na k atpase α1  (Millipore)


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    Structured Review

    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: 97/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Different roles of the cardiac Na+/Ca2+-exchanger in ouabain-induced inotropy, cell signaling, and hypertrophy"

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

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    doi: 10.1152/ajpheart.00462.2012

    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,
    Figure Legend 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,

    Techniques Used: 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 .
    Figure Legend 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 .

    Techniques Used:

    2) Product Images from "Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits"

    Article Title: Multiple myosin motors interact with sodium/potassium-ATPase alpha 1 subunits

    Journal: Molecular Brain

    doi: 10.1186/s13041-018-0388-1

    Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-myh9 antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + : Figure S13)
    Figure Legend Snippet: Multiple myosins co-immunoprecipitate recombinant Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with mCherry (In, lane 1) or Na + /K + -ATPase α1 tagged with mCherry in the C-terminus (In, lane 4; Na + /K + ATPase α1-mCherry) were precleared (PC) with mouse IgG2b antibodies ( a and b ; lanes 2 and 5) or mouse IgG1 antibodies ( c ; lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-myh9 antibodies of the IgG2b isotypes ( a ; lanes 3 and 6), mouse anti-myh10 antibodies of the IgG2b isotypes ( b ; lanes 3 and 6) or mouse anti-myoVI antibodies of the IgG1 isotypes ( c ; lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. mCherry immunoreactive bands in lanes 4 and 6 but not in any other lanes indicated co-immunoprecipitation of recombinant Na + /K + -ATPase α1 subunits by myh9 (lane 6, panel (i)), myh10 (lane 6, panel (iii)) and myoVI (lane 6, panel (v)) from HEK293 cells transfected with Na + /K + -ATPase α1-mCherry plasmids but not from those transfected with mCherry. As expected β-actin (lanes 3 and 6 in panels (ii)) was co-immunoprecipitated with myh9. Myh10 and myoVI noticeably co-immunoprecipitated β-actin (lane 6 in (iv) and (vi)) from HEK293 cells overexpressing Na + /K + : Figure S13)

    Techniques Used: Recombinant, Transfection, Immunoprecipitation

    Recombinant myh9 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with GFP (In, lane 1) or myh9 tagged with GFP in the C-terminus (In, lane 4; myh9-GFP) were precleared (PC) with mouse IgG1 antibodies ( a , lanes 2 and 5) or goat immunoglobulins (gIgG) ( b , lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-GFP antibodies of the IgG1 isotypes ( a , lanes 3 and 6) or goat anti-GFP antibodies ( b , lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4 and 6 but not in any other lanes ((i) and (iii)) indicated co-immunoprecipitation of Na + /K + -ATPase α1 subunits from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. As expected immunoprecipitation using anti-GFP antibodies led to the co-immunoprecipitation of β-actin (lane 6 in (ii) and (iv)) from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. Immunoprecipitation using goat anti-GFP antibodies ( b ) led to a cleaner co-IP of Na + /K + : Figure S3B (for part a : Figure S4B (for part b )
    Figure Legend Snippet: Recombinant myh9 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of HEK293 cells transiently transfected with GFP (In, lane 1) or myh9 tagged with GFP in the C-terminus (In, lane 4; myh9-GFP) were precleared (PC) with mouse IgG1 antibodies ( a , lanes 2 and 5) or goat immunoglobulins (gIgG) ( b , lanes 2 and 5) prior to immunoprecipitation (IP) using mouse anti-GFP antibodies of the IgG1 isotypes ( a , lanes 3 and 6) or goat anti-GFP antibodies ( b , lanes 3 and 6). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4 and 6 but not in any other lanes ((i) and (iii)) indicated co-immunoprecipitation of Na + /K + -ATPase α1 subunits from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. As expected immunoprecipitation using anti-GFP antibodies led to the co-immunoprecipitation of β-actin (lane 6 in (ii) and (iv)) from HEK293 cells transfected with myh9-GFP plasmids but not from those transfected with GFP plasmids. Immunoprecipitation using goat anti-GFP antibodies ( b ) led to a cleaner co-IP of Na + /K + : Figure S3B (for part a : Figure S4B (for part b )

    Techniques Used: Recombinant, Transfection, Immunoprecipitation, Co-Immunoprecipitation Assay

    Interaction of actin-binding-site-less (ΔABS) and tail-less (Δtail) NMHC-IIs with Na + /K + -ATPase α1 subunits expressed in HEK293 cells. a Tail-less NMHC-IIs were made by deleting the tail regions, yellow shaded, of human (h) myh9 (i.e., hMyh9 AAs: 1928–1960), human (h) myh10 isoform 2 (i.e., hMyh10.2 AAs: 1934–1976) and mouse (m) myh14 isoform 3 (i.e., mMyh14.3 AAs:1946–1992) following a conserved proline residue (bold and underlined) where the numbers indicate the position of the amino acids in the WT constructs. b Actin-binding-site-less (ΔABS) NMHC-IIs were made by deleting a 23 amino acids (AAs) segment, yellow shaded, of hMyh9 (i.e., AAs: 654–676), hMyh10.2 (i.e., AAs: 661–683) and mMyh14.3 (i.e., AAs: 674–696). For both ( a ) and ( b ) symbols below sequences indicate fully (*), strongly (:) or weakly (.) conserved residues, and the lack of a symbol indicates amino acid divergence. c ). Left panel shows the relative position of the ABS (red ribbon), nucleotide analog (adenosine diphosphate vanadate (ADP.VO4): ball and stick model) binding site and N-terminal SH3 domain (deep blue) in the motor domain of human myh14 (5I4E.pdb). The center and right panel show the relative position of the ABS (red ribbon; and ball and stick model) with respect to the position of the adenosine diphosphate vanadate (ADP.VO4) and magnesium co-factor (green ball) in the motor domain of myh14. d Tail-less (Δtail) but not actin-binding-site-less (ΔABS) myh14 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of non-transfected HEK293 cells (In; 1) or HEK293 cells transiently transfected with GFP (In; 4), myh14-GFP (In; 7), myh14-ΔABS-GFP (In; 10), or myh14-Δtail-GFP (In; 13) plasmids (where the GFP tag is in their C-terminus) were precleared with rabbit IgG (PC; lanes 2, 5, 8, 11 and 14) prior to immunoprecipitation using rabbit anti-GFP antibodies (IP; lanes 3, 6, 9, 12 and 15). Loading of PC complexes in the gel preceded those of the IP complexes. Presence of Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4, 7, 9, 10, 13 and 15 and absence of any Na + /K + -ATPase α1 immunoreactive bands in lanes 2, 3, 5, 6, 8, 11, 12 and 14 (in (i)) indicated co-immunoprecipitation of Na + /K + : Figure S6 B
    Figure Legend Snippet: Interaction of actin-binding-site-less (ΔABS) and tail-less (Δtail) NMHC-IIs with Na + /K + -ATPase α1 subunits expressed in HEK293 cells. a Tail-less NMHC-IIs were made by deleting the tail regions, yellow shaded, of human (h) myh9 (i.e., hMyh9 AAs: 1928–1960), human (h) myh10 isoform 2 (i.e., hMyh10.2 AAs: 1934–1976) and mouse (m) myh14 isoform 3 (i.e., mMyh14.3 AAs:1946–1992) following a conserved proline residue (bold and underlined) where the numbers indicate the position of the amino acids in the WT constructs. b Actin-binding-site-less (ΔABS) NMHC-IIs were made by deleting a 23 amino acids (AAs) segment, yellow shaded, of hMyh9 (i.e., AAs: 654–676), hMyh10.2 (i.e., AAs: 661–683) and mMyh14.3 (i.e., AAs: 674–696). For both ( a ) and ( b ) symbols below sequences indicate fully (*), strongly (:) or weakly (.) conserved residues, and the lack of a symbol indicates amino acid divergence. c ). Left panel shows the relative position of the ABS (red ribbon), nucleotide analog (adenosine diphosphate vanadate (ADP.VO4): ball and stick model) binding site and N-terminal SH3 domain (deep blue) in the motor domain of human myh14 (5I4E.pdb). The center and right panel show the relative position of the ABS (red ribbon; and ball and stick model) with respect to the position of the adenosine diphosphate vanadate (ADP.VO4) and magnesium co-factor (green ball) in the motor domain of myh14. d Tail-less (Δtail) but not actin-binding-site-less (ΔABS) myh14 co-immunoprecipitate Na + /K + -ATPase α1 subunits expressed in HEK293 cells. Lysates of non-transfected HEK293 cells (In; 1) or HEK293 cells transiently transfected with GFP (In; 4), myh14-GFP (In; 7), myh14-ΔABS-GFP (In; 10), or myh14-Δtail-GFP (In; 13) plasmids (where the GFP tag is in their C-terminus) were precleared with rabbit IgG (PC; lanes 2, 5, 8, 11 and 14) prior to immunoprecipitation using rabbit anti-GFP antibodies (IP; lanes 3, 6, 9, 12 and 15). Loading of PC complexes in the gel preceded those of the IP complexes. Presence of Na + /K + -ATPase α1 immunoreactive bands in lanes 1, 4, 7, 9, 10, 13 and 15 and absence of any Na + /K + -ATPase α1 immunoreactive bands in lanes 2, 3, 5, 6, 8, 11, 12 and 14 (in (i)) indicated co-immunoprecipitation of Na + /K + : Figure S6 B

    Techniques Used: Binding Assay, Atomic Absorption Spectroscopy, Construct, Transfection, Immunoprecipitation

    Interaction of multiple myosins with Na + /K + -ATPase α1 subunits expressed in rat brain. WT adult rat brain lysates (In, lane 1 in a and b ) were precleared (PC) with indicated immunoglobulin isotypes (PC; lane2 = mIgG2b, lane 6 = rIgG and lane 9 = mIgG1) prior to immunoprecipitation (IP) using indicated antibodies (IP; lane 3 = myh9, lane 4 = myh10, lane 5 = KIF5B, lane 7 = Myh14, lane 8 = myoVa and lane 10 = myoVI). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 subunits (i) were co-immunoprecipitated with myh9, myh10, KIF5B, myh14, myoVa and myoVI expressed in rat brain tissues. Co-immunoprecipitation of Na + /K + -ATPase α1 subunits by KIF5B served as a positive control. All the myosins assayed co-immunoprecipitated β-actin (ii). Denatured mouse IgG-HC (i.e., lanes 2–5, 9 and 10; panel (ii)), but not those of rabbit IgG (i.e., lanes 6–8) separated from their intact immunoglobulins (that is used for PC or IP) could be seen as this section was probed with mouse anti-β-actin antibodies
    Figure Legend Snippet: Interaction of multiple myosins with Na + /K + -ATPase α1 subunits expressed in rat brain. WT adult rat brain lysates (In, lane 1 in a and b ) were precleared (PC) with indicated immunoglobulin isotypes (PC; lane2 = mIgG2b, lane 6 = rIgG and lane 9 = mIgG1) prior to immunoprecipitation (IP) using indicated antibodies (IP; lane 3 = myh9, lane 4 = myh10, lane 5 = KIF5B, lane 7 = Myh14, lane 8 = myoVa and lane 10 = myoVI). Loading of PC complexes in the gel preceded those of the IP complexes. Na + /K + -ATPase α1 subunits (i) were co-immunoprecipitated with myh9, myh10, KIF5B, myh14, myoVa and myoVI expressed in rat brain tissues. Co-immunoprecipitation of Na + /K + -ATPase α1 subunits by KIF5B served as a positive control. All the myosins assayed co-immunoprecipitated β-actin (ii). Denatured mouse IgG-HC (i.e., lanes 2–5, 9 and 10; panel (ii)), but not those of rabbit IgG (i.e., lanes 6–8) separated from their intact immunoglobulins (that is used for PC or IP) could be seen as this section was probed with mouse anti-β-actin antibodies

    Techniques Used: Immunoprecipitation, Positive Control

    Na + /K + -ATPase α1 subunits co-immunoprecipitate multiple myosins expressed in adult rat brain. WT adult rat brain lysates (In, lane 2 in a , b and c ) were precleared (PC) with mouse IgG1 antibodies (PC, lane 1 in a , b and c ) prior to immunoprecipitation (IP) using mouse anti-Na + /K + -ATPase α1 antibodies of the IgG1 isotypes (IP, lane 3 in a , b and c ). Loading of PC complexes in the gel preceded those of the lysate inputs (In). Na + /K + -ATPase α1 subunits co-immunoprecipitated myh9 ( a (i)), myh10 ( b , (i)), myoVa ( c (i)), β-actin ((iii) in a , b and c ) and myosin regulatory light chain (MRLC) ((iv) in a , b and c ) from rat brain. An asterisk (‘*’; (iv) in a , b and c ) indicates lack of detection of the input signal for the MRLCs. As expected anti-Na + /K + -ATPase α1 antibodies immunoprecipitated Na + /K + -ATPase α1 subunits expressed in brain tissues ((ii) in a , b and c )
    Figure Legend Snippet: Na + /K + -ATPase α1 subunits co-immunoprecipitate multiple myosins expressed in adult rat brain. WT adult rat brain lysates (In, lane 2 in a , b and c ) were precleared (PC) with mouse IgG1 antibodies (PC, lane 1 in a , b and c ) prior to immunoprecipitation (IP) using mouse anti-Na + /K + -ATPase α1 antibodies of the IgG1 isotypes (IP, lane 3 in a , b and c ). Loading of PC complexes in the gel preceded those of the lysate inputs (In). Na + /K + -ATPase α1 subunits co-immunoprecipitated myh9 ( a (i)), myh10 ( b , (i)), myoVa ( c (i)), β-actin ((iii) in a , b and c ) and myosin regulatory light chain (MRLC) ((iv) in a , b and c ) from rat brain. An asterisk (‘*’; (iv) in a , b and c ) indicates lack of detection of the input signal for the MRLCs. As expected anti-Na + /K + -ATPase α1 antibodies immunoprecipitated Na + /K + -ATPase α1 subunits expressed in brain tissues ((ii) in a , b and c )

    Techniques Used: Immunoprecipitation

    Interaction of myosin Va (myoVa) and myosin VI (myoVI) with Na + /K + -ATPase α1 subunits endogenously expressed in HEK293 cells. HEK293 cell lysates (In, lane 1 in a and b ) were precleared (PC) with rabbit IgG ( a ) or mouse IgG1 ( b ) prior to immunoprecipitation (IP, lane 3) using antibodies for myoVa ( a ) or myoVI ( b ). Loading of PC complexes in the gel preceded those of the IP complexes. Immunoprecipitation of myoVI ( b (iii)), but not those of myoVa ( a (iii)), led to the co-immunoprecipitation of Na + /K + ATPase α1 subunits ((i) in a and b ) expressed in HEK293 cells. Neither myoVa nor myoVI co-immunoprecipitated β-actin ((ii) in a and b ) expressed in HEK293 cells. Denatured mouse IgG-HC and IgG-LC separated from their intact immunoglobulins (that is used for PC or IP) are seen in B as the blot sections were probed with mouse anti- Na + /K + ATPase α1 and anti-β-actin antibodies
    Figure Legend Snippet: Interaction of myosin Va (myoVa) and myosin VI (myoVI) with Na + /K + -ATPase α1 subunits endogenously expressed in HEK293 cells. HEK293 cell lysates (In, lane 1 in a and b ) were precleared (PC) with rabbit IgG ( a ) or mouse IgG1 ( b ) prior to immunoprecipitation (IP, lane 3) using antibodies for myoVa ( a ) or myoVI ( b ). Loading of PC complexes in the gel preceded those of the IP complexes. Immunoprecipitation of myoVI ( b (iii)), but not those of myoVa ( a (iii)), led to the co-immunoprecipitation of Na + /K + ATPase α1 subunits ((i) in a and b ) expressed in HEK293 cells. Neither myoVa nor myoVI co-immunoprecipitated β-actin ((ii) in a and b ) expressed in HEK293 cells. Denatured mouse IgG-HC and IgG-LC separated from their intact immunoglobulins (that is used for PC or IP) are seen in B as the blot sections were probed with mouse anti- Na + /K + ATPase α1 and anti-β-actin antibodies

    Techniques Used: Immunoprecipitation

    Interaction of non-muscle myosin heavy chains with Na + /K + -ATPase α1 subunits endogenously expressed in HEK293 cells. HEK293 cell lysates (In, lane 1 in a and b ) were precleared (PC) with mouse IgG2b (PC, lane 2 in a and b ) prior to immunoprecipitation (IP, lane 3) using antibodies for myh9 ( a ) and myh10 ( b ). Loading of PC complexes in the gel preceded those of the IP complexes. Immunoprecipitation of myh9 ( a ) and myh10 ( b ) led to the co-immunoprecipitation of Na + /K + ATPase α1 subunits ((i) in a and b ) and β-actin ((ii) in a and b ) expressed in HEK293 cells. Na + /K + -ATPase α1 and β-actin immunoreactive signals in the depleted supernatant lane (DS, lane 4 in a ) indicates that the ATPase survives the IP procedure. Denatured mouse IgG-HC and IgG-LC separated from their intact immunoglobulins (that is used for PC or IP) are seen in ( a and b ) as those blot sections were probed with mouse anti-β-actin antibodies
    Figure Legend Snippet: Interaction of non-muscle myosin heavy chains with Na + /K + -ATPase α1 subunits endogenously expressed in HEK293 cells. HEK293 cell lysates (In, lane 1 in a and b ) were precleared (PC) with mouse IgG2b (PC, lane 2 in a and b ) prior to immunoprecipitation (IP, lane 3) using antibodies for myh9 ( a ) and myh10 ( b ). Loading of PC complexes in the gel preceded those of the IP complexes. Immunoprecipitation of myh9 ( a ) and myh10 ( b ) led to the co-immunoprecipitation of Na + /K + ATPase α1 subunits ((i) in a and b ) and β-actin ((ii) in a and b ) expressed in HEK293 cells. Na + /K + -ATPase α1 and β-actin immunoreactive signals in the depleted supernatant lane (DS, lane 4 in a ) indicates that the ATPase survives the IP procedure. Denatured mouse IgG-HC and IgG-LC separated from their intact immunoglobulins (that is used for PC or IP) are seen in ( a and b ) as those blot sections were probed with mouse anti-β-actin antibodies

    Techniques Used: Immunoprecipitation

    3) Product Images from "New 99mTc-Labeled Digitoxigenin Derivative for Cancer Cell Identification"

    Article Title: New 99mTc-Labeled Digitoxigenin Derivative for Cancer Cell Identification

    Journal: ACS Omega

    doi: 10.1021/acsomega.9b03167

    Inhibition of Na + /K + -ATPase activity by DIG, DTPA, DTPA–DIG, and 99m Tc-DTPA–DIG tested at 0.1 μM. Effects of DIG, DTPA–DIG, and 99m Tc-DTPA–DIG on Na + /K + -ATPase activity were assayed with the Na + /K + -ATPase α1,2,3 subunit of the porcine cortex. Results indicated Na + /K + -ATPase inhibition by DIG, DTPA–DIG, and 99m Tc-DTPA–DIG. However, labeling solution, as well as DTPA alone, has no influence on the activity of Na + /K + -ATPase.
    Figure Legend Snippet: Inhibition of Na + /K + -ATPase activity by DIG, DTPA, DTPA–DIG, and 99m Tc-DTPA–DIG tested at 0.1 μM. Effects of DIG, DTPA–DIG, and 99m Tc-DTPA–DIG on Na + /K + -ATPase activity were assayed with the Na + /K + -ATPase α1,2,3 subunit of the porcine cortex. Results indicated Na + /K + -ATPase inhibition by DIG, DTPA–DIG, and 99m Tc-DTPA–DIG. However, labeling solution, as well as DTPA alone, has no influence on the activity of Na + /K + -ATPase.

    Techniques Used: Inhibition, Activity Assay, Labeling

    4) Product Images from "A new semisynthetic cardenolide analog 3β-[2-(1-amantadine)- 1-on-ethylamine]-digitoxigenin (AMANTADIG) affects G2/M cell cycle arrest and miRNA expression profiles and enhances proapoptotic survivin-2B expression in renal cell carcinoma cell lines"

    Article Title: A new semisynthetic cardenolide analog 3β-[2-(1-amantadine)- 1-on-ethylamine]-digitoxigenin (AMANTADIG) affects G2/M cell cycle arrest and miRNA expression profiles and enhances proapoptotic survivin-2B expression in renal cell carcinoma cell lines

    Journal: Oncotarget

    doi: 10.18632/oncotarget.14644

    Cytotoxicity effects of cardiac glycosides and inhibition of Na+/K+-ATPase in four RCC cell lines IC50 values for cytotoxicity and IC50 values for Na+/K+ - ATPase inhibition were related to each other after treatment of the four cell lines with the three cardiac glycosides (A) or only with AMANTADIG (B) .
    Figure Legend Snippet: Cytotoxicity effects of cardiac glycosides and inhibition of Na+/K+-ATPase in four RCC cell lines IC50 values for cytotoxicity and IC50 values for Na+/K+ - ATPase inhibition were related to each other after treatment of the four cell lines with the three cardiac glycosides (A) or only with AMANTADIG (B) .

    Techniques Used: Inhibition

    5) Product Images from "Long-term exposure to hypoxia inhibits tumor progression of lung cancer in rats and mice"

    Article Title: Long-term exposure to hypoxia inhibits tumor progression of lung cancer in rats and mice

    Journal: BMC Cancer

    doi: 10.1186/1471-2407-11-331

    Cell proliferation, apoptosis and Na+-K+ ATPase expression in lung cancer tumors. Immunohistochemistry was used to evaluate cell proliferation and apoptosis. Mitosis was analyzed in slides with H E stain. (A) Percent Ki67 positive cell number for cell proliferation; (B) Mitosis index and (C) Apoptosis. Left panel showing quantitative data and right panel showing representative micrographs. n = 5 for each group. Expression of Na + -K + ATPase α1 in lung cancer tumors and colon cancer tumors (D to F) : Proteins were isolated from the tumors and Western blot was performed for analysis of Na + -K + ATPase α1 expression. Expression of Na + -K + ATPase α1 in lung cancer tumor in rats (D) and in A549 cells and in the lung cancer tumor from hypoxia-pretreated A549 cells in mice (E). (F) Na + -K + ATPase α1 expression in colon cancer tumor in rats (F). n = 3 for each group. Upper panels show representative images and lower panels show quantitative data, setting normoxia as 1. *p
    Figure Legend Snippet: Cell proliferation, apoptosis and Na+-K+ ATPase expression in lung cancer tumors. Immunohistochemistry was used to evaluate cell proliferation and apoptosis. Mitosis was analyzed in slides with H E stain. (A) Percent Ki67 positive cell number for cell proliferation; (B) Mitosis index and (C) Apoptosis. Left panel showing quantitative data and right panel showing representative micrographs. n = 5 for each group. Expression of Na + -K + ATPase α1 in lung cancer tumors and colon cancer tumors (D to F) : Proteins were isolated from the tumors and Western blot was performed for analysis of Na + -K + ATPase α1 expression. Expression of Na + -K + ATPase α1 in lung cancer tumor in rats (D) and in A549 cells and in the lung cancer tumor from hypoxia-pretreated A549 cells in mice (E). (F) Na + -K + ATPase α1 expression in colon cancer tumor in rats (F). n = 3 for each group. Upper panels show representative images and lower panels show quantitative data, setting normoxia as 1. *p

    Techniques Used: Expressing, Immunohistochemistry, Staining, Isolation, Western Blot, Mouse Assay

    6) Product Images from "Ouabain prevents pathological cardiac hypertrophy and heart failure through activation of phosphoinositide 3-kinase α in mouse"

    Article Title: Ouabain prevents pathological cardiac hypertrophy and heart failure through activation of phosphoinositide 3-kinase α in mouse

    Journal: Cell & Bioscience

    doi: 10.1186/s13578-015-0053-7

    Schematic presentation of ouabain’s different growth-related effects on α1 and α2 isoforms of Na + /K + -ATPase in the mouse cardiomyocytes. a α2-isoform: activation by sub-inotropic ouabain concentrations (
    Figure Legend Snippet: Schematic presentation of ouabain’s different growth-related effects on α1 and α2 isoforms of Na + /K + -ATPase in the mouse cardiomyocytes. a α2-isoform: activation by sub-inotropic ouabain concentrations (

    Techniques Used: Activation Assay

    Effects of ouabain on TAC-induced changes on Na + /K + -ATPase (NKA) isoforms in Con and KO hearts after 8 weeks of surgery. a Representative blots ( top ) and quantitative data ( bottom ) of protein expression of NKA α1 and α2 in Con hearts; b representative blots ( top ) and quantitative data ( bottom ) of protein expression of NKA α1 and α2 in p85-KO hearts; c mRNA expression of NKA α2 in Con hearts and d mRNA expression of NKA α2 in KO hearts. n = 6 ~ 7, * P
    Figure Legend Snippet: Effects of ouabain on TAC-induced changes on Na + /K + -ATPase (NKA) isoforms in Con and KO hearts after 8 weeks of surgery. a Representative blots ( top ) and quantitative data ( bottom ) of protein expression of NKA α1 and α2 in Con hearts; b representative blots ( top ) and quantitative data ( bottom ) of protein expression of NKA α1 and α2 in p85-KO hearts; c mRNA expression of NKA α2 in Con hearts and d mRNA expression of NKA α2 in KO hearts. n = 6 ~ 7, * P

    Techniques Used: Expressing

    Comparison of ouabain-induced signaling in cultured cardiomyocytes from Con and p85-KO mice. a . Representative blots of Na + /K + -ATPase isoforms ( top ). GAPDH was used as a loading control. Quantitative data of expression of Na + /K + -ATPase isoforms (n = 6) ( bottom ); b . representative PI(3)P dots show the effect of ouabain (50 μM, 5 min) on PI3Kα and PI3Kγ lipid kinase activities in Con and p85-KO cardiomyocytes, vehicle (vehi) ( top ). Quantitative data of PI3K activity from the top. (n = 9, *P
    Figure Legend Snippet: Comparison of ouabain-induced signaling in cultured cardiomyocytes from Con and p85-KO mice. a . Representative blots of Na + /K + -ATPase isoforms ( top ). GAPDH was used as a loading control. Quantitative data of expression of Na + /K + -ATPase isoforms (n = 6) ( bottom ); b . representative PI(3)P dots show the effect of ouabain (50 μM, 5 min) on PI3Kα and PI3Kγ lipid kinase activities in Con and p85-KO cardiomyocytes, vehicle (vehi) ( top ). Quantitative data of PI3K activity from the top. (n = 9, *P

    Techniques Used: Cell Culture, Mouse Assay, Expressing, Activity Assay

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    Transduction:

    Article Title: Insulin regulates alveolar epithelial function by inducing Na+/K+-ATPase translocation to the plasma membrane in a process mediated by the action of Akt
    Article Snippet: .. The following mouse monoclonal antibodies were purchased: FLAG (Sigma-Aldrich), Na+ /K+ -ATPase α1 subunit (clone 464.6, Millipore), GFP (Santa Cruz Biotechnology), HA (Covance), V5 (Invitrogen) and Rab8 (Transduction Laboratories). .. Plasmids encoding WT-AS160 tagged with a FLAG epitope (FLAG-WT-AS160), AS160 with four of its six predicted Akt phosphorylation sites mutated to alanine (S318A, S588A, T642A and S751A; FLAG-4P-AS160) or AS160 with arginine 973 mutated to lysine (FLAG-R/K-AS160) were kind gifts from Gustav E. Lienhard (Dartmouth Medical School, Hanover, NH, USA) ( ; ).

    Immunohistochemistry:

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth
    Article Snippet: .. Antibody for IHC- mouse monoclonal anti- Na/K-ATPase α1 antibody (Millipore). .. Two independent investigators examined the staining intensity and scored each slide three times as defined: 0, absent; 1, weak; 2, moderate; 3, strong.

    Immunoprecipitation:

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth
    Article Snippet: .. Immunoprecipitation was performed by adding 5 µg of anti-Src (Millipore Cat# 05-184) antibody to 500 µg of cell lysate (1 µg/µl concentration) or 8 µg of anti-α1 Na/K-ATPase antibody (Millipore Cat# 06-520) to 800 µg of cell lysate (1 µg/µl concentration). .. For immunostaining antibodies used - anti-α1 Na/K-ATPase antibody (Millipore Cat# 05-369) and Alexa Fluor 488-conjugated anti-mouse secondary antibody.

    Concentration Assay:

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth
    Article Snippet: .. Immunoprecipitation was performed by adding 5 µg of anti-Src (Millipore Cat# 05-184) antibody to 500 µg of cell lysate (1 µg/µl concentration) or 8 µg of anti-α1 Na/K-ATPase antibody (Millipore Cat# 06-520) to 800 µg of cell lysate (1 µg/µl concentration). .. For immunostaining antibodies used - anti-α1 Na/K-ATPase antibody (Millipore Cat# 05-369) and Alexa Fluor 488-conjugated anti-mouse secondary antibody.

    Article Title: Na/K-ATPase Mimetic pNaKtide Peptide Inhibits the Growth of Human Cancer Cells *
    Article Snippet: .. Tissue sections were incubated with a mouse monoclonal anti-Na/K-ATPase α1 antibody (Millipore) solution (final concentration 3.3 ng/μl) for 1 h at room temperature. .. Slides were washed and then incubated with ImmPRESS Reagent anti-mouse Ig peroxidase (Vector Laboratories) for 1 h followed by incubation with DAB substrate solution (Dako Cytomation) for 5 min.

    Incubation:

    Article Title: Na/K-ATPase Mimetic pNaKtide Peptide Inhibits the Growth of Human Cancer Cells *
    Article Snippet: .. Tissue sections were incubated with a mouse monoclonal anti-Na/K-ATPase α1 antibody (Millipore) solution (final concentration 3.3 ng/μl) for 1 h at room temperature. .. Slides were washed and then incubated with ImmPRESS Reagent anti-mouse Ig peroxidase (Vector Laboratories) for 1 h followed by incubation with DAB substrate solution (Dako Cytomation) for 5 min.

    other:

    Article Title: Rac1 Activation Caused by Membrane Translocation of a Guanine Nucleotide Exchange Factor in Akt2-Mediated Insulin Signaling in Mouse Skeletal Muscle
    Article Snippet: Mouse monoclonal antibodies against α-tubulin (T9026) and Na+ /K+ -ATPase (A-277) were purchased from SIGMA-Aldrich (MO, USA).

    Article Title: Ctr1 Is an Apical Copper Transporter in Mammalian Intestinal Epithelial Cells in Vivo That Is Controlled at the Level of Protein Stability *
    Article Snippet: The anti-Na+ /K+ -ATPase α1 subunit antibody was purchased from Millipore (Temecula, CA).

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  • 96
    Millipore anti na k atpase α1
    Immunofluorescence staining of Na + /K + <t>-ATPase</t> <t>α1.</t> A , C : The corneal epithelium has a bottom-up decreasing gradient of expression of the Na + /K + -ATPase pumps (in red) from the basal layer toward the wing cells in both native corneas ( A ) and reconstructed corneas ( C ). B , D : Immunofluorescence staining of Na + /K + -ATPase α1 of the corneal endothelium in both native ( B ) and reconstructed corneas ( D ). Nuclei were counterstained with Hoechst (in blue). Bar, 10 µm.
    Anti Na K Atpase α1, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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
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    92
    Millipore polyclonal rabbit anti α1 na k atpase
    Y260 phosphorylation and Src- (a) Y260 phosphorylation in purified pig kidney <t>α1</t> <t>Na/K-ATPase</t> (2 µg) by Src (4.5 units) in presence of 2 mM Mg 2+ -ATP in 10 minutes. Representative blots are shown, n = 3. Control blots showing Src phosphorylation at Y418 and Y529 sites by Mg 2+ -ATP are shown. (b) Effects of PP2 (5 μM, 30 minutes) on tyrosine phosphorylation of α1 Na/K-ATPase in LLC-PK1 cells. A representative immunoblot is shown. n = 4–5. (c) Effects of Src family kinase knockout on Y260 phosphorylation. Cell lysates were prepared from Src, Yes, Fyn knockout SYF, and Src-rescued SYF cells. Representative blots are shown, n = 4. (d) Effects of ouabain on Y260 phosphorylation as a function of time in LLC-PK1 cells. **p
    Polyclonal Rabbit Anti α1 Na K Atpase, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Immunofluorescence staining of Na + /K + -ATPase α1. A , C : The corneal epithelium has a bottom-up decreasing gradient of expression of the Na + /K + -ATPase pumps (in red) from the basal layer toward the wing cells in both native corneas ( A ) and reconstructed corneas ( C ). B , D : Immunofluorescence staining of Na + /K + -ATPase α1 of the corneal endothelium in both native ( B ) and reconstructed corneas ( D ). Nuclei were counterstained with Hoechst (in blue). Bar, 10 µm.

    Journal: Molecular Vision

    Article Title: Reconstruction of a human cornea by the self-assembly approach of tissue engineering using the three native cell types

    doi:

    Figure Lengend Snippet: Immunofluorescence staining of Na + /K + -ATPase α1. A , C : The corneal epithelium has a bottom-up decreasing gradient of expression of the Na + /K + -ATPase pumps (in red) from the basal layer toward the wing cells in both native corneas ( A ) and reconstructed corneas ( C ). B , D : Immunofluorescence staining of Na + /K + -ATPase α1 of the corneal endothelium in both native ( B ) and reconstructed corneas ( D ). Nuclei were counterstained with Hoechst (in blue). Bar, 10 µm.

    Article Snippet: Primary antibodies used were: anti-keratin-AE3 (MP Biomedicals, Solon, OH), anti-keratin 3/12 (AE5; MP Biomedicals), anti-human collagen 1 (Calbiochem, Montreal, Quebec, Canada), anti-human collagen VII (Millipore, Nepean, Ontario, Canada), anti-laminin V chain γ2 (Millipore), anti-laminin (Sigma), anti-Na+ /K+ -ATPase α1 (clone C464.6; Millipore) and anti-ZO-1 (ZMD-436; Invitrogen, Burlington, Ontario, Canada).

    Techniques: Immunofluorescence, Staining, Expressing

    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:

    Y260 phosphorylation and Src- (a) Y260 phosphorylation in purified pig kidney α1 Na/K-ATPase (2 µg) by Src (4.5 units) in presence of 2 mM Mg 2+ -ATP in 10 minutes. Representative blots are shown, n = 3. Control blots showing Src phosphorylation at Y418 and Y529 sites by Mg 2+ -ATP are shown. (b) Effects of PP2 (5 μM, 30 minutes) on tyrosine phosphorylation of α1 Na/K-ATPase in LLC-PK1 cells. A representative immunoblot is shown. n = 4–5. (c) Effects of Src family kinase knockout on Y260 phosphorylation. Cell lysates were prepared from Src, Yes, Fyn knockout SYF, and Src-rescued SYF cells. Representative blots are shown, n = 4. (d) Effects of ouabain on Y260 phosphorylation as a function of time in LLC-PK1 cells. **p

    Journal: Scientific Reports

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth

    doi: 10.1038/s41598-018-29995-2

    Figure Lengend Snippet: Y260 phosphorylation and Src- (a) Y260 phosphorylation in purified pig kidney α1 Na/K-ATPase (2 µg) by Src (4.5 units) in presence of 2 mM Mg 2+ -ATP in 10 minutes. Representative blots are shown, n = 3. Control blots showing Src phosphorylation at Y418 and Y529 sites by Mg 2+ -ATP are shown. (b) Effects of PP2 (5 μM, 30 minutes) on tyrosine phosphorylation of α1 Na/K-ATPase in LLC-PK1 cells. A representative immunoblot is shown. n = 4–5. (c) Effects of Src family kinase knockout on Y260 phosphorylation. Cell lysates were prepared from Src, Yes, Fyn knockout SYF, and Src-rescued SYF cells. Representative blots are shown, n = 4. (d) Effects of ouabain on Y260 phosphorylation as a function of time in LLC-PK1 cells. **p

    Article Snippet: Monoclonal anti-Src (GD-11) antibody, polyclonal rabbit anti-α1 Na/K-ATPase (06-520), Protein-G-agarose beads for immunoprecipitation and PP2 -Millipore (Billerica, MA).

    Techniques: Purification, Knock-Out

    Schematic diagrams of α1 Na/K-ATPase-mediated Src regulation in normal and cancer cells. Established signaling pathways are denoted by solid black arrows and speculated signaling pathways are denoted by broken black arrows. NKA = Na/K-ATPase, Cav = Caveolin 1, FAK = Focal Adhesion Kinase, RTK = Receptor Tyrosine Kinase, PI3K = Phosphatidyl Inositol 3 Kinase, ROS = Reactive Oxygen Species, PLC = Phospholipase C, PKC = Protein Kinase C, PKM2 = Pyruvate Kinase isoenzyme M2, PDH = Pyruvate Dehydrogenase, ERK = Extracellular Regulatory Kinase. The circled letter P denotes phosphorylation and activation.

    Journal: Scientific Reports

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth

    doi: 10.1038/s41598-018-29995-2

    Figure Lengend Snippet: Schematic diagrams of α1 Na/K-ATPase-mediated Src regulation in normal and cancer cells. Established signaling pathways are denoted by solid black arrows and speculated signaling pathways are denoted by broken black arrows. NKA = Na/K-ATPase, Cav = Caveolin 1, FAK = Focal Adhesion Kinase, RTK = Receptor Tyrosine Kinase, PI3K = Phosphatidyl Inositol 3 Kinase, ROS = Reactive Oxygen Species, PLC = Phospholipase C, PKC = Protein Kinase C, PKM2 = Pyruvate Kinase isoenzyme M2, PDH = Pyruvate Dehydrogenase, ERK = Extracellular Regulatory Kinase. The circled letter P denotes phosphorylation and activation.

    Article Snippet: Monoclonal anti-Src (GD-11) antibody, polyclonal rabbit anti-α1 Na/K-ATPase (06-520), Protein-G-agarose beads for immunoprecipitation and PP2 -Millipore (Billerica, MA).

    Techniques: Planar Chromatography, Activation Assay

    Y260 phosphorylation and α1 Na/K-ATPase/Src interaction in human cancers- (a) Measurement of Y260 phosphorylation in cancer cell lines. Cell lysates from a panel of prostate (LNCAP, DU145, and PC3) and breast (MCF7, MDAMB231, and BT-20) cancer cell lines were compared with corresponding control cells (prostate RWPE1 and breast MCF10A), for Na/K-ATPase α1 expression and Y260 phosphorylation. **p

    Journal: Scientific Reports

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth

    doi: 10.1038/s41598-018-29995-2

    Figure Lengend Snippet: Y260 phosphorylation and α1 Na/K-ATPase/Src interaction in human cancers- (a) Measurement of Y260 phosphorylation in cancer cell lines. Cell lysates from a panel of prostate (LNCAP, DU145, and PC3) and breast (MCF7, MDAMB231, and BT-20) cancer cell lines were compared with corresponding control cells (prostate RWPE1 and breast MCF10A), for Na/K-ATPase α1 expression and Y260 phosphorylation. **p

    Article Snippet: Monoclonal anti-Src (GD-11) antibody, polyclonal rabbit anti-α1 Na/K-ATPase (06-520), Protein-G-agarose beads for immunoprecipitation and PP2 -Millipore (Billerica, MA).

    Techniques: Expressing

    Identification of Y260 in α1 Na/K-ATPase as the major Src binding site- (a) Comparison of Y260 containing sequences in second cytoplasmic domain (CD2) of different human Na/K-ATPase isoforms. (b) Interaction between CD2 and Src in different cell lines. Representative blots are shown, n = 3. (c) Effects of ouabain on ERK activation. *p

    Journal: Scientific Reports

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth

    doi: 10.1038/s41598-018-29995-2

    Figure Lengend Snippet: Identification of Y260 in α1 Na/K-ATPase as the major Src binding site- (a) Comparison of Y260 containing sequences in second cytoplasmic domain (CD2) of different human Na/K-ATPase isoforms. (b) Interaction between CD2 and Src in different cell lines. Representative blots are shown, n = 3. (c) Effects of ouabain on ERK activation. *p

    Article Snippet: Monoclonal anti-Src (GD-11) antibody, polyclonal rabbit anti-α1 Na/K-ATPase (06-520), Protein-G-agarose beads for immunoprecipitation and PP2 -Millipore (Billerica, MA).

    Techniques: Binding Assay, Activation Assay

    Measurement of α1 Na/K-ATPase expression in primary tumor and metastatic lesions- (a) The expression of α1 Na/K-ATPase in prostate cancer. Left panels show α1 expression patterns in paired human normal prostate tissue (left), carcinoma (middle) and bone metastasis (right). Human tissue arrays were immunostained with a α1 monoclonal antibody (in brown). Hematoxylin was used for counterstaining of cell nucleus (in blue). Quantitative data are shown on the right side. **p

    Journal: Scientific Reports

    Article Title: Na/K-ATPase Y260 Phosphorylation–mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth

    doi: 10.1038/s41598-018-29995-2

    Figure Lengend Snippet: Measurement of α1 Na/K-ATPase expression in primary tumor and metastatic lesions- (a) The expression of α1 Na/K-ATPase in prostate cancer. Left panels show α1 expression patterns in paired human normal prostate tissue (left), carcinoma (middle) and bone metastasis (right). Human tissue arrays were immunostained with a α1 monoclonal antibody (in brown). Hematoxylin was used for counterstaining of cell nucleus (in blue). Quantitative data are shown on the right side. **p

    Article Snippet: Monoclonal anti-Src (GD-11) antibody, polyclonal rabbit anti-α1 Na/K-ATPase (06-520), Protein-G-agarose beads for immunoprecipitation and PP2 -Millipore (Billerica, MA).

    Techniques: Expressing