sheep kidney na k atpase  (Millipore)


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    Structured Review

    Millipore sheep kidney na k atpase
    Stable expression of wild-type and mutant forms of rat α -1 subunit of Na+ /K+ <t>-ATPase</t> in OK cells
    Sheep Kidney Na K Atpase, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sheep kidney na k atpase/product/Millipore
    Average 78 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sheep kidney na k atpase - by Bioz Stars, 2020-02
    78/100 stars

    Related Products / Commonly Used Together

    na + /
    α -
    na + / k
    rat α -1 subunit
    α -1 subunit

    Images

    1) Product Images from "Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase"

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    Journal: The Biochemical journal

    doi: 10.1042/BJ20111398

    Stable expression of wild-type and mutant forms of rat α -1 subunit of Na+ /K+ -ATPase in OK cells
    Figure Legend Snippet: Stable expression of wild-type and mutant forms of rat α -1 subunit of Na+ /K+ -ATPase in OK cells

    Techniques Used: Expressing, Mutagenesis

    Relative effect of Ang II on the elution of plasma membrane protein containing Populations #1, #2 and #3 of Na + /K + -ATPase from rat α -1.wild-type (A), α -1.S11A/S18A (B) and α -1.S938A (C) cells
    Figure Legend Snippet: Relative effect of Ang II on the elution of plasma membrane protein containing Populations #1, #2 and #3 of Na + /K + -ATPase from rat α -1.wild-type (A), α -1.S11A/S18A (B) and α -1.S938A (C) cells

    Techniques Used:

    Three populations of Na+ /K+ -ATPase in plasma membranes of α -1.S11A/S18A and α -1.S938A cells
    Figure Legend Snippet: Three populations of Na+ /K+ -ATPase in plasma membranes of α -1.S11A/S18A and α -1.S938A cells

    Techniques Used:

    Phosphorylation of rat kidney Na + /K + -ATPase at Ser 18
    Figure Legend Snippet: Phosphorylation of rat kidney Na + /K + -ATPase at Ser 18

    Techniques Used:

    Phosphorylation of rat kidney Na + /K + -ATPase at Ser 11
    Figure Legend Snippet: Phosphorylation of rat kidney Na + /K + -ATPase at Ser 11

    Techniques Used:

    Phosphorylation of rat kidney Na + /K + -ATPase at Ser 938
    Figure Legend Snippet: Phosphorylation of rat kidney Na + /K + -ATPase at Ser 938

    Techniques Used:

    Elution from digoxin-affinity columns of plasma membrane protein containing Na + /K + -ATPase Populations #1 (fractions 1–9), #2 (fractions 10–18) and #3 (fractions 19–22) from control and Ang II-treated α -1.S11A/S18A cells
    Figure Legend Snippet: Elution from digoxin-affinity columns of plasma membrane protein containing Na + /K + -ATPase Populations #1 (fractions 1–9), #2 (fractions 10–18) and #3 (fractions 19–22) from control and Ang II-treated α -1.S11A/S18A cells

    Techniques Used:

    Related Articles

    Mutagenesis:

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase
    Article Snippet: Similarly, cells expressing either the wild-type rat α -1 subunit or the S938A mutant were pretreated ± 100 μ M IBMX (isobutylmethylxanthine) and ± 100 μ M H-89 for 30 min. .. Following the detection of phosphorylated forms of Na+/ K+ -ATPase α -1, the blots were stripped and reprobed for total Na+/ K+ -ATPase using either an antibody raised against the rat α -1 subunit of Na+/ K+ -ATPase (Cell Signaling Technology, catalogue number 3010) or to the α -1 subunit of sheep kidney Na+/ K+ -ATPase (Sigma, catalogue number M8-P1-A3).

    Expressing:

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase
    Article Snippet: Similarly, cells expressing either the wild-type rat α -1 subunit or the S938A mutant were pretreated ± 100 μ M IBMX (isobutylmethylxanthine) and ± 100 μ M H-89 for 30 min. .. Following the detection of phosphorylated forms of Na+/ K+ -ATPase α -1, the blots were stripped and reprobed for total Na+/ K+ -ATPase using either an antibody raised against the rat α -1 subunit of Na+/ K+ -ATPase (Cell Signaling Technology, catalogue number 3010) or to the α -1 subunit of sheep kidney Na+/ K+ -ATPase (Sigma, catalogue number M8-P1-A3).

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    Millipore mouse monoclonal anti na k atpase α1 antibody
    Down-regulation of <t>α1</t> <t>Na/K-ATPase</t> in prostate cancer cells. A , α1 expression patterns in paired human normal prostate tissue ( left ) and carcinoma ( right ). Human tissue arrays were immunostained with monoclonal antibody against α1
    Mouse Monoclonal Anti Na K Atpase α1 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal anti na k atpase α1 antibody/product/Millipore
    Average 90 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    mouse monoclonal anti na k atpase α1 antibody - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    90
    Millipore mouse monoclonal anti na k atpase α subunit antibody
    Down-regulation of <t>α1</t> <t>Na/K-ATPase</t> in prostate cancer cells. A , α1 expression patterns in paired human normal prostate tissue ( left ) and carcinoma ( right ). Human tissue arrays were immunostained with monoclonal antibody against α1
    Mouse Monoclonal Anti Na K Atpase α Subunit Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal anti na k atpase α subunit antibody/product/Millipore
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse monoclonal anti na k atpase α subunit antibody - by Bioz Stars, 2020-02
    90/100 stars
      Buy from Supplier

    Image Search Results


    Down-regulation of α1 Na/K-ATPase in prostate cancer cells. A , α1 expression patterns in paired human normal prostate tissue ( left ) and carcinoma ( right ). Human tissue arrays were immunostained with monoclonal antibody against α1

    Journal: The Journal of Biological Chemistry

    Article Title: Na/K-ATPase Mimetic pNaKtide Peptide Inhibits the Growth of Human Cancer Cells *

    doi: 10.1074/jbc.M110.207597

    Figure Lengend Snippet: Down-regulation of α1 Na/K-ATPase in prostate cancer cells. A , α1 expression patterns in paired human normal prostate tissue ( left ) and carcinoma ( right ). Human tissue arrays were immunostained with monoclonal antibody against α1

    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.

    Techniques: Expressing

    Decreases in surface expression of α1 Na/K-ATPase in prostate cancer cells. A , cellular distribution of α1 Na/K-ATPase. The fixed cells were immunostained with anti-α1 antibody and visualized (in red ) with a Leica DMIRE2 confocal

    Journal: The Journal of Biological Chemistry

    Article Title: Na/K-ATPase Mimetic pNaKtide Peptide Inhibits the Growth of Human Cancer Cells *

    doi: 10.1074/jbc.M110.207597

    Figure Lengend Snippet: Decreases in surface expression of α1 Na/K-ATPase in prostate cancer cells. A , cellular distribution of α1 Na/K-ATPase. The fixed cells were immunostained with anti-α1 antibody and visualized (in red ) with a Leica DMIRE2 confocal

    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.

    Techniques: Expressing

    Deglutathionylation of the Na,K-ATPase α1-subunit in the absence of denaturing reagents. ( A ) Deglutathionylation using the coupled en zyme system glutaredoxin (20.6 µg/mL) and glutathione reductase in the presence of 0.5 mM glutathione and 200 µM nicotinamide adenine dinucleotide phosphate (NADPH). Samples were incubated for 30 min at 37 °C. Control samples (taken as 100%) were incubated under the same conditions without reduced glutathione and the enzymes. The upper panel presents results of immunoblotting with staining by antibodies against bound glutathione and against Na,K-ATPase α1-subunit. The lower panel shows change in enzyme activity (number of experiments: N = 3); ( B ) Deglutathionylation using chemical reducing agents: 25 mM tris(2-carboxyethyl)-phosphine (TCEP), 10 mM Na 2 S 2 O 4 , and 3% NaBH 4 . The incubation time was 30 min at 37 °C. The upper panel depicts immunoblotting with staining by antibodies against bound glutathione and against the α1-subunit. The results were normalized to the α1-subunit content. Lower panel: change in Na,K-ATPase activity after treatment by reducing agents ( N = 4). Data are presented as mean ± standard deviation (SD) of independent experiments. * p

    Journal: Biomolecules

    Article Title: Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity

    doi: 10.3390/biom7010018

    Figure Lengend Snippet: Deglutathionylation of the Na,K-ATPase α1-subunit in the absence of denaturing reagents. ( A ) Deglutathionylation using the coupled en zyme system glutaredoxin (20.6 µg/mL) and glutathione reductase in the presence of 0.5 mM glutathione and 200 µM nicotinamide adenine dinucleotide phosphate (NADPH). Samples were incubated for 30 min at 37 °C. Control samples (taken as 100%) were incubated under the same conditions without reduced glutathione and the enzymes. The upper panel presents results of immunoblotting with staining by antibodies against bound glutathione and against Na,K-ATPase α1-subunit. The lower panel shows change in enzyme activity (number of experiments: N = 3); ( B ) Deglutathionylation using chemical reducing agents: 25 mM tris(2-carboxyethyl)-phosphine (TCEP), 10 mM Na 2 S 2 O 4 , and 3% NaBH 4 . The incubation time was 30 min at 37 °C. The upper panel depicts immunoblotting with staining by antibodies against bound glutathione and against the α1-subunit. The results were normalized to the α1-subunit content. Lower panel: change in Na,K-ATPase activity after treatment by reducing agents ( N = 4). Data are presented as mean ± standard deviation (SD) of independent experiments. * p

    Article Snippet: The membranes were then stripped, and mouse monoclonal antibody against Na,K-ATPase α1-subunit clone C464-6 (Upstate Millipore, Billerica, MA, USA) was applied to detect the total amount of α1-subunit, followed by horseradish peroxidase-conjugated secondary antibodies.

    Techniques: Incubation, Staining, Activity Assay, Standard Deviation

    Chemical modifications of the α1-subunit ( A – C ) and changes in Na,K-ATPase activity ( D ) after treatment of the enzyme by TCEP (25 mM) and sodium borohydride (3%). The Na,K-ATPase was incubated with or without reducing agent for 30 min at 37 °C. The left panel depicts immunoblotting with staining by antibodies against α1-subunit by antibodies against sulfenic acid (Cys-SOH), against all oxidized SH-groups (Cys-SOH, Cys-SO 2 H, Cys-SO 3 H), and against nitrosylated cysteine thiols (Cys-SNO). Diagrams representing densitometric analysis of immunoblots: ( A ) α1-subunit stained using antibodies against sulfenic acid (Cys-SOH); ( B ) α1-subunit stained using antibodies against all oxidized SH-groups (Cys-SOH, Cys-SO 2 H, Cys-SO 3 H); ( C ) α1-subunit stained using antibodies against S -nitrosylated cysteine thiols (Cys-SNO). The bars are normalized to the α1-subunit content stained by antibodies against α1-subunit after stripping (number of experiments: N = 3). Data are presented as means ± SD of independent experiments. * p

    Journal: Biomolecules

    Article Title: Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity

    doi: 10.3390/biom7010018

    Figure Lengend Snippet: Chemical modifications of the α1-subunit ( A – C ) and changes in Na,K-ATPase activity ( D ) after treatment of the enzyme by TCEP (25 mM) and sodium borohydride (3%). The Na,K-ATPase was incubated with or without reducing agent for 30 min at 37 °C. The left panel depicts immunoblotting with staining by antibodies against α1-subunit by antibodies against sulfenic acid (Cys-SOH), against all oxidized SH-groups (Cys-SOH, Cys-SO 2 H, Cys-SO 3 H), and against nitrosylated cysteine thiols (Cys-SNO). Diagrams representing densitometric analysis of immunoblots: ( A ) α1-subunit stained using antibodies against sulfenic acid (Cys-SOH); ( B ) α1-subunit stained using antibodies against all oxidized SH-groups (Cys-SOH, Cys-SO 2 H, Cys-SO 3 H); ( C ) α1-subunit stained using antibodies against S -nitrosylated cysteine thiols (Cys-SNO). The bars are normalized to the α1-subunit content stained by antibodies against α1-subunit after stripping (number of experiments: N = 3). Data are presented as means ± SD of independent experiments. * p

    Article Snippet: The membranes were then stripped, and mouse monoclonal antibody against Na,K-ATPase α1-subunit clone C464-6 (Upstate Millipore, Billerica, MA, USA) was applied to detect the total amount of α1-subunit, followed by horseradish peroxidase-conjugated secondary antibodies.

    Techniques: Activity Assay, Incubation, Staining, Western Blot, Stripping Membranes