atpase assays  (Millipore)


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    Structured Review

    Millipore atpase assays
    ( A ) Esf2 stimulates Dbp8 ATP hydrolysis activity in vitro . A total of 10 <t>pmol</t> of Dbp8 was incubated with various amounts of GST-Esf2 or GST-Rpa34 (0–1.5 M excess over Dbp8, X -axis) in buffers containing 200 mM KCl, for 25 min on ice to allow complex formation to occur. ATP was then added to the reaction and ATP hydrolysis ( Y -axis) was measured after 30 min of incubation at 30°C. Plotted are the averages and standard errors that were derived from three independent experiments. ( B ) Esf2-mediated stimulation of Dbp8 <t>ATPase</t> activity is optimal at lower potassium chloride concentrations. ATP hydrolysis assays were performed using 5 pmol of recombinant Dbp8 and GST-Esf2 and varying salt concentrations (50–450 mM KCl). ATP hydrolysis was measured after 30 min of incubation at 30°C. Plotted are the averages and standard errors that were derived from three independent experiments. To determine if under these conditions GST-Esf2 and Dbp8 still form a complex, 300 pmols of each protein were incubated under the same conditions used for the ATP hydrolysis assay. Protein complexes were precipitated using Ni-NTA beads, resolved by SDS–PAGE and stained with Coomassie brilliant blue [Figure embedded in the graph shown in (B)]. ( C ) Dbp8 binding to Esf2 increases Dbp8 affinity for ATP and increases the ATP turnover rate. ATP hydrolysis assays were performed using 5 pmols of Dbp8 in the presence or absence of equimolar amounts of Esf2 in 50 mM KCl and various ATP concentrations. The initial velocities, plotted on the Y -axis, were determined by measuring the amount of ATP hydrolysis (µM) during a 3 min period (data not shown) in the presence of various [ATP] (10, 50, 100, 250 and 500 µM). The data were fitted to the Michaelis–Menten equation from which the K M and k cat were determined. Plotted are the averages derived from two independent experiments.
    Atpase Assays, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis"

    Article Title: The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkl419

    ( A ) Esf2 stimulates Dbp8 ATP hydrolysis activity in vitro . A total of 10 pmol of Dbp8 was incubated with various amounts of GST-Esf2 or GST-Rpa34 (0–1.5 M excess over Dbp8, X -axis) in buffers containing 200 mM KCl, for 25 min on ice to allow complex formation to occur. ATP was then added to the reaction and ATP hydrolysis ( Y -axis) was measured after 30 min of incubation at 30°C. Plotted are the averages and standard errors that were derived from three independent experiments. ( B ) Esf2-mediated stimulation of Dbp8 ATPase activity is optimal at lower potassium chloride concentrations. ATP hydrolysis assays were performed using 5 pmol of recombinant Dbp8 and GST-Esf2 and varying salt concentrations (50–450 mM KCl). ATP hydrolysis was measured after 30 min of incubation at 30°C. Plotted are the averages and standard errors that were derived from three independent experiments. To determine if under these conditions GST-Esf2 and Dbp8 still form a complex, 300 pmols of each protein were incubated under the same conditions used for the ATP hydrolysis assay. Protein complexes were precipitated using Ni-NTA beads, resolved by SDS–PAGE and stained with Coomassie brilliant blue [Figure embedded in the graph shown in (B)]. ( C ) Dbp8 binding to Esf2 increases Dbp8 affinity for ATP and increases the ATP turnover rate. ATP hydrolysis assays were performed using 5 pmols of Dbp8 in the presence or absence of equimolar amounts of Esf2 in 50 mM KCl and various ATP concentrations. The initial velocities, plotted on the Y -axis, were determined by measuring the amount of ATP hydrolysis (µM) during a 3 min period (data not shown) in the presence of various [ATP] (10, 50, 100, 250 and 500 µM). The data were fitted to the Michaelis–Menten equation from which the K M and k cat were determined. Plotted are the averages derived from two independent experiments.
    Figure Legend Snippet: ( A ) Esf2 stimulates Dbp8 ATP hydrolysis activity in vitro . A total of 10 pmol of Dbp8 was incubated with various amounts of GST-Esf2 or GST-Rpa34 (0–1.5 M excess over Dbp8, X -axis) in buffers containing 200 mM KCl, for 25 min on ice to allow complex formation to occur. ATP was then added to the reaction and ATP hydrolysis ( Y -axis) was measured after 30 min of incubation at 30°C. Plotted are the averages and standard errors that were derived from three independent experiments. ( B ) Esf2-mediated stimulation of Dbp8 ATPase activity is optimal at lower potassium chloride concentrations. ATP hydrolysis assays were performed using 5 pmol of recombinant Dbp8 and GST-Esf2 and varying salt concentrations (50–450 mM KCl). ATP hydrolysis was measured after 30 min of incubation at 30°C. Plotted are the averages and standard errors that were derived from three independent experiments. To determine if under these conditions GST-Esf2 and Dbp8 still form a complex, 300 pmols of each protein were incubated under the same conditions used for the ATP hydrolysis assay. Protein complexes were precipitated using Ni-NTA beads, resolved by SDS–PAGE and stained with Coomassie brilliant blue [Figure embedded in the graph shown in (B)]. ( C ) Dbp8 binding to Esf2 increases Dbp8 affinity for ATP and increases the ATP turnover rate. ATP hydrolysis assays were performed using 5 pmols of Dbp8 in the presence or absence of equimolar amounts of Esf2 in 50 mM KCl and various ATP concentrations. The initial velocities, plotted on the Y -axis, were determined by measuring the amount of ATP hydrolysis (µM) during a 3 min period (data not shown) in the presence of various [ATP] (10, 50, 100, 250 and 500 µM). The data were fitted to the Michaelis–Menten equation from which the K M and k cat were determined. Plotted are the averages derived from two independent experiments.

    Techniques Used: Activity Assay, In Vitro, Incubation, Derivative Assay, Recombinant, Hydrolysis Assay, SDS Page, Staining, Binding Assay

    The essential C-terminal domain of Esf2 is required for binding to Dbp8 and stimulating its ATPase activity in vitro . ( A ) Schematic representation of the Esf2 wild-type (WT) and deletion mutants (ΔN, ΔC and ΔRRM) that were tested in the yeast two-hybrid screen for their association with Dbp8. The predicted RRM motif and coiled-coil domains are represented as boxes. The amino acid positions relevant to the deletions made are indicated. ( B ) The C-terminal domain of Esf2 is required for Dbp8 interaction in the yeast 2-hybrid assay. The yeast 2-hybrid host strain carrying either the Esf2 wild-type or Esf2 deletion mutants (bait) in combination with either Dbp8 (prey) or empty prey vector were serial diluted and tested for growth on permissive (+His) or selective media (His selection). ( C ) The C-terminal domain of Esf2 is required for stimulation of Dbp8 ATPase activity in vitro . ATP hydrolysis experiments were performed with 10 µM ATP, 5 pmol of Dbp8 and 50 mM KCl, in the presence or absence (Dbp8 alone) of 5 pmols of GST-Esf2 wild-type (WT) or GST-Esf2 ΔC. ATP hydrolysis (plotted on the Y -axis) was measured after 30 min incubation at 30°C. Graphed are the averages and standard errors derived from three independent experiments. ( D ) The C-terminal domain of Esf2 is essential for function in vivo . Serial dilutions (10-fold) of GAL::3HA-ESF2 strains carrying the empty vector or, p415GPD- ESF2 wild-type and mutant alleles (ΔN, ΔRRM and ΔC) were grown in synthetic galactose media (SG/R-LEU) and spotted on either galactose containing plates (left panel; SG/R-LEU) or galactose containing plates (right panel; SD-LEU).
    Figure Legend Snippet: The essential C-terminal domain of Esf2 is required for binding to Dbp8 and stimulating its ATPase activity in vitro . ( A ) Schematic representation of the Esf2 wild-type (WT) and deletion mutants (ΔN, ΔC and ΔRRM) that were tested in the yeast two-hybrid screen for their association with Dbp8. The predicted RRM motif and coiled-coil domains are represented as boxes. The amino acid positions relevant to the deletions made are indicated. ( B ) The C-terminal domain of Esf2 is required for Dbp8 interaction in the yeast 2-hybrid assay. The yeast 2-hybrid host strain carrying either the Esf2 wild-type or Esf2 deletion mutants (bait) in combination with either Dbp8 (prey) or empty prey vector were serial diluted and tested for growth on permissive (+His) or selective media (His selection). ( C ) The C-terminal domain of Esf2 is required for stimulation of Dbp8 ATPase activity in vitro . ATP hydrolysis experiments were performed with 10 µM ATP, 5 pmol of Dbp8 and 50 mM KCl, in the presence or absence (Dbp8 alone) of 5 pmols of GST-Esf2 wild-type (WT) or GST-Esf2 ΔC. ATP hydrolysis (plotted on the Y -axis) was measured after 30 min incubation at 30°C. Graphed are the averages and standard errors derived from three independent experiments. ( D ) The C-terminal domain of Esf2 is essential for function in vivo . Serial dilutions (10-fold) of GAL::3HA-ESF2 strains carrying the empty vector or, p415GPD- ESF2 wild-type and mutant alleles (ΔN, ΔRRM and ΔC) were grown in synthetic galactose media (SG/R-LEU) and spotted on either galactose containing plates (left panel; SG/R-LEU) or galactose containing plates (right panel; SD-LEU).

    Techniques Used: Binding Assay, Activity Assay, In Vitro, Two Hybrid Screening, Y2H Assay, Plasmid Preparation, Selection, Incubation, Derivative Assay, In Vivo, Mutagenesis

    Pre-rRNA fragments stimulate Dbp8 ATPase activity in vitro . ( A ) In vitro transcribed fragments of the 5′ETS rRNA stimulate Dbp8 ATP hydrolysis in the presence of Esf2. ATP hydrolysis assays were carried out with 10 µM ATP, 10 pmol of Dbp8 and 10 pmol of Esf2, 1 µg/µl of total yeast RNA, 0.8 µM of ribosomal RNAs (schematically outlined on top of the graph) and 50 mM KCl. Samples were incubated at 30°C for 30 min. Plotted are the averages and standard errors derived from three independent experiments. ( B ) In vitro transcribed 5′ETS rRNA fragments stimulate Dbp8 ATP hydrolysis in the absence of Esf2. ATP hydrolysis experiments were performed with 10 µM ATP, 5 pmol of Dbp8 and 50 mM KCl, in the presence or absence of equimolar amounts of Esf2 and various amounts of 5′ETS rRNA (0–360 fragment; plotted on the X -axis). ATP hydrolysis (plotted on the Y -axis) was measured after 30 min incubation at 30°C. Plotted are the averages and standard errors derived from three independent experiments.
    Figure Legend Snippet: Pre-rRNA fragments stimulate Dbp8 ATPase activity in vitro . ( A ) In vitro transcribed fragments of the 5′ETS rRNA stimulate Dbp8 ATP hydrolysis in the presence of Esf2. ATP hydrolysis assays were carried out with 10 µM ATP, 10 pmol of Dbp8 and 10 pmol of Esf2, 1 µg/µl of total yeast RNA, 0.8 µM of ribosomal RNAs (schematically outlined on top of the graph) and 50 mM KCl. Samples were incubated at 30°C for 30 min. Plotted are the averages and standard errors derived from three independent experiments. ( B ) In vitro transcribed 5′ETS rRNA fragments stimulate Dbp8 ATP hydrolysis in the absence of Esf2. ATP hydrolysis experiments were performed with 10 µM ATP, 5 pmol of Dbp8 and 50 mM KCl, in the presence or absence of equimolar amounts of Esf2 and various amounts of 5′ETS rRNA (0–360 fragment; plotted on the X -axis). ATP hydrolysis (plotted on the Y -axis) was measured after 30 min incubation at 30°C. Plotted are the averages and standard errors derived from three independent experiments.

    Techniques Used: Activity Assay, In Vitro, Incubation, Derivative Assay

    2) Product Images from "MORC2 regulates DNA damage response through a PARP1-dependent pathway"

    Article Title: MORC2 regulates DNA damage response through a PARP1-dependent pathway

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkz545

    PARP1 recruits MORC2 to DNA damage sites and PARylation of MORC2 stimulates its chromatin remodeling activities. ( A ) Reconstitution of MORC2 KO MCF-7 cells with Flag-MORC2 and Flag-MORC2–2A by lentiviral infection. Expression status of exogenous and endogenous MORC2 was validated by immunoblotting. ( B ) MCF-7 KO cells stably expressing pCDH, Flag-MORC2 and Flag-MORC2–2A were treated with or without 1 mM MMS for 30 min, and then subjected to in vivo PLA assays with indicated antibodies. Three independent experiments were performed, and total 50 cells were counted for each experiment. ( C ) MCF-7 KO cells stably expressing Flag-MORC2 and Flag-MORC2–2A were treated with or without 1 mM MMS for 30 min, and subjected to cellular fractionation as described in ‘Materials and Methods’ section. Chromatin-bound fractions and total cellular lysates from undamaged and DNA damaged cells were immunoblotted with the indicated antibodies. ( D ) MCF-7 KO cells stably expressing Flag-MORC2 and Flag-MORC2–2A were treated with or without 1 mM MMS for 30 min. Immunoprecipitated Flag-MORC2 or Flag-MORC2–2A was subjected to ATPase assays using the ATPase/GTPase Activity Assay Kit (Sigma). Data represent mean ± s.d. from three biologically independent experiments. ( E ) MCF-7 KO cells stably expressing pCDH, Flag-MORC2 and Flag-MORC2–5A were treated with or without 1 mM MMS for 30 min. Isolated nuclei were subjected to MNase assays as described in ‘Materials and Methods’ section. ( F and G ) MCF-7 KO cells stably expressing pCDH, Flag-MORC2 and Flag-MORC2–2A were treated with or without increasing doses of MMS for 2 weeks. The representative images of Crystal Violet-stained colonies are shown in F. Quantitative results (G) are represented as mean ± s.d. as indicated from three independent experiments; *, P
    Figure Legend Snippet: PARP1 recruits MORC2 to DNA damage sites and PARylation of MORC2 stimulates its chromatin remodeling activities. ( A ) Reconstitution of MORC2 KO MCF-7 cells with Flag-MORC2 and Flag-MORC2–2A by lentiviral infection. Expression status of exogenous and endogenous MORC2 was validated by immunoblotting. ( B ) MCF-7 KO cells stably expressing pCDH, Flag-MORC2 and Flag-MORC2–2A were treated with or without 1 mM MMS for 30 min, and then subjected to in vivo PLA assays with indicated antibodies. Three independent experiments were performed, and total 50 cells were counted for each experiment. ( C ) MCF-7 KO cells stably expressing Flag-MORC2 and Flag-MORC2–2A were treated with or without 1 mM MMS for 30 min, and subjected to cellular fractionation as described in ‘Materials and Methods’ section. Chromatin-bound fractions and total cellular lysates from undamaged and DNA damaged cells were immunoblotted with the indicated antibodies. ( D ) MCF-7 KO cells stably expressing Flag-MORC2 and Flag-MORC2–2A were treated with or without 1 mM MMS for 30 min. Immunoprecipitated Flag-MORC2 or Flag-MORC2–2A was subjected to ATPase assays using the ATPase/GTPase Activity Assay Kit (Sigma). Data represent mean ± s.d. from three biologically independent experiments. ( E ) MCF-7 KO cells stably expressing pCDH, Flag-MORC2 and Flag-MORC2–5A were treated with or without 1 mM MMS for 30 min. Isolated nuclei were subjected to MNase assays as described in ‘Materials and Methods’ section. ( F and G ) MCF-7 KO cells stably expressing pCDH, Flag-MORC2 and Flag-MORC2–2A were treated with or without increasing doses of MMS for 2 weeks. The representative images of Crystal Violet-stained colonies are shown in F. Quantitative results (G) are represented as mean ± s.d. as indicated from three independent experiments; *, P

    Techniques Used: Infection, Expressing, Stable Transfection, In Vivo, Proximity Ligation Assay, Cell Fractionation, Immunoprecipitation, Activity Assay, Isolation, Staining

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    Staining:

    Article Title: Polarized retinal pigment epithelium generates electrical signals that diminish with age and regulate retinal pathology, et al. Polarized retinal pigment epithelium generates electrical signals that diminish with age and regulate retinal pathology
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    Article Title: Endogenous bioelectric currents promote differentiation of the mammalian lens. Endogenous bioelectric currents promote differentiation of the mammalian lens
    Article Snippet: .. The cells were stained for 2 hr with antibodies to α‐ and β‐subunit of Na+ /K+ ‐ATPase (EMD Millipore, Watford, UK), α and β‐crystallin (BD Biosciences, Oxford, UK), respectively and then were incubated with secondary antibodies (Invitrogen) and phalloidin‐TRITC (Sigma–Aldrich) for 1 hr. .. Images were obtained with the Zeiss Axio Observer Z1 inverted fluorescence microscope (Carl Zeiss, Germany).

    Incubation:

    Article Title: Polarized retinal pigment epithelium generates electrical signals that diminish with age and regulate retinal pathology, et al. Polarized retinal pigment epithelium generates electrical signals that diminish with age and regulate retinal pathology
    Article Snippet: .. The cells were stained for 2 hours with antibodies to Na+ /K+ ‐ATPase (α1 and β1 subunits, EMD Millipore), E‐cad (BD Biosciences) and ZO‐1 (Invitrogen, UK), respectively, and then were incubated with secondary antibodies (Invitrogen) and phalloidin‐TRITC (Sigma‐Aldrich, UK) for 1 hour. .. Images were obtained with the Zeiss Axio Observer Z1 inverted fluorescence microscope and Confocal Zeiss 710 LSM (Carl Zeiss, Germany).

    Article Title: Endogenous bioelectric currents promote differentiation of the mammalian lens. Endogenous bioelectric currents promote differentiation of the mammalian lens
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    other:

    Article Title: Stress‐induced modulation of volume‐regulated anions channels in human alveolar carcinoma cells . Stress‐induced modulation of volume‐regulated anions channels in human alveolar carcinoma cells
    Article Snippet: Primary antibodies Anti‐β ‐actin (A1978, mouse monoclonal Ab, 42 kDa, Sigma‐Aldrich; 1:1000); Anti‐Akt // Anti‐Phospho‐Akt (9272 // 4058, rabbit Ab, 60 kDa, Cell Signaling, Danvers, MA; 1:500 // 1:250 (P‐Akt)); Anti‐histone H3 (9717, rabbit Ab, 18 kDa, Cell Signaling 1:250); Anti‐human‐LRRC8A (SAB1412855, mouse monoclonal Ab, 95 kDa, Sigma‐Aldrich; 1:250); Anti‐FoxO3a // Anti‐Phospho‐FoxO3 (Ser413) (2497//8174, rabbit Ab, 82‐97 kDa, Cell Signaling; 1:250//1:250); Anti‐GAPDH (ZG003, mouse monoclonal Ab, 37 kDa, Thermo Fisher, 1:500); Anti‐NOXA (14766, rabbit Ab, 10 kDa, Cell Signaling; 1:100); Anti‐human p21Waf1/Cip1 (P1484, mouse monoclonal Ab, 21 kDa, Sigma‐Aldrich, 1:250); Anti‐Phospho‐p53 (9284, rabbit Ab, 53 kDa, Cell Signaling, 1:500); Anti‐Rictor (9476, Cell Signaling, 200 kDa, 1:1000) and monoclonal Anti‐Na+ /K+ ‐ATPase (clone M7‐PB‐E9, Sigma‐Aldrich, 110 kDa, 1:150).

    Article Title: Stress‐induced modulation of volume‐regulated anions channels in human alveolar carcinoma cells . Stress‐induced modulation of volume‐regulated anions channels in human alveolar carcinoma cells
    Article Snippet: Anti‐ β ‐actin (A1978, mouse monoclonal Ab, 42 kDa, Sigma‐Aldrich; 1:1000); Anti‐Akt // Anti‐Phospho‐Akt (9272 // 4058, rabbit Ab, 60 kDa, Cell Signaling, Danvers, MA; 1:500 // 1:250 (P‐Akt)); Anti‐histone H3 (9717, rabbit Ab, 18 kDa, Cell Signaling 1:250); Anti‐human‐LRRC8A (SAB1412855, mouse monoclonal Ab, 95 kDa, Sigma‐Aldrich; 1:250); Anti‐FoxO3a // Anti‐Phospho‐FoxO3 (Ser413) (2497//8174, rabbit Ab, 82‐97 kDa, Cell Signaling; 1:250//1:250); Anti‐GAPDH (ZG003, mouse monoclonal Ab, 37 kDa, Thermo Fisher, 1:500); Anti‐NOXA (14766, rabbit Ab, 10 kDa, Cell Signaling; 1:100); Anti‐human p21Waf1/Cip1 (P1484, mouse monoclonal Ab, 21 kDa, Sigma‐Aldrich, 1:250); Anti‐Phospho‐p53 (9284, rabbit Ab, 53 kDa, Cell Signaling, 1:500); Anti‐Rictor (9476, Cell Signaling, 200 kDa, 1:1000) and monoclonal Anti‐Na+ /K+ ‐ATPase (clone M7‐PB‐E9, Sigma‐Aldrich, 110 kDa, 1:150).

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    Millipore na k atpase activity
    PKCη phosphorylated occludin from decreased Na + /K + <t>-ATPase</t> activity is a mechanism for noise-induced blood-labyrinth barrier disruption. A, Confocal images of IgG leakage from capillaries in disrupted blood-labyrinth barrier of noise-exposed (NE) animals. Stria vascularis capillary networks were labeled with anti-collagen type IV (red) and anti-serum protein IgG (H+L, green) antibodies. IgG was confined in normal stria vascularis capillaries (Left) but not in NE animals (Right). B, REE analysis shows significantly increased blood-labyrinth barrier permeability in NE mice (**P = 0.005
    Na K Atpase Activity, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/na k atpase activity/product/Millipore
    Average 88 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    na k atpase activity - by Bioz Stars, 2020-05
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    89
    Millipore na k atpase α1
    Expressions of NCX1 ( A ) and the major subunits of Na + /K + <t>-ATPase</t> ( B ) in adult myocytes isolated from Wt and NCX1 KO hearts. Myocyte isolation and protein immunoassays were done as indicated in methods . GAPDH was used as a loading control. n = 3–4,
    Na K Atpase α1, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/na k atpase α1/product/Millipore
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    94
    Millipore na k atpase
    TRPM2 channels are expressed in the sarcolemma and transverse tubules of adult cardiac myocytes. Confocal images of adult WT mouse ventricular myocytes labeled with anti-α 1 -subunit of Na + -K + <t>-ATPase</t> antibody ( A and D ), with ( B ) or without ( E ) rabbit
    Na K Atpase, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 46 article reviews
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    Image Search Results


    PKCη phosphorylated occludin from decreased Na + /K + -ATPase activity is a mechanism for noise-induced blood-labyrinth barrier disruption. A, Confocal images of IgG leakage from capillaries in disrupted blood-labyrinth barrier of noise-exposed (NE) animals. Stria vascularis capillary networks were labeled with anti-collagen type IV (red) and anti-serum protein IgG (H+L, green) antibodies. IgG was confined in normal stria vascularis capillaries (Left) but not in NE animals (Right). B, REE analysis shows significantly increased blood-labyrinth barrier permeability in NE mice (**P = 0.005

    Journal: PLoS ONE

    Article Title: Na+/K+-ATPase ?1 Identified as an Abundant Protein in the Blood-Labyrinth Barrier That Plays an Essential Role in the Barrier Integrity

    doi: 10.1371/journal.pone.0016547

    Figure Lengend Snippet: PKCη phosphorylated occludin from decreased Na + /K + -ATPase activity is a mechanism for noise-induced blood-labyrinth barrier disruption. A, Confocal images of IgG leakage from capillaries in disrupted blood-labyrinth barrier of noise-exposed (NE) animals. Stria vascularis capillary networks were labeled with anti-collagen type IV (red) and anti-serum protein IgG (H+L, green) antibodies. IgG was confined in normal stria vascularis capillaries (Left) but not in NE animals (Right). B, REE analysis shows significantly increased blood-labyrinth barrier permeability in NE mice (**P = 0.005

    Article Snippet: Enzymatic activity assay Both PKCη and Na+ /K+ -ATPase activity were respectively determined with a PKCη KinEASETM FP Fluorescein Green Assay Kit (Millipore) and an ATPase assay kit (Novus Biologicals).

    Techniques: Activity Assay, Labeling, Permeability, Mouse Assay

    Decreased Na + /K + -ATPase activity increases TJ permeability via PKCη phosphorylated occludin. A and B , Co-immunoprecipitation using isolated stria vascularis capillary lysates shows that PKCη is in a complex with ATP1A1. Goat IgG served as a negative control. C , Protein-protein interaction analysis with purified ATP1A1 (250 ng) and PKCη (250 ng). Ouabain (10 µM) was added where indicated. Control lanes consisted of either anti-ATP1A1 antibody and purified PKCη or anti-PKCη antibody and purified ATP1A1. D , Ouabain inhibition of Na + /K + -ATPase activity causes increased PKCη activity in isolated stria vascularis capillaries (*P = 0.013

    Journal: PLoS ONE

    Article Title: Na+/K+-ATPase ?1 Identified as an Abundant Protein in the Blood-Labyrinth Barrier That Plays an Essential Role in the Barrier Integrity

    doi: 10.1371/journal.pone.0016547

    Figure Lengend Snippet: Decreased Na + /K + -ATPase activity increases TJ permeability via PKCη phosphorylated occludin. A and B , Co-immunoprecipitation using isolated stria vascularis capillary lysates shows that PKCη is in a complex with ATP1A1. Goat IgG served as a negative control. C , Protein-protein interaction analysis with purified ATP1A1 (250 ng) and PKCη (250 ng). Ouabain (10 µM) was added where indicated. Control lanes consisted of either anti-ATP1A1 antibody and purified PKCη or anti-PKCη antibody and purified ATP1A1. D , Ouabain inhibition of Na + /K + -ATPase activity causes increased PKCη activity in isolated stria vascularis capillaries (*P = 0.013

    Article Snippet: Enzymatic activity assay Both PKCη and Na+ /K+ -ATPase activity were respectively determined with a PKCη KinEASETM FP Fluorescein Green Assay Kit (Millipore) and an ATPase assay kit (Novus Biologicals).

    Techniques: Activity Assay, Permeability, Immunoprecipitation, Isolation, Negative Control, Purification, Inhibition

    Expressions of NCX1 ( A ) and the major subunits of Na + /K + -ATPase ( B ) in adult myocytes isolated from Wt and NCX1 KO hearts. Myocyte isolation and protein immunoassays were done as indicated in methods . GAPDH was used as a loading control. n = 3–4,

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Different roles of the cardiac Na+/Ca2+-exchanger in ouabain-induced inotropy, cell signaling, and hypertrophy

    doi: 10.1152/ajpheart.00462.2012

    Figure Lengend Snippet: Expressions of NCX1 ( A ) and the major subunits of Na + /K + -ATPase ( B ) in adult myocytes isolated from Wt and NCX1 KO hearts. Myocyte isolation and protein immunoassays were done as indicated in methods . GAPDH was used as a loading control. n = 3–4,

    Article Snippet: Primary antibodies and their sources were as follows: RDI Research Diagnostics, rabbit anti-Na+ /Ca2+ exchanger; BD Transduction Laboratories, anti-PI3K p85; Cell Signaling Technology, rabbit anti-phospho 473-Akt and anti-Akt; Developmental Studies Hybridoma Bank, University of Iowa: Na+ -K+ -ATPase α1 (α6F); ABR, Na+ /K+ -ATPase α2 ; Millipore, Na+ /K+ ATPase β1; Santa Cruz, anti-phospho-ERK and ERK.

    Techniques: Isolation

    Schematic presentation of the two parallel cell signaling cascades that are linked to digitalis-inhibited Na + /K + -ATPase of the cardiac myocytes, and their relations to digitalis-induced hypertrophy and positive inotropy. See discussion .

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Different roles of the cardiac Na+/Ca2+-exchanger in ouabain-induced inotropy, cell signaling, and hypertrophy

    doi: 10.1152/ajpheart.00462.2012

    Figure Lengend Snippet: Schematic presentation of the two parallel cell signaling cascades that are linked to digitalis-inhibited Na + /K + -ATPase of the cardiac myocytes, and their relations to digitalis-induced hypertrophy and positive inotropy. See discussion .

    Article Snippet: Primary antibodies and their sources were as follows: RDI Research Diagnostics, rabbit anti-Na+ /Ca2+ exchanger; BD Transduction Laboratories, anti-PI3K p85; Cell Signaling Technology, rabbit anti-phospho 473-Akt and anti-Akt; Developmental Studies Hybridoma Bank, University of Iowa: Na+ -K+ -ATPase α1 (α6F); ABR, Na+ /K+ -ATPase α2 ; Millipore, Na+ /K+ ATPase β1; Santa Cruz, anti-phospho-ERK and ERK.

    Techniques:

    TRPM2 channels are expressed in the sarcolemma and transverse tubules of adult cardiac myocytes. Confocal images of adult WT mouse ventricular myocytes labeled with anti-α 1 -subunit of Na + -K + -ATPase antibody ( A and D ), with ( B ) or without ( E ) rabbit

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: The second member of transient receptor potential-melastatin channel family protects hearts from ischemia-reperfusion injury

    doi: 10.1152/ajpheart.00906.2012

    Figure Lengend Snippet: TRPM2 channels are expressed in the sarcolemma and transverse tubules of adult cardiac myocytes. Confocal images of adult WT mouse ventricular myocytes labeled with anti-α 1 -subunit of Na + -K + -ATPase antibody ( A and D ), with ( B ) or without ( E ) rabbit

    Article Snippet: Immunolocalization experiments indicated that both TRPM2 channels and the α1 -subunit of Na+ -K+ -ATPase (sarcolemma marker) were expressed in the sarcolemma and transverse tubules in adult LV myocytes ( ).

    Techniques: Labeling

    I/R decreases Na + -K + -ATPase current ( I pump ) more in TRPM2 KO myocytes. WT or KO hearts were subjected to either sham operation or 30 min ischemia of followed by 3 days of reperfusion before myocyte isolation. LV myocytes were held at 0 mV and 30°C.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: The second member of transient receptor potential-melastatin channel family protects hearts from ischemia-reperfusion injury

    doi: 10.1152/ajpheart.00906.2012

    Figure Lengend Snippet: I/R decreases Na + -K + -ATPase current ( I pump ) more in TRPM2 KO myocytes. WT or KO hearts were subjected to either sham operation or 30 min ischemia of followed by 3 days of reperfusion before myocyte isolation. LV myocytes were held at 0 mV and 30°C.

    Article Snippet: Immunolocalization experiments indicated that both TRPM2 channels and the α1 -subunit of Na+ -K+ -ATPase (sarcolemma marker) were expressed in the sarcolemma and transverse tubules in adult LV myocytes ( ).

    Techniques: Isolation