HeLa cells treated with arenobufagin(Arg) at different doses for 24 h. ( C ) Quantitation of the intracellular Ca(2+) level in HeLa cells treated with 10 nM arenobufagin for different time periods. ( D ) Quantitation of the intracellular ROS level in HeLa cells treated with 10 nM arenobufagin for different time periods. ( E ) Quantitation of the intracellular ROS level in HeLa cells treated with arenobufagin at different doses for 3h. (F) The viability of HeLa cells treated with 10 nM arenobufagin for 72 h in the presence of ROS scavenger NAC (N-acetyl cysteine). Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P

    Article Snippet: The primary antibodies used in the present study were mouse anti-Na, K-ATPase α1 monoclonal antibody (1:200, Santa Cruz Biotechnology), mouse anti-Na, K-ATPase α3 monoclonal antibody (1:200, Santa Cruz Biotechnology), mouse anti-WEE1 monoclonal antibody (1:500, Abnova, Taipei City, Taiwan), mouse anti-GAPDH monoclonal antibody(1:2000, Sigma) and mouse anti-actin monoclonal antibody (1:2000, Sigma).

    Techniques: Activity Assay, Quantitation Assay, Western Blot

    Ataxin-1 and translationally-controlled tumor protein might be intermediate proteins between Na, K-ATPase and proteasome. ( A ) Protein-protein interaction network constructed to connect α1, α2 or α3 subunits of Na,K-ATPase and proteasomal-related proteins found in the proteomic study. The red dots were α1, α2 or α3 subunits of Na,K-ATPase and the yellow dots were 5 proteasomal-related proteins found in the proteomic study. The intermediate partner proteins except ataxin-1 and translationally-controlled tumor protein were shown in black. Ataxin-1 and translationally-controlled tumor protein (shown in blue) were considered as the most important intermediate partners between Na,K-ATPase and proteasome. ( B ) The protein expression level of ataxin-1 in control HeLa cells or cells treated with arenobufagin at different doses for 24 h. ( C ) The protein expression level of translationally-controlled tumor protein in control HeLa cells or cells treated with arenobufagin at different doses for 24 h. Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P

    Journal: PLoS ONE

    Article Title: Proteasome Inhibition Contributed to the Cytotoxicity of Arenobufagin after Its Binding with Na, K-ATPase in Human Cervical Carcinoma HeLa Cells

    doi: 10.1371/journal.pone.0159034

    Figure Lengend Snippet: Ataxin-1 and translationally-controlled tumor protein might be intermediate proteins between Na, K-ATPase and proteasome. ( A ) Protein-protein interaction network constructed to connect α1, α2 or α3 subunits of Na,K-ATPase and proteasomal-related proteins found in the proteomic study. The red dots were α1, α2 or α3 subunits of Na,K-ATPase and the yellow dots were 5 proteasomal-related proteins found in the proteomic study. The intermediate partner proteins except ataxin-1 and translationally-controlled tumor protein were shown in black. Ataxin-1 and translationally-controlled tumor protein (shown in blue) were considered as the most important intermediate partners between Na,K-ATPase and proteasome. ( B ) The protein expression level of ataxin-1 in control HeLa cells or cells treated with arenobufagin at different doses for 24 h. ( C ) The protein expression level of translationally-controlled tumor protein in control HeLa cells or cells treated with arenobufagin at different doses for 24 h. Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P

    Article Snippet: The primary antibodies used in the present study were mouse anti-Na, K-ATPase α1 monoclonal antibody (1:200, Santa Cruz Biotechnology), mouse anti-Na, K-ATPase α3 monoclonal antibody (1:200, Santa Cruz Biotechnology), mouse anti-WEE1 monoclonal antibody (1:500, Abnova, Taipei City, Taiwan), mouse anti-GAPDH monoclonal antibody(1:2000, Sigma) and mouse anti-actin monoclonal antibody (1:2000, Sigma).

    Techniques: Construct, Expressing

    Cellular proteasomal activity was inhibited by arenobufagin, which might be related to the binding of Na, K-ATPase. (A ) Inhibition of arenobufagin (Arg) at different doses on cytosolic proteasomal activity for 24h. ( B ) Three types of cellular proteasome enzyme activities (C-L, T-L and CT-L) in HeLa cells treated with 0.1% DMSO or arenobufagin(Arg) at different concentrations for 24h. ( C ) Western blotting results of WEE1 and actin in control HeLa cells and cells treated with 10 nM arenobufagin for 24 h and 48 h. Each blot was the representative result of three independent experiments. ( D ) Inhibition of antibodies against α1 or α3 subunits of Na,K-ATPase or combination of antibodies against α1 or α3 subunits of Na,K-ATPase and 10 nM arenobufagin on cytosolic proteasomal activity for 24h,48h and 72h, respectively. Data were statistical results of three independent experiments. Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P

    Journal: PLoS ONE

    Article Title: Proteasome Inhibition Contributed to the Cytotoxicity of Arenobufagin after Its Binding with Na, K-ATPase in Human Cervical Carcinoma HeLa Cells

    doi: 10.1371/journal.pone.0159034

    Figure Lengend Snippet: Cellular proteasomal activity was inhibited by arenobufagin, which might be related to the binding of Na, K-ATPase. (A ) Inhibition of arenobufagin (Arg) at different doses on cytosolic proteasomal activity for 24h. ( B ) Three types of cellular proteasome enzyme activities (C-L, T-L and CT-L) in HeLa cells treated with 0.1% DMSO or arenobufagin(Arg) at different concentrations for 24h. ( C ) Western blotting results of WEE1 and actin in control HeLa cells and cells treated with 10 nM arenobufagin for 24 h and 48 h. Each blot was the representative result of three independent experiments. ( D ) Inhibition of antibodies against α1 or α3 subunits of Na,K-ATPase or combination of antibodies against α1 or α3 subunits of Na,K-ATPase and 10 nM arenobufagin on cytosolic proteasomal activity for 24h,48h and 72h, respectively. Data were statistical results of three independent experiments. Data were statistical results of three independent experiments. Data were expressed as mean ± SD. *Significant difference from the control group at P

    Article Snippet: The primary antibodies used in the present study were mouse anti-Na, K-ATPase α1 monoclonal antibody (1:200, Santa Cruz Biotechnology), mouse anti-Na, K-ATPase α3 monoclonal antibody (1:200, Santa Cruz Biotechnology), mouse anti-WEE1 monoclonal antibody (1:500, Abnova, Taipei City, Taiwan), mouse anti-GAPDH monoclonal antibody(1:2000, Sigma) and mouse anti-actin monoclonal antibody (1:2000, Sigma).

    Techniques: Activity Assay, Binding Assay, Inhibition, Western Blot

    Identification of the functional role of Na + /K + -ATPase α 3 subunit. (A) The expression of Na + /K + -ATPase α 3 subunit was detected using Western blot analysis. The anti-proliferative IC 50 values were determined using SRB assays except for

    Journal: Biochemical pharmacology

    Article Title: Reevesioside F induces potent and efficient anti-proliferative and apoptotic activities through Na+/K+-ATPase α3 subunit-involved mitochondrial stress and amplification of caspase cascades

    doi: 10.1016/j.bcp.2013.09.021

    Figure Lengend Snippet: Identification of the functional role of Na + /K + -ATPase α 3 subunit. (A) The expression of Na + /K + -ATPase α 3 subunit was detected using Western blot analysis. The anti-proliferative IC 50 values were determined using SRB assays except for

    Article Snippet: Antibodies to GAPDH, Na+ /K+ -ATPase α3 subunit, Bcl-2, Bid, Bak, Bax, Mcl-1, Noxa, Bim, cytochrome c and anti-mouse and anti-rabbit IgGs were obtained from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA).

    Techniques: Functional Assay, Expressing, Western Blot, Sulforhodamine B Assay

    Visualizing IHC synapses in confocal z-stacks from immunostained cochlear whole mounts, acquired in the x - y plane ( A ) and re-projected into y - z ( B ) plane. A Pre- and post-synaptic elements in the IHC area are counted in cochlear whole mounts quadruple-immunostained for CtBP2 ( red ), GluA2 ( green ), Na-K ATPase ( blue ), and myosin VIIa ( white ). White arrows indicate several synapses, i.e., closely juxtaposed red and green puncta ; red-filled arrows indicate several terminal swellings of cochlear nerve fibers. B The size gradients in pre- and post-synaptic elements are quantified by defining a new set of axes in the y - z plane designed to (1) minimize the habenular-cuticular spread of synaptic distances from new modiolar-pillar axis while (2) keeping the new origin as close to the IHC midline as possible. This maximum projection in the y - z plane is from the same z -stack shown in the acquisition ( x - y ) plane in panel A .

    Journal: JARO: Journal of the Association for Research in Otolaryngology

    Article Title: Dynamics of cochlear synaptopathy after acoustic overexposure

    doi: 10.1007/s10162-015-0510-3

    Figure Lengend Snippet: Visualizing IHC synapses in confocal z-stacks from immunostained cochlear whole mounts, acquired in the x - y plane ( A ) and re-projected into y - z ( B ) plane. A Pre- and post-synaptic elements in the IHC area are counted in cochlear whole mounts quadruple-immunostained for CtBP2 ( red ), GluA2 ( green ), Na-K ATPase ( blue ), and myosin VIIa ( white ). White arrows indicate several synapses, i.e., closely juxtaposed red and green puncta ; red-filled arrows indicate several terminal swellings of cochlear nerve fibers. B The size gradients in pre- and post-synaptic elements are quantified by defining a new set of axes in the y - z plane designed to (1) minimize the habenular-cuticular spread of synaptic distances from new modiolar-pillar axis while (2) keeping the new origin as close to the IHC midline as possible. This maximum projection in the y - z plane is from the same z -stack shown in the acquisition ( x - y ) plane in panel A .

    Article Snippet: Immunostaining began with a blocking buffer (PBS with 5 % normal horse serum and 0.3–1 % Triton X-100) for 1 h at room temperature and followed by overnight incubation at 37 °C with some combination of the following primary antibodies: (1) mouse (IgG1) anti-CtBP2 (C-terminal Binding Protein) from BD Biosciences at 1:200, to quantify pre-synaptic ribbons; (2) mouse (IgG2a) anti-GluA2 (Glutamate receptor subunit A2) from Millipore at 1:2000, to quantify post-synaptic receptor patches; (3) goat anti-Na-K ATPase α3 from Santa Cruz at 1:100 to label dendrites of cochlear nerve fibers; and (4) rabbit anti-Myosin VIIa from Proteus Biosciences at 1:200 to delineate the inner hair cell cytoplasm.

    Techniques: Immunohistochemistry