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  • 93
    Alomone Labs anti aqp2
    Anti Aqp2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti aqp2/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti aqp2 - by Bioz Stars, 2022-10
    93/100 stars
      Buy from Supplier

    93
    Alomone Labs anti aqp2 antibody
    Mass spectrometry analysis of synthetic peptides corresponding to the COOH-terminal tail of human <t>AQP2</t> did not detect any significant phosphorylation of the water channel by AMPK. Protease-treated peptides (trypsin or LysC) or full-length peptides are indicated with bold underlined amino acids, indicating where phosphorylation was detected. The no. in parentheses indicates the adjusted spectral count of that particular phosphorylation site. The adjusted spectral count is obtained by multiplying the spectral count of each site with its phosphorylated probability reported by PhosphoRS. The last column indicates the percent sequence coverage. SAMS peptide was used as a positive control.
    Anti Aqp2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti aqp2 antibody/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti aqp2 antibody - by Bioz Stars, 2022-10
    93/100 stars
      Buy from Supplier

    Image Search Results


    Mass spectrometry analysis of synthetic peptides corresponding to the COOH-terminal tail of human AQP2 did not detect any significant phosphorylation of the water channel by AMPK. Protease-treated peptides (trypsin or LysC) or full-length peptides are indicated with bold underlined amino acids, indicating where phosphorylation was detected. The no. in parentheses indicates the adjusted spectral count of that particular phosphorylation site. The adjusted spectral count is obtained by multiplying the spectral count of each site with its phosphorylated probability reported by PhosphoRS. The last column indicates the percent sequence coverage. SAMS peptide was used as a positive control.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Activation of the metabolic sensor AMP-activated protein kinase inhibits aquaporin-2 function in kidney principal cells

    doi: 10.1152/ajprenal.00308.2016

    Figure Lengend Snippet: Mass spectrometry analysis of synthetic peptides corresponding to the COOH-terminal tail of human AQP2 did not detect any significant phosphorylation of the water channel by AMPK. Protease-treated peptides (trypsin or LysC) or full-length peptides are indicated with bold underlined amino acids, indicating where phosphorylation was detected. The no. in parentheses indicates the adjusted spectral count of that particular phosphorylation site. The adjusted spectral count is obtained by multiplying the spectral count of each site with its phosphorylated probability reported by PhosphoRS. The last column indicates the percent sequence coverage. SAMS peptide was used as a positive control.

    Article Snippet: After each incubation of the membrane with a particular anti-phospho COOH-terminal antibody, the nitrocellulose membrane was stripped and reblotted using anti-AQP2 antibody (Alomone Labs).

    Techniques: Mass Spectrometry, Sequencing, Positive Control

    AMPK activator AICAR prevents apical membrane accumulation of AQP2. Polarized mpkCCD c14 cells were treated with vehicle (DMSO) or the AMPK activator AICAR (1 mM) for 4 h and then 10 μM forskolin (vs. vehicle) for the last 2 h before cell harvesting. 5% of the cell lysates were used for immunoblotting using antibodies against AQP2 or actin as a loading control. The rest of the lysates were affinity purified using streptavidin followed by immunoblotting. A : representative immunoblots of 3 separate surface biotinylation experiments are shown. B : summary densitometric data comparing the mean (±SE) amounts of apical AQP2 as a percentage of that in the control condition for nonglycosylated (solid bars), core glycosylated (open bars), and fully glycosylated (shaded bars) forms of AQP2 are shown. Nonglycosylated: * P

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Activation of the metabolic sensor AMP-activated protein kinase inhibits aquaporin-2 function in kidney principal cells

    doi: 10.1152/ajprenal.00308.2016

    Figure Lengend Snippet: AMPK activator AICAR prevents apical membrane accumulation of AQP2. Polarized mpkCCD c14 cells were treated with vehicle (DMSO) or the AMPK activator AICAR (1 mM) for 4 h and then 10 μM forskolin (vs. vehicle) for the last 2 h before cell harvesting. 5% of the cell lysates were used for immunoblotting using antibodies against AQP2 or actin as a loading control. The rest of the lysates were affinity purified using streptavidin followed by immunoblotting. A : representative immunoblots of 3 separate surface biotinylation experiments are shown. B : summary densitometric data comparing the mean (±SE) amounts of apical AQP2 as a percentage of that in the control condition for nonglycosylated (solid bars), core glycosylated (open bars), and fully glycosylated (shaded bars) forms of AQP2 are shown. Nonglycosylated: * P

    Article Snippet: After each incubation of the membrane with a particular anti-phospho COOH-terminal antibody, the nitrocellulose membrane was stripped and reblotted using anti-AQP2 antibody (Alomone Labs).

    Techniques: Cell Harvesting, Affinity Purification, Western Blot

    AMPK activator AICAR induces intracellular redistribution of AQP2 in ex vivo kidney slices. A : confocal images of AQP2 immunofluorescence labeling (green) in kidney slices incubated in Ringer buffer alone for 75 min display an apical distribution of the water channel. Asterisks indicate the position of the lumen of the collecting ducts. B : addition of 1 mM AICAR for 75 min induced a cytosolic distribution of AQP2. C : incubation of kidney slices with dDAVP for the last 15 min of a 75-min incubation revealed apical accumulation of AQP2. D : however, preincubation of slices with AICAR did not prevent the dDAVP-induced apical accumulation of AQP2. E : regions of interest (ROIs; example shown in A ). Quantification of the mean (±SE) AQP2-associated mean pixel intensity (MPI) of apical-to-cytoplasmic ratio [arbitrary units (AU)] relative to that of cells measured under the control condition was used as a measure of apical AQP2 accumulation. Additional incubations of kidney slices in Ringer buffer were performed in the absence ( F ) or presence ( G ) of the PKA inhibitor myristoylated protein kinase inhibitor (mPKI; 10 μM) for 75 min. H : the relative AQP2 mean pixel intensity apical-to-cytoplasmic ratio was reduced dramatically with mPKI treatment. Data were obtained from at least 3 separate kidney slice experiments, using kidneys from at least 3 animals, and measuring a total of at least 30 cells per condition. * P

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Activation of the metabolic sensor AMP-activated protein kinase inhibits aquaporin-2 function in kidney principal cells

    doi: 10.1152/ajprenal.00308.2016

    Figure Lengend Snippet: AMPK activator AICAR induces intracellular redistribution of AQP2 in ex vivo kidney slices. A : confocal images of AQP2 immunofluorescence labeling (green) in kidney slices incubated in Ringer buffer alone for 75 min display an apical distribution of the water channel. Asterisks indicate the position of the lumen of the collecting ducts. B : addition of 1 mM AICAR for 75 min induced a cytosolic distribution of AQP2. C : incubation of kidney slices with dDAVP for the last 15 min of a 75-min incubation revealed apical accumulation of AQP2. D : however, preincubation of slices with AICAR did not prevent the dDAVP-induced apical accumulation of AQP2. E : regions of interest (ROIs; example shown in A ). Quantification of the mean (±SE) AQP2-associated mean pixel intensity (MPI) of apical-to-cytoplasmic ratio [arbitrary units (AU)] relative to that of cells measured under the control condition was used as a measure of apical AQP2 accumulation. Additional incubations of kidney slices in Ringer buffer were performed in the absence ( F ) or presence ( G ) of the PKA inhibitor myristoylated protein kinase inhibitor (mPKI; 10 μM) for 75 min. H : the relative AQP2 mean pixel intensity apical-to-cytoplasmic ratio was reduced dramatically with mPKI treatment. Data were obtained from at least 3 separate kidney slice experiments, using kidneys from at least 3 animals, and measuring a total of at least 30 cells per condition. * P

    Article Snippet: After each incubation of the membrane with a particular anti-phospho COOH-terminal antibody, the nitrocellulose membrane was stripped and reblotted using anti-AQP2 antibody (Alomone Labs).

    Techniques: Ex Vivo, Immunofluorescence, Labeling, Incubation

    AMPK inhibition promotes AQP2-mediated oocyte swelling and shortens time to lysis. Oocytes were microinjected with cRNAs for AQP2 and the different indicated AMPK constructs [WT-AMPK-α (●), dominant-negative (DN) AMPK-α1-K45R (■), and constitutively active (CA) AMPK-γ1-R70Q (▲)]. After 3 days, the oocytes were subjected to hypotonic shock in deionized water. Oocyte times to lysis were assessed by microscopy, and the mean times to lysis (normalized to that of the WT-AMPK-expressing group for each batch) are shown for all of the data obtained for these 3 groups. Oocytes expressing DN-AMPK had a significantly reduced time to lysis relative to each of the other two groups. * P

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Activation of the metabolic sensor AMP-activated protein kinase inhibits aquaporin-2 function in kidney principal cells

    doi: 10.1152/ajprenal.00308.2016

    Figure Lengend Snippet: AMPK inhibition promotes AQP2-mediated oocyte swelling and shortens time to lysis. Oocytes were microinjected with cRNAs for AQP2 and the different indicated AMPK constructs [WT-AMPK-α (●), dominant-negative (DN) AMPK-α1-K45R (■), and constitutively active (CA) AMPK-γ1-R70Q (▲)]. After 3 days, the oocytes were subjected to hypotonic shock in deionized water. Oocyte times to lysis were assessed by microscopy, and the mean times to lysis (normalized to that of the WT-AMPK-expressing group for each batch) are shown for all of the data obtained for these 3 groups. Oocytes expressing DN-AMPK had a significantly reduced time to lysis relative to each of the other two groups. * P

    Article Snippet: After each incubation of the membrane with a particular anti-phospho COOH-terminal antibody, the nitrocellulose membrane was stripped and reblotted using anti-AQP2 antibody (Alomone Labs).

    Techniques: Inhibition, Lysis, Construct, Dominant Negative Mutation, Microscopy, Expressing

    AMPK fails to significantly phosphorylate AQP2 in vitro. V5-tagged AQP2 was expressed in HEK-293 cells, immunoprecipitated, and incubated with [γ- 32 P]ATP in the presence of PKA catalytic subunit (positive control) or in the presence or absence of AMPK holoenzyme. A phosphoscreen image ( top ) and immunoblot ( bottom ) of the same membrane are shown (representative of 4 experiments). AQP2 gets robustly phosphorylated in the presence of PKA, but only weakly phosphorylated in the presence of AMPK ( top ). PKA catalytic subunit and the AMPK β-subunit get autophosphorylated, as indicated. The immunoblot ( bottom ) reveals similar AQP2 loading in all lanes.

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Activation of the metabolic sensor AMP-activated protein kinase inhibits aquaporin-2 function in kidney principal cells

    doi: 10.1152/ajprenal.00308.2016

    Figure Lengend Snippet: AMPK fails to significantly phosphorylate AQP2 in vitro. V5-tagged AQP2 was expressed in HEK-293 cells, immunoprecipitated, and incubated with [γ- 32 P]ATP in the presence of PKA catalytic subunit (positive control) or in the presence or absence of AMPK holoenzyme. A phosphoscreen image ( top ) and immunoblot ( bottom ) of the same membrane are shown (representative of 4 experiments). AQP2 gets robustly phosphorylated in the presence of PKA, but only weakly phosphorylated in the presence of AMPK ( top ). PKA catalytic subunit and the AMPK β-subunit get autophosphorylated, as indicated. The immunoblot ( bottom ) reveals similar AQP2 loading in all lanes.

    Article Snippet: After each incubation of the membrane with a particular anti-phospho COOH-terminal antibody, the nitrocellulose membrane was stripped and reblotted using anti-AQP2 antibody (Alomone Labs).

    Techniques: In Vitro, Immunoprecipitation, Incubation, Positive Control

    Changes in AQP2 phosphorylation pattern following dDAVP treatment in the presence or absence of AMPK activator in mpkCCD c14 cells. Twenty-four hours posttransfection with wild-type AQP2 plasmid, cells were incubated in the presence or absence of AICAR (2 mM) for 4 h, and then dDAVP (10 nM) or vehicle was added for 30 min before cell harvesting. Immunoblot analysis of immunoprecipitated V5-AQP2 was performed using the corresponding rabbit polyclonal antibodies against phosphorylated AQP2 COOH-terminal sites: −S256, −S261, −S264, and −S269. To confirm successful immunoprecipitation, the membranes were reblotted using anti-AQP2 and anti-V5 antibodies coupled to HRP. A : representative set of immunoblots from these experiments using antibodies against AQP2 and its different COOH-terminal phosphorylation sites. B : quantification of AQP2 phosphorylation signal for different AQP2 COOH-terminal sites normalized for protein loading, as assessed by densitometry of the immunoblot. Values are means ± SE of 4 independent experiments. * P

    Journal: American Journal of Physiology - Renal Physiology

    Article Title: Activation of the metabolic sensor AMP-activated protein kinase inhibits aquaporin-2 function in kidney principal cells

    doi: 10.1152/ajprenal.00308.2016

    Figure Lengend Snippet: Changes in AQP2 phosphorylation pattern following dDAVP treatment in the presence or absence of AMPK activator in mpkCCD c14 cells. Twenty-four hours posttransfection with wild-type AQP2 plasmid, cells were incubated in the presence or absence of AICAR (2 mM) for 4 h, and then dDAVP (10 nM) or vehicle was added for 30 min before cell harvesting. Immunoblot analysis of immunoprecipitated V5-AQP2 was performed using the corresponding rabbit polyclonal antibodies against phosphorylated AQP2 COOH-terminal sites: −S256, −S261, −S264, and −S269. To confirm successful immunoprecipitation, the membranes were reblotted using anti-AQP2 and anti-V5 antibodies coupled to HRP. A : representative set of immunoblots from these experiments using antibodies against AQP2 and its different COOH-terminal phosphorylation sites. B : quantification of AQP2 phosphorylation signal for different AQP2 COOH-terminal sites normalized for protein loading, as assessed by densitometry of the immunoblot. Values are means ± SE of 4 independent experiments. * P

    Article Snippet: After each incubation of the membrane with a particular anti-phospho COOH-terminal antibody, the nitrocellulose membrane was stripped and reblotted using anti-AQP2 antibody (Alomone Labs).

    Techniques: Plasmid Preparation, Incubation, Cell Harvesting, Immunoprecipitation, Western Blot