na k atpase β1 subunit  (Thermo Fisher)


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    Structured Review

    Thermo Fisher na k atpase β1 subunit
    The endogenous plasma membrane-resident <t>Na,K-ATPase</t> β 1 subunit is bound to YFP-linked Na,K-ATPase dog β 1 subunit in MDCK cell monolayers. A , Western blot analysis using anti-YFP and anti-Na,K-ATPase α 1 antibodies shows that immunoprecipitation
    Na K Atpase β1 Subunit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Epithelial Junctions Depend on Intercellular Trans-interactions between the Na,K-ATPase ?1 Subunits *"

    Article Title: Epithelial Junctions Depend on Intercellular Trans-interactions between the Na,K-ATPase ?1 Subunits *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M111.252247

    The endogenous plasma membrane-resident Na,K-ATPase β 1 subunit is bound to YFP-linked Na,K-ATPase dog β 1 subunit in MDCK cell monolayers. A , Western blot analysis using anti-YFP and anti-Na,K-ATPase α 1 antibodies shows that immunoprecipitation
    Figure Legend Snippet: The endogenous plasma membrane-resident Na,K-ATPase β 1 subunit is bound to YFP-linked Na,K-ATPase dog β 1 subunit in MDCK cell monolayers. A , Western blot analysis using anti-YFP and anti-Na,K-ATPase α 1 antibodies shows that immunoprecipitation

    Techniques Used: Western Blot, Immunoprecipitation

    Interactions between the endogenous and exogenous Na,K-ATPase β subunits in MDCK cell monolayers depend on their amino acid sequence and presence of N -glycans. A , confocal microscopy images of MDCK cell monolayers (horizontal sections) show predominant
    Figure Legend Snippet: Interactions between the endogenous and exogenous Na,K-ATPase β subunits in MDCK cell monolayers depend on their amino acid sequence and presence of N -glycans. A , confocal microscopy images of MDCK cell monolayers (horizontal sections) show predominant

    Techniques Used: Sequencing, Confocal Microscopy

    Disruption of intercellular junctions decreases the amount of the endogenous Na,K-ATPase β 1 subunit bound to YFP-β 1 . A , confocal microscopy images of MDCK cells expressing dog YFP-β 1 show that a short incubation of confluent cell
    Figure Legend Snippet: Disruption of intercellular junctions decreases the amount of the endogenous Na,K-ATPase β 1 subunit bound to YFP-β 1 . A , confocal microscopy images of MDCK cells expressing dog YFP-β 1 show that a short incubation of confluent cell

    Techniques Used: Confocal Microscopy, Expressing, Incubation

    2) Product Images from "Diverse Pathways for Maturation of the Na,K-ATPase β1 and β2 Subunits in the Endoplasmic Reticulum of Madin-Darby Canine Kidney Cells"

    Article Title: Diverse Pathways for Maturation of the Na,K-ATPase β1 and β2 Subunits in the Endoplasmic Reticulum of Madin-Darby Canine Kidney Cells

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.172858

    YFP-β 1 and YFP-β 2 preferentially interact with different ER chaperones. A , an anti-YFP antibody precipitates YFP-β 1 and YFP-β 2 ( bottom ) and co-precipitates BiP (middle) and calnexin ( top ) from the whole lysates of the YFP-β 1 - and YFP-β 2 -expressing cells ( lanes 2 and 3 ) but not from the cell lysates of non-transfected MDCK cells ( lane 1 ). B , densitometry quantification of the results shown in A. C , an anti-Na,K-ATPase α 1 antibody precipitates the α 1 subunit ( top ) and co-precipitates BiP ( middle ) from the whole lysates of the YFP-β 1 - and YFP-β 2 -expressing cells ( lanes 2 and 3 ). No bands are detected in a negative control sample containing all of the components used for immunoprecipitation except for cell lysate ( lane 1 ). Error bars , ± S.D. ( n = 3); *, significant difference from YFP-β 2 ; **, significant difference from YFP-β 1 ; p
    Figure Legend Snippet: YFP-β 1 and YFP-β 2 preferentially interact with different ER chaperones. A , an anti-YFP antibody precipitates YFP-β 1 and YFP-β 2 ( bottom ) and co-precipitates BiP (middle) and calnexin ( top ) from the whole lysates of the YFP-β 1 - and YFP-β 2 -expressing cells ( lanes 2 and 3 ) but not from the cell lysates of non-transfected MDCK cells ( lane 1 ). B , densitometry quantification of the results shown in A. C , an anti-Na,K-ATPase α 1 antibody precipitates the α 1 subunit ( top ) and co-precipitates BiP ( middle ) from the whole lysates of the YFP-β 1 - and YFP-β 2 -expressing cells ( lanes 2 and 3 ). No bands are detected in a negative control sample containing all of the components used for immunoprecipitation except for cell lysate ( lane 1 ). Error bars , ± S.D. ( n = 3); *, significant difference from YFP-β 2 ; **, significant difference from YFP-β 1 ; p

    Techniques Used: Expressing, Transfection, Negative Control, Immunoprecipitation

    The plasma membrane-resident Na,K-ATPase subunits are degraded at a similar rate. A , cell monolayers of non-transfected, YFP-β 1 -expressing, and YFP-β 2 -expressing MDCK cells were biotinylated from the basolateral side using a membrane-impermeable biotinylation reagent and then were chased at 37 °C for the indicated time periods. After cell lysis, the biotinylated proteins were isolated and analyzed by SDS-PAGE followed by immunoblotting using the antibodies against the α 1 and β 1 subunits of the Na,K-ATPase and against YFP. B , densitometry of the results presented in A. Error bars , ±S.D. ( n = 3); PM , plasma membrane; Na,K -α 1 and Na,K- β 1 , the endogenous α 1 and β 1 subunits of the Na,K-ATPase; Non-tr ., non-transfected MDCK cells.
    Figure Legend Snippet: The plasma membrane-resident Na,K-ATPase subunits are degraded at a similar rate. A , cell monolayers of non-transfected, YFP-β 1 -expressing, and YFP-β 2 -expressing MDCK cells were biotinylated from the basolateral side using a membrane-impermeable biotinylation reagent and then were chased at 37 °C for the indicated time periods. After cell lysis, the biotinylated proteins were isolated and analyzed by SDS-PAGE followed by immunoblotting using the antibodies against the α 1 and β 1 subunits of the Na,K-ATPase and against YFP. B , densitometry of the results presented in A. Error bars , ±S.D. ( n = 3); PM , plasma membrane; Na,K -α 1 and Na,K- β 1 , the endogenous α 1 and β 1 subunits of the Na,K-ATPase; Non-tr ., non-transfected MDCK cells.

    Techniques Used: Transfection, Expressing, Lysis, Isolation, SDS Page

    The unassembled YFP-linked β 2 subunit, but not β 1 subunit, is largely retained in the ER in MDCK cells grown at low density. A , confocal microscopy images of YFP-β 1 - and YFP-β 2 -expressing cells showing that intracellular retention of both fusion proteins, but especially of YFP-β 2 , gradually decreases during development of the mature cell monolayers. B , YFP-β 2 ( green ) is co-localized with the endogenous α 1 subunit ( red ) in the lateral membranes but not inside the cells as detected by immunostaining of subconfluent YFP-β 2 -expressing cells using the monoclonal antibody against the Na,K-ATPase α 1 subunit. C , the intracellular fraction of YFP-β 2 ( green ) co-localized with the ER ( red ) as detected by transient expression of the fluorescent ER marker DsRed2-ER in subconfluent YFP-β 2 -expressing cells. N , nucleus; PM , plasma membrane; Na,K- α 1 , the endogenous Na,K-ATPase α 1 subunit.
    Figure Legend Snippet: The unassembled YFP-linked β 2 subunit, but not β 1 subunit, is largely retained in the ER in MDCK cells grown at low density. A , confocal microscopy images of YFP-β 1 - and YFP-β 2 -expressing cells showing that intracellular retention of both fusion proteins, but especially of YFP-β 2 , gradually decreases during development of the mature cell monolayers. B , YFP-β 2 ( green ) is co-localized with the endogenous α 1 subunit ( red ) in the lateral membranes but not inside the cells as detected by immunostaining of subconfluent YFP-β 2 -expressing cells using the monoclonal antibody against the Na,K-ATPase α 1 subunit. C , the intracellular fraction of YFP-β 2 ( green ) co-localized with the ER ( red ) as detected by transient expression of the fluorescent ER marker DsRed2-ER in subconfluent YFP-β 2 -expressing cells. N , nucleus; PM , plasma membrane; Na,K- α 1 , the endogenous Na,K-ATPase α 1 subunit.

    Techniques Used: Confocal Microscopy, Expressing, Immunostaining, Marker

    Impairment of α-β association due to point mutations in the α-interacting regions of the β 1 and β 2 subunits correlates with increased BIP binding to both β 1 and β 2 subunits. A , alanine substitutions of Tyr 39 , Phe 42 , and Tyr 43 in YFP-linked rat β 1 subunit produced a triple mutant Y39A/F42A/Y43A ( YFY 1 ) of YFP-β 1 . The residues homologous to Tyr 39 , Phe 42 , and Tyr 43 were also mutated in YFP-linked human β 2 subunit, producing a triple mutant, Y44A/F47A/Y48A ( YFY 2 ) of YFP-β 2 . The proteins were immunoprecipitated from lysates of the cells expressing the wild type YFP-β 1 or YFP-β 2 ( WT ) or their mutants ( YFY ) using the antibody against YFP and were analyzed by SDS-PAGE followed by immunoblotting using the antibodies against YFP, the Na,K-ATPase α 1 subunit, BiP, and calnexin. B , densitometry quantification of the results shown in A. C , the products of tryptic digestion of the whole lysates of the cells expressing the wild type or mutated YFP-β 1 were analyzed by immunoblotting using the antibody against YFP as described under “Experimental Procedures.” D , densitometry quantification of the results shown in C. Error bars , ±S.D. ( n = 3); PM , plasma membrane.
    Figure Legend Snippet: Impairment of α-β association due to point mutations in the α-interacting regions of the β 1 and β 2 subunits correlates with increased BIP binding to both β 1 and β 2 subunits. A , alanine substitutions of Tyr 39 , Phe 42 , and Tyr 43 in YFP-linked rat β 1 subunit produced a triple mutant Y39A/F42A/Y43A ( YFY 1 ) of YFP-β 1 . The residues homologous to Tyr 39 , Phe 42 , and Tyr 43 were also mutated in YFP-linked human β 2 subunit, producing a triple mutant, Y44A/F47A/Y48A ( YFY 2 ) of YFP-β 2 . The proteins were immunoprecipitated from lysates of the cells expressing the wild type YFP-β 1 or YFP-β 2 ( WT ) or their mutants ( YFY ) using the antibody against YFP and were analyzed by SDS-PAGE followed by immunoblotting using the antibodies against YFP, the Na,K-ATPase α 1 subunit, BiP, and calnexin. B , densitometry quantification of the results shown in A. C , the products of tryptic digestion of the whole lysates of the cells expressing the wild type or mutated YFP-β 1 were analyzed by immunoblotting using the antibody against YFP as described under “Experimental Procedures.” D , densitometry quantification of the results shown in C. Error bars , ±S.D. ( n = 3); PM , plasma membrane.

    Techniques Used: Binding Assay, Produced, Mutagenesis, Immunoprecipitation, Expressing, SDS Page

    The degree of the ER retention of YFP-linked β 1 and β 2 subunits correlates with BiP binding to the subunits. A , equal amounts of total lysates of YFP-β 1 - and YFP-β 2 -expressing cells (6 μg of protein) obtained from small colonies or from mature cell monolayers were analyzed by SDS-PAGE followed by immunoblotting using the antibodies against α 1 and β 1 subunits of the Na,K-ATPase. B , equal amounts of total lysates of YFP-β 1 - and YFP-β 2 -expressing cells (600 μg of protein) obtained from small colonies or from mature cell monolayers were used for immunoprecipitation of YFP-linked subunits. Immunoprecipitated YFP-β 1 and YFP-β 2 , as well as co-immunoprecipitated BiP and calnexin, were analyzed by immunoblotting. C , densitometry quantification of the results shown in B. IP , immunoprecipitation; PM , plasma membrane.
    Figure Legend Snippet: The degree of the ER retention of YFP-linked β 1 and β 2 subunits correlates with BiP binding to the subunits. A , equal amounts of total lysates of YFP-β 1 - and YFP-β 2 -expressing cells (6 μg of protein) obtained from small colonies or from mature cell monolayers were analyzed by SDS-PAGE followed by immunoblotting using the antibodies against α 1 and β 1 subunits of the Na,K-ATPase. B , equal amounts of total lysates of YFP-β 1 - and YFP-β 2 -expressing cells (600 μg of protein) obtained from small colonies or from mature cell monolayers were used for immunoprecipitation of YFP-linked subunits. Immunoprecipitated YFP-β 1 and YFP-β 2 , as well as co-immunoprecipitated BiP and calnexin, were analyzed by immunoblotting. C , densitometry quantification of the results shown in B. IP , immunoprecipitation; PM , plasma membrane.

    Techniques Used: Binding Assay, Expressing, SDS Page, Immunoprecipitation

    The ER-resident YFP-β 2 is degraded more slowly than ER-resident YFP-β 1 . A , cells expressing YFP-β 1 or YFP-β 2 were incubated in the presence of 20 μg/ml CHX for the indicated time periods and lysed. To separate the high mannose form of YFP-β 2 from its complex type form on SDS-PAGE, immunoprecipitated YFP-β 2 was treated with endoglycosidase H ( EndoH ) to transform the high mannose form to the deglycosylated form prior to SDS-PAGE. B , densitometry of the results presented in A. C , the proteins immunoprecipitated using the antibody against the Na,K-ATPase α 1 subunit were obtained from the YFP-β 1 - and YFP-β 2 -expressing cells before or after a 1-h cell incubation with 20 μg/ml CHX and then were analyzed by SDS-PAGE followed by immunoblotting using the antibodies against YFP. Error bars , ± S.D. ( n = 3); IP , immunoprecipitation; PM , plasma membrane.
    Figure Legend Snippet: The ER-resident YFP-β 2 is degraded more slowly than ER-resident YFP-β 1 . A , cells expressing YFP-β 1 or YFP-β 2 were incubated in the presence of 20 μg/ml CHX for the indicated time periods and lysed. To separate the high mannose form of YFP-β 2 from its complex type form on SDS-PAGE, immunoprecipitated YFP-β 2 was treated with endoglycosidase H ( EndoH ) to transform the high mannose form to the deglycosylated form prior to SDS-PAGE. B , densitometry of the results presented in A. C , the proteins immunoprecipitated using the antibody against the Na,K-ATPase α 1 subunit were obtained from the YFP-β 1 - and YFP-β 2 -expressing cells before or after a 1-h cell incubation with 20 μg/ml CHX and then were analyzed by SDS-PAGE followed by immunoblotting using the antibodies against YFP. Error bars , ± S.D. ( n = 3); IP , immunoprecipitation; PM , plasma membrane.

    Techniques Used: Expressing, Incubation, SDS Page, Immunoprecipitation

    3) Product Images from "Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na,K-ATPase ?1 subunit * subunit * **"

    Article Title: Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na,K-ATPase ?1 subunit * subunit * **

    Journal:

    doi: 10.1074/jbc.M704713200

    Prevention of glycosylation of the Na,K-ATPase β 1 subunit increases the paracellular permeability of the MDCK cell monolayer and decreases the tightening effect of swainsonine
    Figure Legend Snippet: Prevention of glycosylation of the Na,K-ATPase β 1 subunit increases the paracellular permeability of the MDCK cell monolayer and decreases the tightening effect of swainsonine

    Techniques Used: Permeability

    Prevention of glycosylation of the Na,K-ATPase β 1 subunit decreases detergent resistance of E-cadherin and abolishes a swainsonine-induced increase in detergent resistance of E-cadherin
    Figure Legend Snippet: Prevention of glycosylation of the Na,K-ATPase β 1 subunit decreases detergent resistance of E-cadherin and abolishes a swainsonine-induced increase in detergent resistance of E-cadherin

    Techniques Used:

    Prevention of glycosylation of the Na,K-ATPase β 1 subunit and exposure of cell to tunicamycin results in the distortion of cell-cell junctions
    Figure Legend Snippet: Prevention of glycosylation of the Na,K-ATPase β 1 subunit and exposure of cell to tunicamycin results in the distortion of cell-cell junctions

    Techniques Used:

    Swainsonine increases detergent resistance of the E-cadherin and the Na,K-ATPase β 1 subunit in the tight monolayers of MDCK cells
    Figure Legend Snippet: Swainsonine increases detergent resistance of the E-cadherin and the Na,K-ATPase β 1 subunit in the tight monolayers of MDCK cells

    Techniques Used:

    Progression of the dispersed MDCK cells into the tight cell monolayer is associated with a gradual decrease in the paracellular permeability, increase in resistance of E-cadherin and the Na,K-ATPase to the non-ionic detergent, and increase in electrophoretic
    Figure Legend Snippet: Progression of the dispersed MDCK cells into the tight cell monolayer is associated with a gradual decrease in the paracellular permeability, increase in resistance of E-cadherin and the Na,K-ATPase to the non-ionic detergent, and increase in electrophoretic

    Techniques Used: Permeability

    Electrophoretic gel mobility of E-cadherin, β 1 -integrin and the Na,K-ATPase β 1 subunit isolated from kidney is greater than that of the proteins isolated from small intestine
    Figure Legend Snippet: Electrophoretic gel mobility of E-cadherin, β 1 -integrin and the Na,K-ATPase β 1 subunit isolated from kidney is greater than that of the proteins isolated from small intestine

    Techniques Used: Isolation

    The complex-type N-glycans of E-cadherin and the Na,K-ATPase β 1 subunit have fewer branches or shorter branches in the tight MDCK cell monolayers as compared to the dispersed MDCK cells
    Figure Legend Snippet: The complex-type N-glycans of E-cadherin and the Na,K-ATPase β 1 subunit have fewer branches or shorter branches in the tight MDCK cell monolayers as compared to the dispersed MDCK cells

    Techniques Used:

    4) Product Images from "Human Breast Tumor Cells Are More Resistant to Cardiac Glycoside Toxicity Than Non-Tumorigenic Breast Cells"

    Article Title: Human Breast Tumor Cells Are More Resistant to Cardiac Glycoside Toxicity Than Non-Tumorigenic Breast Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0084306

    ATPase Assay of breast cell membranes treated with cardiac glycosides; (A) ouabain, (B) digitoxin, and (C) bufalin. The Na,K-ATPase activity in total membranes isolated from non-tumorous 184D, 184A, and MCF10A (10A) cells, as well as cancerous MDA-MB-231 (MDA), MCF7, and MCF10CA1 (CA1) cells is inhibited in a concentration dependent manner for all cells types. Na,K-ATPase activity (µmol Pi liberated per mg protein per hour) was determined and displayed as the percentage of activity relative to the untreated sample for each cell type. There was no statistically significant difference in activity between normal and tumor cells treated with similar concentrations of ouabain, digitoxin, or bufalin (p > 0.05).
    Figure Legend Snippet: ATPase Assay of breast cell membranes treated with cardiac glycosides; (A) ouabain, (B) digitoxin, and (C) bufalin. The Na,K-ATPase activity in total membranes isolated from non-tumorous 184D, 184A, and MCF10A (10A) cells, as well as cancerous MDA-MB-231 (MDA), MCF7, and MCF10CA1 (CA1) cells is inhibited in a concentration dependent manner for all cells types. Na,K-ATPase activity (µmol Pi liberated per mg protein per hour) was determined and displayed as the percentage of activity relative to the untreated sample for each cell type. There was no statistically significant difference in activity between normal and tumor cells treated with similar concentrations of ouabain, digitoxin, or bufalin (p > 0.05).

    Techniques Used: ATPase Assay, Activity Assay, Isolation, Multiple Displacement Amplification, Concentration Assay

    Src kinase does not coimmunoprecipitate with α-subunit in MCF10A or MDA-MB-231 cells. MCF10A and MDA-MB-231 cells were treated with (+) or without (-) 500 nM ouabain for 24 hours. Lysates were collected and subject to immunoprecipitation using a rabbit anti-α antibody, raised against Na,K-ATPase α-subunit’s M4/M5 cytoplasmic loop. 10% of the initial lysate (IN), the co-immunoprecipitated proteins (IP), and 10% of the unbound supernatant (Sup) after IP were used for western blots. Western blot analysis was performed and probed using mouse anti-Na,K-ATPase α 1 -subunit, mouse anti-Src, and mouse anti-Na,K-ATPase β 1 subunit antibodies.
    Figure Legend Snippet: Src kinase does not coimmunoprecipitate with α-subunit in MCF10A or MDA-MB-231 cells. MCF10A and MDA-MB-231 cells were treated with (+) or without (-) 500 nM ouabain for 24 hours. Lysates were collected and subject to immunoprecipitation using a rabbit anti-α antibody, raised against Na,K-ATPase α-subunit’s M4/M5 cytoplasmic loop. 10% of the initial lysate (IN), the co-immunoprecipitated proteins (IP), and 10% of the unbound supernatant (Sup) after IP were used for western blots. Western blot analysis was performed and probed using mouse anti-Na,K-ATPase α 1 -subunit, mouse anti-Src, and mouse anti-Na,K-ATPase β 1 subunit antibodies.

    Techniques Used: Multiple Displacement Amplification, Immunoprecipitation, Western Blot

    5) Product Images from "The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits"

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.186148

    The increase in cell adhesion by silencing FXYD5 is not abolished by preventing complex glycosylation of the β 1 subunit. (A) The levels of the Na,K-ATPase α 1 and β 1 subunits, E-cadherin (E-cad), CD29, FXYD5 and actin were determined
    Figure Legend Snippet: The increase in cell adhesion by silencing FXYD5 is not abolished by preventing complex glycosylation of the β 1 subunit. (A) The levels of the Na,K-ATPase α 1 and β 1 subunits, E-cadherin (E-cad), CD29, FXYD5 and actin were determined

    Techniques Used:

    The disruptive effect of FXYD5 on the tight junctions is prevented by overexpression of the Na,K-ATPase β 1 subunit. (A) rATII cells were infected with Ad-mCherry-HA-FXYD5, Ad-WT-YFP-β 1 or Ad-Y199-YFP-β 1 and analyzed by confocal
    Figure Legend Snippet: The disruptive effect of FXYD5 on the tight junctions is prevented by overexpression of the Na,K-ATPase β 1 subunit. (A) rATII cells were infected with Ad-mCherry-HA-FXYD5, Ad-WT-YFP-β 1 or Ad-Y199-YFP-β 1 and analyzed by confocal

    Techniques Used: Over Expression, Infection

    The increase in cell adhesion by FXYD5 knockdown is prevented by antibody specific to the Na,K-ATPase β 1 subunit. (A) siRNA-transfected A549 cells were incubated in the presence or absence of a control (CT), Na,K-ATPase β 1 subunit (β
    Figure Legend Snippet: The increase in cell adhesion by FXYD5 knockdown is prevented by antibody specific to the Na,K-ATPase β 1 subunit. (A) siRNA-transfected A549 cells were incubated in the presence or absence of a control (CT), Na,K-ATPase β 1 subunit (β

    Techniques Used: Transfection, Incubation

    6) Product Images from "Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart"

    Article Title: Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M116.751735

    Na,K-ATPase β 2 and α 2 subunits are localized almost exclusively in T-tubules in cardiomyocytes, whereas the α 1 and β 1 subunits are localized in both sarcolemma and T-tubules. A , frozen sections of rat heart were double-stained
    Figure Legend Snippet: Na,K-ATPase β 2 and α 2 subunits are localized almost exclusively in T-tubules in cardiomyocytes, whereas the α 1 and β 1 subunits are localized in both sarcolemma and T-tubules. A , frozen sections of rat heart were double-stained

    Techniques Used: Staining

    Expression of purified Na,K-ATPase isoforms. Coomassie-stained SDS-PAGE of purified isoforms (5 μg/lane). For deglycosylation, samples were denatured and treated with PNGase F for 60 min at 37 °C.
    Figure Legend Snippet: Expression of purified Na,K-ATPase isoforms. Coomassie-stained SDS-PAGE of purified isoforms (5 μg/lane). For deglycosylation, samples were denatured and treated with PNGase F for 60 min at 37 °C.

    Techniques Used: Expressing, Purification, Staining, SDS Page

    Models for docking of DcB to α 1 β 1 , α 2 β 2 , and α 2 β 3 . DcB was docked into homology models of human Na,K-ATPase isoforms derived from the porcine E2P·Mg·digoxin structure (Protein Data Bank code
    Figure Legend Snippet: Models for docking of DcB to α 1 β 1 , α 2 β 2 , and α 2 β 3 . DcB was docked into homology models of human Na,K-ATPase isoforms derived from the porcine E2P·Mg·digoxin structure (Protein Data Bank code

    Techniques Used: Derivative Assay

    The Na,K-ATPase α 2 subunit and β 2 subunit preferentially interact with each other in mouse heart. A , Western blotting analysis of proteins immunoprecipitated and co-immunoprecipitated from the detergent extracts of mouse heart microsome
    Figure Legend Snippet: The Na,K-ATPase α 2 subunit and β 2 subunit preferentially interact with each other in mouse heart. A , Western blotting analysis of proteins immunoprecipitated and co-immunoprecipitated from the detergent extracts of mouse heart microsome

    Techniques Used: Western Blot, Immunoprecipitation

    The Na,K-ATPase α 2 subunit and β 2 subunit are preferentially expressed in the mouse embryonic heart in contrast to the ubiquitously expressed α 1 subunit. A , paraffin-embedded sections of mouse embryos (embryonic day 12.5) were
    Figure Legend Snippet: The Na,K-ATPase α 2 subunit and β 2 subunit are preferentially expressed in the mouse embryonic heart in contrast to the ubiquitously expressed α 1 subunit. A , paraffin-embedded sections of mouse embryos (embryonic day 12.5) were

    Techniques Used:

    Potassium-digoxin antagonism depicted for α 1 β 1 , α 2 β 1 , α 2 β 2 , and α 2 β 3 . Inhibition of purified Na,K-ATPase isoforms by digoxin was measured, and K i values were plotted against the potassium
    Figure Legend Snippet: Potassium-digoxin antagonism depicted for α 1 β 1 , α 2 β 1 , α 2 β 2 , and α 2 β 3 . Inhibition of purified Na,K-ATPase isoforms by digoxin was measured, and K i values were plotted against the potassium

    Techniques Used: Inhibition, Purification

    Potassium-[ 3 H]digoxin antagonism. Yeast membranes harboring α 2 β 1 , α 2 β 2 , or α 2 β 3 Na,K-ATPase were incubated with varying concentrations of KCl, and residual [ 3 H]digoxin binding was measured. The lines represent
    Figure Legend Snippet: Potassium-[ 3 H]digoxin antagonism. Yeast membranes harboring α 2 β 1 , α 2 β 2 , or α 2 β 3 Na,K-ATPase were incubated with varying concentrations of KCl, and residual [ 3 H]digoxin binding was measured. The lines represent

    Techniques Used: Incubation, Binding Assay

    Inhibition of Na,K-ATPase Isoforms by Perhydro-1,4-oxazepine Derivatives of Digoxin
    Figure Legend Snippet: Inhibition of Na,K-ATPase Isoforms by Perhydro-1,4-oxazepine Derivatives of Digoxin

    Techniques Used: Inhibition

    7) Product Images from "Subunit Isoform Selectivity in Assembly of Na,K-ATPase ?-? Heterodimers *"

    Article Title: Subunit Isoform Selectivity in Assembly of Na,K-ATPase ?-? Heterodimers *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M112.370734

    Localization of the Na,K-ATPase β 2 subunit in nerve sections is similar to that of the Na,K-ATPase α 2 subunit, but not of the Na,K-ATPase α 1 subunit or β 1 subunit. A , frozen sections of rat sciatic nerve were double stained
    Figure Legend Snippet: Localization of the Na,K-ATPase β 2 subunit in nerve sections is similar to that of the Na,K-ATPase α 2 subunit, but not of the Na,K-ATPase α 1 subunit or β 1 subunit. A , frozen sections of rat sciatic nerve were double stained

    Techniques Used: Staining

    The Na,K-ATPase α 2 -β 2 complex is less stable than the Na,K-ATPase α-β 1 or α-β 3 complexes in detergent extracts obtained from mouse brain membranes. A , various concentrations of DDM were used to extract proteins
    Figure Legend Snippet: The Na,K-ATPase α 2 -β 2 complex is less stable than the Na,K-ATPase α-β 1 or α-β 3 complexes in detergent extracts obtained from mouse brain membranes. A , various concentrations of DDM were used to extract proteins

    Techniques Used:

    Localization of the Na,K-ATPase α 1 , α 2 , and β 2 subunits in rat kidney and brain sections. Frozen sections of rat kidney ( A ) and rat brain ( B ) were double-stained by using mouse antibodies against α 1 subunit ( green ) and
    Figure Legend Snippet: Localization of the Na,K-ATPase α 1 , α 2 , and β 2 subunits in rat kidney and brain sections. Frozen sections of rat kidney ( A ) and rat brain ( B ) were double-stained by using mouse antibodies against α 1 subunit ( green ) and

    Techniques Used: Staining

    The Na,K-ATPase α 1 -β 1 complex is more stable than the Na,K-ATPase α 1 -β 2 complex in detergent extracts from MDCK cells. A , MDCK cells stably expressing either YFP-β 1 or YFP-β 2 were lysed by incubation with
    Figure Legend Snippet: The Na,K-ATPase α 1 -β 1 complex is more stable than the Na,K-ATPase α 1 -β 2 complex in detergent extracts from MDCK cells. A , MDCK cells stably expressing either YFP-β 1 or YFP-β 2 were lysed by incubation with

    Techniques Used: Stable Transfection, Expressing, Incubation

    The Na,K-ATPase α 1 -β 2 complex is preserved in digitonin and CHAPS extracts from MDCK cells. A , proteins were extracted from MDCK cells expressing YFP-β 1 , or YFP-β 2 , or YFP-linked bile acid transporter (YFP-NTCP), with the
    Figure Legend Snippet: The Na,K-ATPase α 1 -β 2 complex is preserved in digitonin and CHAPS extracts from MDCK cells. A , proteins were extracted from MDCK cells expressing YFP-β 1 , or YFP-β 2 , or YFP-linked bile acid transporter (YFP-NTCP), with the

    Techniques Used: Expressing

    The Na,K-ATPase α 2 and β 2 subunits are selectively co-immunoprecipitated from mouse brain extracts. Proteins were extracted from mouse brain homogenate by using 1% Nonidet P-40/0.5% DOC. A , the antibodies against the Na,K-ATPase β
    Figure Legend Snippet: The Na,K-ATPase α 2 and β 2 subunits are selectively co-immunoprecipitated from mouse brain extracts. Proteins were extracted from mouse brain homogenate by using 1% Nonidet P-40/0.5% DOC. A , the antibodies against the Na,K-ATPase β

    Techniques Used: Immunoprecipitation

    8) Product Images from "The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits"

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.186148

    The increase in cell adhesion by silencing FXYD5 is not abolished by preventing complex glycosylation of the β 1 subunit. (A) The levels of the Na,K-ATPase α 1 and β 1 subunits, E-cadherin (E-cad), CD29, FXYD5 and actin were determined
    Figure Legend Snippet: The increase in cell adhesion by silencing FXYD5 is not abolished by preventing complex glycosylation of the β 1 subunit. (A) The levels of the Na,K-ATPase α 1 and β 1 subunits, E-cadherin (E-cad), CD29, FXYD5 and actin were determined

    Techniques Used:

    The disruptive effect of FXYD5 on the tight junctions is prevented by overexpression of the Na,K-ATPase β 1 subunit. (A) rATII cells were infected with Ad-mCherry-HA-FXYD5, Ad-WT-YFP-β 1 or Ad-Y199-YFP-β 1 and analyzed by confocal
    Figure Legend Snippet: The disruptive effect of FXYD5 on the tight junctions is prevented by overexpression of the Na,K-ATPase β 1 subunit. (A) rATII cells were infected with Ad-mCherry-HA-FXYD5, Ad-WT-YFP-β 1 or Ad-Y199-YFP-β 1 and analyzed by confocal

    Techniques Used: Over Expression, Infection

    The increase in cell adhesion by FXYD5 knockdown is prevented by antibody specific to the Na,K-ATPase β 1 subunit. (A) siRNA-transfected A549 cells were incubated in the presence or absence of a control (CT), Na,K-ATPase β 1 subunit (β
    Figure Legend Snippet: The increase in cell adhesion by FXYD5 knockdown is prevented by antibody specific to the Na,K-ATPase β 1 subunit. (A) siRNA-transfected A549 cells were incubated in the presence or absence of a control (CT), Na,K-ATPase β 1 subunit (β

    Techniques Used: Transfection, Incubation

    Related Articles

    Transduction:

    Article Title: Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart
    Article Snippet: For immunofluorescent staining, the following monoclonal antibodies were used: Na,K-ATPase α1 subunit (mouse, clone C464.6, 1:20; Millipore) and Na,K-ATPase β1 subunit (mouse, clone M17 P5 F11, 1:100; Affinity Bioreagents). .. For Western blotting analysis, the following monoclonal antibodies were used: against the Na,K-ATPase α1 subunit (mouse, clone C464.6, 1:1000; Millipore), against the Na,K-ATPase β2 subunit (mouse, clone 35; BD Transduction Laboratories), and Na,K-ATPase β3 subunit (goat, 1:500; Santa Cruz Biotechnology, Inc.).

    Clone Assay:

    Article Title: Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na,K-ATPase ?1 subunit * subunit * **
    Article Snippet: .. The following monoclonal antibodies were used for Western blot analysis: against E-cadherin (Alexis Biochemicals), against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents), against GFP, clones 7.1 and 13.1, that also recognized YFP (Roche Molecular Biochemicals), against β1 -integrin (BD Transduction Laboratories), and against the Na+ /Ca2+ exchanger (Novus Biologicals, Inc). .. Also, a polyclonal antibody against polycystin-2 (Chemicon International) was used.

    Article Title: Diverse Pathways for Maturation of the Na,K-ATPase β1 and β2 Subunits in the Endoplasmic Reticulum of Madin-Darby Canine Kidney Cells
    Article Snippet: .. The following monoclonal antibodies were used for immunoprecipitation and/or Western blot analysis: against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore); against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Applied Science); and against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents). .. Also, polyclonal antibodies against the Na,K-ATPase α1 subunit (Cell Signaling), against calnexin (Abcam), against BiP (Abcam), and against GFP, which also recognizes YFP (Clontech), were used.

    Article Title: Subunit Isoform Selectivity in Assembly of Na,K-ATPase ?-? Heterodimers *
    Article Snippet: For immunofluorescent staining, the monoclonal antibodies against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore) and against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents) and polyclonal antibodies against the Na,K-ATPase α2 subunit, (Millipore) and against the Na,K-ATPase β2 subunit (Millipore) were used. .. Also, the following monoclonal antibodies were used for Western blot analysis: against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Diagnostics), against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore), against the Na,K-ATPase α3 subunit (Upstate), against the Na,K-ATPase β2 subunit, clone 35 (BD Bioscience Pharmingen), and against the Na,K-ATPase β3 subunit (Santa Cruz Biotechnology).

    Article Title: Epithelial Junctions Depend on Intercellular Trans-interactions between the Na,K-ATPase ?1 Subunits *
    Article Snippet: .. The following monoclonal antibodies were used for immunoprecipitation and/or Western blot analysis: against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore); against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Diagnostics); against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents); against β-catenin (BD Transduction Laboratories); against E-cadherin, clone DECMA (Sigma); and against occludin (Zymed Laboratories Inc.. Also, a polyclonal antibody against GFP, which recognizes YFP (Clontech), was used. .. Confluent monolayers of MDCK cells expressing the YFP-linked dog β1 subunit grown in 35-mm2 wells of a 6-well plate were rinsed twice with PBS containing 1 m m EDTA and incubated with PBS for 60 min at 37 °C in CO2 incubator.

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits
    Article Snippet: .. The following monoclonal antibodies were used: GFP, clones 7.1 and 13.1, which also recognize YFP (dilution 1:1000; cat. no. 11814460001; Roche Diagnostics, Indianapolis, IN), Na,K-ATPase α1 subunit, clone C464.6 (dilution 1:2000; cat. no. 05-369; EMD Millipore, MA), Na,K-ATPase β1 subunit, clone M17-P5-F11 (dilution 1:1000; cat. no. MA3-930; Affinity Bioreagents, Golden, CO), Na,K-ATPase β1 subunit, clone 464.8 (dilution 1:1000; cat. no. NB300-147; Novus Biologicals, Littleton, CO), β1-integrin/CD29 (dilution 1:1000; cat. no. 610467; BD Transduction Laboratories, CA), Dysadherin, clone D-2 (dilution 1:500; cat. no. sc-166782; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), E-cadherin, clone 36 (dilution 1:1000; cat. no. 610181; BD Biosciences), HA (clone 16B12; dilution 1:1000; cat. no. 901502; Biolegend, San Diego, CA, USA) and HA, clone F-7 (dilution 1:500; cat. no. sc-7392; Santa Cruz Biotechnology). .. The following polyclonal antibodies were used: FXYD5 (dilution 1:1000; cat. no. HPA010817; Sigma-Aldrich), Na,K-ATPase β1 subunit (dilution 1:1000; cat. no. GTX113390; GeneTex, Irvine, CA) which was used to detect the β1 subunit after PNGase F treatment in rATII cells, and β-actin (dilution 1:1000; cat. no. 4967; Cell Signaling, Danvers, MA).

    Immunoprecipitation:

    Article Title: Diverse Pathways for Maturation of the Na,K-ATPase β1 and β2 Subunits in the Endoplasmic Reticulum of Madin-Darby Canine Kidney Cells
    Article Snippet: .. The following monoclonal antibodies were used for immunoprecipitation and/or Western blot analysis: against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore); against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Applied Science); and against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents). .. Also, polyclonal antibodies against the Na,K-ATPase α1 subunit (Cell Signaling), against calnexin (Abcam), against BiP (Abcam), and against GFP, which also recognizes YFP (Clontech), were used.

    Article Title: Epithelial Junctions Depend on Intercellular Trans-interactions between the Na,K-ATPase ?1 Subunits *
    Article Snippet: .. The following monoclonal antibodies were used for immunoprecipitation and/or Western blot analysis: against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore); against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Diagnostics); against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents); against β-catenin (BD Transduction Laboratories); against E-cadherin, clone DECMA (Sigma); and against occludin (Zymed Laboratories Inc.. Also, a polyclonal antibody against GFP, which recognizes YFP (Clontech), was used. .. Confluent monolayers of MDCK cells expressing the YFP-linked dog β1 subunit grown in 35-mm2 wells of a 6-well plate were rinsed twice with PBS containing 1 m m EDTA and incubated with PBS for 60 min at 37 °C in CO2 incubator.

    Western Blot:

    Article Title: Inverse correlation between the extent of N-glycan branching and intercellular adhesion in epithelia: contribution of the Na,K-ATPase ?1 subunit * subunit * **
    Article Snippet: .. The following monoclonal antibodies were used for Western blot analysis: against E-cadherin (Alexis Biochemicals), against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents), against GFP, clones 7.1 and 13.1, that also recognized YFP (Roche Molecular Biochemicals), against β1 -integrin (BD Transduction Laboratories), and against the Na+ /Ca2+ exchanger (Novus Biologicals, Inc). .. Also, a polyclonal antibody against polycystin-2 (Chemicon International) was used.

    Article Title: Diverse Pathways for Maturation of the Na,K-ATPase β1 and β2 Subunits in the Endoplasmic Reticulum of Madin-Darby Canine Kidney Cells
    Article Snippet: .. The following monoclonal antibodies were used for immunoprecipitation and/or Western blot analysis: against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore); against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Applied Science); and against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents). .. Also, polyclonal antibodies against the Na,K-ATPase α1 subunit (Cell Signaling), against calnexin (Abcam), against BiP (Abcam), and against GFP, which also recognizes YFP (Clontech), were used.

    Article Title: Subunit Isoform Selectivity in Assembly of Na,K-ATPase ?-? Heterodimers *
    Article Snippet: Paragraph title: Primary Antibodies Used for Immunofluorescent Staining and Western Blot Analysis ... For immunofluorescent staining, the monoclonal antibodies against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore) and against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents) and polyclonal antibodies against the Na,K-ATPase α2 subunit, (Millipore) and against the Na,K-ATPase β2 subunit (Millipore) were used.

    Article Title: Epithelial Junctions Depend on Intercellular Trans-interactions between the Na,K-ATPase ?1 Subunits *
    Article Snippet: .. The following monoclonal antibodies were used for immunoprecipitation and/or Western blot analysis: against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore); against GFP, clones 7.1 and 13.1, which also recognizes YFP (Roche Diagnostics); against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents); against β-catenin (BD Transduction Laboratories); against E-cadherin, clone DECMA (Sigma); and against occludin (Zymed Laboratories Inc.. Also, a polyclonal antibody against GFP, which recognizes YFP (Clontech), was used. .. Confluent monolayers of MDCK cells expressing the YFP-linked dog β1 subunit grown in 35-mm2 wells of a 6-well plate were rinsed twice with PBS containing 1 m m EDTA and incubated with PBS for 60 min at 37 °C in CO2 incubator.

    Article Title: Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart
    Article Snippet: For immunofluorescent staining, the following monoclonal antibodies were used: Na,K-ATPase α1 subunit (mouse, clone C464.6, 1:20; Millipore) and Na,K-ATPase β1 subunit (mouse, clone M17 P5 F11, 1:100; Affinity Bioreagents). .. For Western blotting analysis, the following monoclonal antibodies were used: against the Na,K-ATPase α1 subunit (mouse, clone C464.6, 1:1000; Millipore), against the Na,K-ATPase β2 subunit (mouse, clone 35; BD Transduction Laboratories), and Na,K-ATPase β3 subunit (goat, 1:500; Santa Cruz Biotechnology, Inc.).

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits
    Article Snippet: Paragraph title: Primary antibodies and western blot analysis ... The following monoclonal antibodies were used: GFP, clones 7.1 and 13.1, which also recognize YFP (dilution 1:1000; cat. no. 11814460001; Roche Diagnostics, Indianapolis, IN), Na,K-ATPase α1 subunit, clone C464.6 (dilution 1:2000; cat. no. 05-369; EMD Millipore, MA), Na,K-ATPase β1 subunit, clone M17-P5-F11 (dilution 1:1000; cat. no. MA3-930; Affinity Bioreagents, Golden, CO), Na,K-ATPase β1 subunit, clone 464.8 (dilution 1:1000; cat. no. NB300-147; Novus Biologicals, Littleton, CO), β1-integrin/CD29 (dilution 1:1000; cat. no. 610467; BD Transduction Laboratories, CA), Dysadherin, clone D-2 (dilution 1:500; cat. no. sc-166782; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), E-cadherin, clone 36 (dilution 1:1000; cat. no. 610181; BD Biosciences), HA (clone 16B12; dilution 1:1000; cat. no. 901502; Biolegend, San Diego, CA, USA) and HA, clone F-7 (dilution 1:500; cat. no. sc-7392; Santa Cruz Biotechnology).

    IA:

    Article Title: Human Breast Tumor Cells Are More Resistant to Cardiac Glycoside Toxicity Than Non-Tumorigenic Breast Cells
    Article Snippet: .. Antibody dilutions used for immunoblotting were as follows: 1:10,000 of mouse Na,K-ATPase anti-α1 or Na,K-ATPase β1 -subunit (Affinity Bioreagents, Golden, CO), 1:1000 mouse anti-actin JLA20 (Developmental Studies Hybridoma Bank, Iowa City, IA), 1:1000 of either rabbit anti-total ERK1/2 or mouse anti-phospho-ERK1/2 (Santa Cruz, Dallas, TX), 1:1000 of mouse anti-p53 (Santa Cruz, Dallas, TX), 1:500 mouse anti-Src (Millipore, Billerica, MA). .. Peroxidase AffiniPure goat anti-mouse or goat anti-rabbit (Jackson Immunoresearch, West Grove, PA) secondary antibodies were diluted 1:5000.

    Staining:

    Article Title: Subunit Isoform Selectivity in Assembly of Na,K-ATPase ?-? Heterodimers *
    Article Snippet: .. For immunofluorescent staining, the monoclonal antibodies against the Na,K-ATPase α1 subunit, clone C464.6 (Millipore) and against the Na,K-ATPase β1 subunit, clone M17-P5-F11 (Affinity Bioreagents) and polyclonal antibodies against the Na,K-ATPase α2 subunit, (Millipore) and against the Na,K-ATPase β2 subunit (Millipore) were used. .. The polyclonal antibody against the Na,K-ATPase β1 subunit , which was a generous gift of Dr. W. James Ball, Jr. (University of Cincinnati), was used for Western blot analysis.

    Article Title: Selective Assembly of Na,K-ATPase α2β2 Heterodimers in the Heart
    Article Snippet: .. For immunofluorescent staining, the following monoclonal antibodies were used: Na,K-ATPase α1 subunit (mouse, clone C464.6, 1:20; Millipore) and Na,K-ATPase β1 subunit (mouse, clone M17 P5 F11, 1:100; Affinity Bioreagents). .. The polyclonal antibodies used were Na,K-ATPase α2 subunit (rabbit, 1:200; Millipore) and Na,K-ATPase β2 subunit (rabbit, 1:200; Millipore).

    SDS Page:

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits
    Article Snippet: The following monoclonal antibodies were used: GFP, clones 7.1 and 13.1, which also recognize YFP (dilution 1:1000; cat. no. 11814460001; Roche Diagnostics, Indianapolis, IN), Na,K-ATPase α1 subunit, clone C464.6 (dilution 1:2000; cat. no. 05-369; EMD Millipore, MA), Na,K-ATPase β1 subunit, clone M17-P5-F11 (dilution 1:1000; cat. no. MA3-930; Affinity Bioreagents, Golden, CO), Na,K-ATPase β1 subunit, clone 464.8 (dilution 1:1000; cat. no. NB300-147; Novus Biologicals, Littleton, CO), β1-integrin/CD29 (dilution 1:1000; cat. no. 610467; BD Transduction Laboratories, CA), Dysadherin, clone D-2 (dilution 1:500; cat. no. sc-166782; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), E-cadherin, clone 36 (dilution 1:1000; cat. no. 610181; BD Biosciences), HA (clone 16B12; dilution 1:1000; cat. no. 901502; Biolegend, San Diego, CA, USA) and HA, clone F-7 (dilution 1:500; cat. no. sc-7392; Santa Cruz Biotechnology). .. The following monoclonal antibodies were used: GFP, clones 7.1 and 13.1, which also recognize YFP (dilution 1:1000; cat. no. 11814460001; Roche Diagnostics, Indianapolis, IN), Na,K-ATPase α1 subunit, clone C464.6 (dilution 1:2000; cat. no. 05-369; EMD Millipore, MA), Na,K-ATPase β1 subunit, clone M17-P5-F11 (dilution 1:1000; cat. no. MA3-930; Affinity Bioreagents, Golden, CO), Na,K-ATPase β1 subunit, clone 464.8 (dilution 1:1000; cat. no. NB300-147; Novus Biologicals, Littleton, CO), β1-integrin/CD29 (dilution 1:1000; cat. no. 610467; BD Transduction Laboratories, CA), Dysadherin, clone D-2 (dilution 1:500; cat. no. sc-166782; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), E-cadherin, clone 36 (dilution 1:1000; cat. no. 610181; BD Biosciences), HA (clone 16B12; dilution 1:1000; cat. no. 901502; Biolegend, San Diego, CA, USA) and HA, clone F-7 (dilution 1:500; cat. no. sc-7392; Santa Cruz Biotechnology).

    Software:

    Article Title: The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell–cell trans-dimerization of Na,K-ATPase β1 subunits
    Article Snippet: The following monoclonal antibodies were used: GFP, clones 7.1 and 13.1, which also recognize YFP (dilution 1:1000; cat. no. 11814460001; Roche Diagnostics, Indianapolis, IN), Na,K-ATPase α1 subunit, clone C464.6 (dilution 1:2000; cat. no. 05-369; EMD Millipore, MA), Na,K-ATPase β1 subunit, clone M17-P5-F11 (dilution 1:1000; cat. no. MA3-930; Affinity Bioreagents, Golden, CO), Na,K-ATPase β1 subunit, clone 464.8 (dilution 1:1000; cat. no. NB300-147; Novus Biologicals, Littleton, CO), β1-integrin/CD29 (dilution 1:1000; cat. no. 610467; BD Transduction Laboratories, CA), Dysadherin, clone D-2 (dilution 1:500; cat. no. sc-166782; Santa Cruz Biotechnology, Inc., Santa Cruz, CA), E-cadherin, clone 36 (dilution 1:1000; cat. no. 610181; BD Biosciences), HA (clone 16B12; dilution 1:1000; cat. no. 901502; Biolegend, San Diego, CA, USA) and HA, clone F-7 (dilution 1:500; cat. no. sc-7392; Santa Cruz Biotechnology). .. Immunoblots were quantified by densitometry using Image J 1.46r (National Institutes of Health, Bethesda, MD) or Image Studio Software (LI-COR Inc., Lincoln, NE).

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    Thermo Fisher gene exp atp1b1 mm00437612 m1
    Real-time PCR analysis of mRNA levels of 2-cell embryos cultured for 48 h with AICAR. Cdx2 , Cdh1 , Aqp9 , <t>Atp1b1</t> , Atp1a1 , Actb , Tjp1 , Ocln and Gadd45a are shown. Significant differences between control and AICAR-treated embryos are signified by * P
    Gene Exp Atp1b1 Mm00437612 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gene exp atp1b1 mm00437612 m1/product/Thermo Fisher
    Average 78 stars, based on 4 article reviews
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    gene exp atp1b1 mm00437612 m1 - by Bioz Stars, 2020-02
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    76
    Thermo Fisher anti na k atpase β1 subunit antibody
    Real-time PCR analysis of mRNA levels of 2-cell embryos cultured for 48 h with AICAR. Cdx2 , Cdh1 , Aqp9 , <t>Atp1b1</t> , Atp1a1 , Actb , Tjp1 , Ocln and Gadd45a are shown. Significant differences between control and AICAR-treated embryos are signified by * P
    Anti Na K Atpase β1 Subunit Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti na k atpase β1 subunit antibody - by Bioz Stars, 2020-02
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    Real-time PCR analysis of mRNA levels of 2-cell embryos cultured for 48 h with AICAR. Cdx2 , Cdh1 , Aqp9 , Atp1b1 , Atp1a1 , Actb , Tjp1 , Ocln and Gadd45a are shown. Significant differences between control and AICAR-treated embryos are signified by * P

    Journal: Molecular Human Reproduction

    Article Title: Treatment with AICAR inhibits blastocyst development, trophectoderm differentiation and tight junction formation and function in mice

    doi: 10.1093/molehr/gax050

    Figure Lengend Snippet: Real-time PCR analysis of mRNA levels of 2-cell embryos cultured for 48 h with AICAR. Cdx2 , Cdh1 , Aqp9 , Atp1b1 , Atp1a1 , Actb , Tjp1 , Ocln and Gadd45a are shown. Significant differences between control and AICAR-treated embryos are signified by * P

    Article Snippet: Commercially available TaqMan® Gene Expression Assays for Cdx2 (caudal homeobox domain 2, Mm01212880_m1), Cdh1 (E-cadherin, Mm00486918_m1), Aqp9 (aquaporin 9, Mm00508094_m1), Ocln (occludin, Mm00500912_m1), Tjp1 (tight junction protein 1, ZO1, Mm00493699_m1), Actb (beta actin, Mm01205647_g1), Gadd45a (growth arrest and DNA damage-inducible 45 alpha, Mm00432802_m1), Atp1b1 (Na+/K+ ATPase β1 subunit, Mm00437612_m1) and Atp1a1 ( Na+/K+ ATPase α1 subunit, Mm00523255_m1) were used to assess effects to mRNA transcript relative levels.

    Techniques: Real-time Polymerase Chain Reaction, Cell Culture

    Real-time PCR analysis of blastocyst mRNA levels at time 0, 9 h of treatment or 24 h of recovery. Cdx2 , Cdh1 , Aqp9 , Atp1b1 , Atp1a1 , Actb , Tjp1 , Ocln and Gadd45a are shown. Significant differences between control and AICAR-treated embryos are signified by a,b,c,d P

    Journal: Molecular Human Reproduction

    Article Title: Treatment with AICAR inhibits blastocyst development, trophectoderm differentiation and tight junction formation and function in mice

    doi: 10.1093/molehr/gax050

    Figure Lengend Snippet: Real-time PCR analysis of blastocyst mRNA levels at time 0, 9 h of treatment or 24 h of recovery. Cdx2 , Cdh1 , Aqp9 , Atp1b1 , Atp1a1 , Actb , Tjp1 , Ocln and Gadd45a are shown. Significant differences between control and AICAR-treated embryos are signified by a,b,c,d P

    Article Snippet: Commercially available TaqMan® Gene Expression Assays for Cdx2 (caudal homeobox domain 2, Mm01212880_m1), Cdh1 (E-cadherin, Mm00486918_m1), Aqp9 (aquaporin 9, Mm00508094_m1), Ocln (occludin, Mm00500912_m1), Tjp1 (tight junction protein 1, ZO1, Mm00493699_m1), Actb (beta actin, Mm01205647_g1), Gadd45a (growth arrest and DNA damage-inducible 45 alpha, Mm00432802_m1), Atp1b1 (Na+/K+ ATPase β1 subunit, Mm00437612_m1) and Atp1a1 ( Na+/K+ ATPase α1 subunit, Mm00523255_m1) were used to assess effects to mRNA transcript relative levels.

    Techniques: Real-time Polymerase Chain Reaction