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    Alomone Labs anti kv11 1
    Dominant-negative (DN)-Rab11B-green fluorescent protein (GFP) and Rab11B short hairpin (sh)RNA increases <t>WT-Kv11.1</t> and Bap31 colocalization. A : representative fluorescent images of cells coexpressing WT-Kv11.1 and Rab11B-GFP or DN-Rab11B-GFP immunostained
    Anti Kv11 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    94
    Alomone Labs anti kcnh2 herg antibody
    Dominant-negative (DN)-Rab11B-green fluorescent protein (GFP) and Rab11B short hairpin (sh)RNA increases <t>WT-Kv11.1</t> and Bap31 colocalization. A : representative fluorescent images of cells coexpressing WT-Kv11.1 and Rab11B-GFP or DN-Rab11B-GFP immunostained
    Anti Kcnh2 Herg Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti kcnh2 herg antibody/product/Alomone Labs
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    96
    Millipore anti potassium channel kv11 1 extracellular antibody produced in rabbit
    Representative microscopy images of HEK293 cells expressing <t>WT-Kv11.1</t> and H1153Y-Kv11.1. GFP fluorescence is shown in green. Anti-Kv11.1 extracellular immunostaining (Alexa 647 fluorescence) is shown in red. Overlapping immunostaining of red and green signals of similar intensities is shown as yellow, and the cell nuclei are labeled blue. The scale bar represents 100 µm at 20× magnification and 50 µM at 63× magnification.
    Anti Potassium Channel Kv11 1 Extracellular Antibody Produced In Rabbit, 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
    https://www.bioz.com/result/anti potassium channel kv11 1 extracellular antibody produced in rabbit/product/Millipore
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    Image Search Results


    Dominant-negative (DN)-Rab11B-green fluorescent protein (GFP) and Rab11B short hairpin (sh)RNA increases WT-Kv11.1 and Bap31 colocalization. A : representative fluorescent images of cells coexpressing WT-Kv11.1 and Rab11B-GFP or DN-Rab11B-GFP immunostained

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Pharmacological correction of long QT-linked mutations in KCNH2 (hERG) increases the trafficking of Kv11.1 channels stored in the transitional endoplasmic reticulum

    doi: 10.1152/ajpcell.00406.2012

    Figure Lengend Snippet: Dominant-negative (DN)-Rab11B-green fluorescent protein (GFP) and Rab11B short hairpin (sh)RNA increases WT-Kv11.1 and Bap31 colocalization. A : representative fluorescent images of cells coexpressing WT-Kv11.1 and Rab11B-GFP or DN-Rab11B-GFP immunostained

    Article Snippet: Cells not expressing Kv11.1 did not show any immunostaining with anti-Kv11.1 (data not shown) nor any of the secondary antibodies alone (data not shown).

    Techniques: Dominant Negative Mutation

    Pharmacological correction of Kv11.1 current ( I Kv11.1 ) occurs in cells treated with cycloheximide and after 30 min. A : representative I Kv11.1 traces recorded from cells expressing G601S in control conditions ( n = 8 cells) and after E-4031 treatment without

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Pharmacological correction of long QT-linked mutations in KCNH2 (hERG) increases the trafficking of Kv11.1 channels stored in the transitional endoplasmic reticulum

    doi: 10.1152/ajpcell.00406.2012

    Figure Lengend Snippet: Pharmacological correction of Kv11.1 current ( I Kv11.1 ) occurs in cells treated with cycloheximide and after 30 min. A : representative I Kv11.1 traces recorded from cells expressing G601S in control conditions ( n = 8 cells) and after E-4031 treatment without

    Article Snippet: Cells not expressing Kv11.1 did not show any immunostaining with anti-Kv11.1 (data not shown) nor any of the secondary antibodies alone (data not shown).

    Techniques: Expressing

    G601S and Bap31 show a similar sensitivity to brefeldin a (bfa) and nocodazole (noc). A – D : representative fluorescent images of cells expressing G601S immunostained with anti-Kv11.1 (red, first column), anti-Bap31 (green, second column), and anti-ERGIC-53

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Pharmacological correction of long QT-linked mutations in KCNH2 (hERG) increases the trafficking of Kv11.1 channels stored in the transitional endoplasmic reticulum

    doi: 10.1152/ajpcell.00406.2012

    Figure Lengend Snippet: G601S and Bap31 show a similar sensitivity to brefeldin a (bfa) and nocodazole (noc). A – D : representative fluorescent images of cells expressing G601S immunostained with anti-Kv11.1 (red, first column), anti-Bap31 (green, second column), and anti-ERGIC-53

    Article Snippet: Cells not expressing Kv11.1 did not show any immunostaining with anti-Kv11.1 (data not shown) nor any of the secondary antibodies alone (data not shown).

    Techniques: Expressing

    G601S selectively colocalizes with Bap31. Shown are representative fluorescent images of cells expressing wild-type (WT)-Kv11.1 or G601S immunostained with anti-Kv11.1 (red, first column) and anti-Derlin-1 ( A ), anti-Bap31 ( B ), anti-Sec31 ( C ), or anti-ERGIC-53

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Pharmacological correction of long QT-linked mutations in KCNH2 (hERG) increases the trafficking of Kv11.1 channels stored in the transitional endoplasmic reticulum

    doi: 10.1152/ajpcell.00406.2012

    Figure Lengend Snippet: G601S selectively colocalizes with Bap31. Shown are representative fluorescent images of cells expressing wild-type (WT)-Kv11.1 or G601S immunostained with anti-Kv11.1 (red, first column) and anti-Derlin-1 ( A ), anti-Bap31 ( B ), anti-Sec31 ( C ), or anti-ERGIC-53

    Article Snippet: Cells not expressing Kv11.1 did not show any immunostaining with anti-Kv11.1 (data not shown) nor any of the secondary antibodies alone (data not shown).

    Techniques: Expressing

    E-4031 treatment decreases G601S and Bap31 colocalization. A : representative fluorescent images of cells expressing G601S immunostained with anti-Kv11.1 (red, first column) and anti-Bap31 (green, second column) in control conditions ( n = 30 images) and

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Pharmacological correction of long QT-linked mutations in KCNH2 (hERG) increases the trafficking of Kv11.1 channels stored in the transitional endoplasmic reticulum

    doi: 10.1152/ajpcell.00406.2012

    Figure Lengend Snippet: E-4031 treatment decreases G601S and Bap31 colocalization. A : representative fluorescent images of cells expressing G601S immunostained with anti-Kv11.1 (red, first column) and anti-Bap31 (green, second column) in control conditions ( n = 30 images) and

    Article Snippet: Cells not expressing Kv11.1 did not show any immunostaining with anti-Kv11.1 (data not shown) nor any of the secondary antibodies alone (data not shown).

    Techniques: Expressing

    Pharmacological correction increases the terminal glycosylation of G601S in cells treated with cycloheximide. A : representative fluorescent images of cells expressing G601S immunostained with anti-Kv11.1 (red, first column) and anti-Bap31 (green, second

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Pharmacological correction of long QT-linked mutations in KCNH2 (hERG) increases the trafficking of Kv11.1 channels stored in the transitional endoplasmic reticulum

    doi: 10.1152/ajpcell.00406.2012

    Figure Lengend Snippet: Pharmacological correction increases the terminal glycosylation of G601S in cells treated with cycloheximide. A : representative fluorescent images of cells expressing G601S immunostained with anti-Kv11.1 (red, first column) and anti-Bap31 (green, second

    Article Snippet: Cells not expressing Kv11.1 did not show any immunostaining with anti-Kv11.1 (data not shown) nor any of the secondary antibodies alone (data not shown).

    Techniques: Expressing

    Representative microscopy images of HEK293 cells expressing WT-Kv11.1 and H1153Y-Kv11.1. GFP fluorescence is shown in green. Anti-Kv11.1 extracellular immunostaining (Alexa 647 fluorescence) is shown in red. Overlapping immunostaining of red and green signals of similar intensities is shown as yellow, and the cell nuclei are labeled blue. The scale bar represents 100 µm at 20× magnification and 50 µM at 63× magnification.

    Journal: International Journal of Molecular Sciences

    Article Title: H1153Y-KCNH2 Mutation Identified in a Sudden Arrhythmic Death Syndrome Case Alters Channel Gating

    doi: 10.3390/ijms22179235

    Figure Lengend Snippet: Representative microscopy images of HEK293 cells expressing WT-Kv11.1 and H1153Y-Kv11.1. GFP fluorescence is shown in green. Anti-Kv11.1 extracellular immunostaining (Alexa 647 fluorescence) is shown in red. Overlapping immunostaining of red and green signals of similar intensities is shown as yellow, and the cell nuclei are labeled blue. The scale bar represents 100 µm at 20× magnification and 50 µM at 63× magnification.

    Article Snippet: They were then incubated with rabbit anti-potassium channel Kv11.1 extracellular antibody (1:16; Sigma P0749; Sigma-Aldrich, Saint Louis, MO, USA) for 30 min at 4 °C, rinsed twice with PBS, and incubated with goat anti-rabbit antibody conjugated to Alexa Fluor 647 (1:400; Abcam 150087, Cambridge, UK) for 30 min at 4 °C.

    Techniques: Microscopy, Expressing, Fluorescence, Immunostaining, Labeling

    Trafficking phenotype of WT-Kv11.1 and H1153-Kv11.1 channel protein. ( A ) Representative Western blot analyses of HEK293 cells transiently transfected with pcDNA3.1-N-eGFP (control cells), WT-Kv11.1, or H1153-Kv11.1, with or without pK treatment (200 μg/mL, 30 min); Kv11.1 channel protein was detected with an anti-Kv11.1 antibody targeting intracellular domain. Kv11.1 WT and H1153 showed two bands corresponding to a mature complex-glycosylated 182 kDA Kv11.1 band (155 kD + 27 kDA of GFP) completely digested by pK and one band at slightly lower molecular weight (162 kD) resistant to pK cleavage corresponding to immature core-glycosylated Kv11.1 protein band. ( B – D ) Semi-quantification of mature ( B ) and immature proteins ( C ) in WT and H1153Y cells with and without pK. Total protein measured with stain-free method was used to normalize, n = 5 independent experiments (** ( p

    Journal: International Journal of Molecular Sciences

    Article Title: H1153Y-KCNH2 Mutation Identified in a Sudden Arrhythmic Death Syndrome Case Alters Channel Gating

    doi: 10.3390/ijms22179235

    Figure Lengend Snippet: Trafficking phenotype of WT-Kv11.1 and H1153-Kv11.1 channel protein. ( A ) Representative Western blot analyses of HEK293 cells transiently transfected with pcDNA3.1-N-eGFP (control cells), WT-Kv11.1, or H1153-Kv11.1, with or without pK treatment (200 μg/mL, 30 min); Kv11.1 channel protein was detected with an anti-Kv11.1 antibody targeting intracellular domain. Kv11.1 WT and H1153 showed two bands corresponding to a mature complex-glycosylated 182 kDA Kv11.1 band (155 kD + 27 kDA of GFP) completely digested by pK and one band at slightly lower molecular weight (162 kD) resistant to pK cleavage corresponding to immature core-glycosylated Kv11.1 protein band. ( B – D ) Semi-quantification of mature ( B ) and immature proteins ( C ) in WT and H1153Y cells with and without pK. Total protein measured with stain-free method was used to normalize, n = 5 independent experiments (** ( p

    Article Snippet: They were then incubated with rabbit anti-potassium channel Kv11.1 extracellular antibody (1:16; Sigma P0749; Sigma-Aldrich, Saint Louis, MO, USA) for 30 min at 4 °C, rinsed twice with PBS, and incubated with goat anti-rabbit antibody conjugated to Alexa Fluor 647 (1:400; Abcam 150087, Cambridge, UK) for 30 min at 4 °C.

    Techniques: Western Blot, Transfection, Molecular Weight, Staining

    Flow cytometry qualitative ( A ) and quantitative ( B , C ) assessment of WT-Kv11.1 and H1153-Kv11.1 channel expression. ( A ) Representative histograms for unstained cells (corresponding to non-transfected cells) and cells transiently transfected with WT-Kv11.1 and H153Y-Kv11.1 stained with antiKv11.1 conjugated antibody. ( B ) Quantification of surface Kv11.1 channel (Alexia 647 fluorescence) for WT and H1153 variants in non-permeabilized cells. ( C ) Quantification of total Kv11.1 channel (GFP fused to the N-terminus of Kv11.1) for WT and H1153-Kv11.1 in non-permeabilized cells. The Median Kv11.1 Intensity of Fluorescence (MIF) represents the median of fluorescence intensity of 10,000 cells counted for each experiment ( p > 0.05). Each value represents the median+ S.E.M. of four independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: H1153Y-KCNH2 Mutation Identified in a Sudden Arrhythmic Death Syndrome Case Alters Channel Gating

    doi: 10.3390/ijms22179235

    Figure Lengend Snippet: Flow cytometry qualitative ( A ) and quantitative ( B , C ) assessment of WT-Kv11.1 and H1153-Kv11.1 channel expression. ( A ) Representative histograms for unstained cells (corresponding to non-transfected cells) and cells transiently transfected with WT-Kv11.1 and H153Y-Kv11.1 stained with antiKv11.1 conjugated antibody. ( B ) Quantification of surface Kv11.1 channel (Alexia 647 fluorescence) for WT and H1153 variants in non-permeabilized cells. ( C ) Quantification of total Kv11.1 channel (GFP fused to the N-terminus of Kv11.1) for WT and H1153-Kv11.1 in non-permeabilized cells. The Median Kv11.1 Intensity of Fluorescence (MIF) represents the median of fluorescence intensity of 10,000 cells counted for each experiment ( p > 0.05). Each value represents the median+ S.E.M. of four independent experiments.

    Article Snippet: They were then incubated with rabbit anti-potassium channel Kv11.1 extracellular antibody (1:16; Sigma P0749; Sigma-Aldrich, Saint Louis, MO, USA) for 30 min at 4 °C, rinsed twice with PBS, and incubated with goat anti-rabbit antibody conjugated to Alexa Fluor 647 (1:400; Abcam 150087, Cambridge, UK) for 30 min at 4 °C.

    Techniques: Flow Cytometry, Expressing, Transfection, Staining, Fluorescence

    Molecular position of the KCNH2 H1153Y variant (NM_0002383; rs 199473035) detected using the Ion torrent TM PGM platform and confirmed with Sanger sequencing. ( A ) The reads of NGS sequencing and the DNA sequence chromatogram illustrate the heterozygous c:3457C > T nucleotide substitution that results in the substitution of a Histidine-H (positively charged amino acid) for a Tyrosine-Y (polar uncharged amino acid) at amino acid residue 1153. ( B ) Cartoon of one Kv11.1 channel subunit. The circle denotes the approximate location of the p.H1153Y variant in the C-term region.

    Journal: International Journal of Molecular Sciences

    Article Title: H1153Y-KCNH2 Mutation Identified in a Sudden Arrhythmic Death Syndrome Case Alters Channel Gating

    doi: 10.3390/ijms22179235

    Figure Lengend Snippet: Molecular position of the KCNH2 H1153Y variant (NM_0002383; rs 199473035) detected using the Ion torrent TM PGM platform and confirmed with Sanger sequencing. ( A ) The reads of NGS sequencing and the DNA sequence chromatogram illustrate the heterozygous c:3457C > T nucleotide substitution that results in the substitution of a Histidine-H (positively charged amino acid) for a Tyrosine-Y (polar uncharged amino acid) at amino acid residue 1153. ( B ) Cartoon of one Kv11.1 channel subunit. The circle denotes the approximate location of the p.H1153Y variant in the C-term region.

    Article Snippet: They were then incubated with rabbit anti-potassium channel Kv11.1 extracellular antibody (1:16; Sigma P0749; Sigma-Aldrich, Saint Louis, MO, USA) for 30 min at 4 °C, rinsed twice with PBS, and incubated with goat anti-rabbit antibody conjugated to Alexa Fluor 647 (1:400; Abcam 150087, Cambridge, UK) for 30 min at 4 °C.

    Techniques: Variant Assay, Sequencing, Next-Generation Sequencing