anti hcn2 antibody  (Alomone Labs)


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    Alomone Labs anti hcn2 antibody
    Effect of chronic training on HCN1, KCN2 and HCN4 protein expression determined by immunocytochemical techniques in sedentary and trained dog. Bar diagram on top left indicates that the relative density of dog cardiomyocytes with HCN4 immunolabelling obtained from the trained group (n=30 cells/6 dogs) is significantly increased compared to that measured in the sedentary group (n=30 cells/6 dogs). Original immunofluorescent images are shown on the left . Bottom panels indicate lack of effect of chronic training on the relative density of dog cardiomyocytes with HCN1 and <t>HCN2</t> immunolabelling (n=30 – 30 cells/6 – 6 dogs for sedentary and trained groups, respectively). Figure 7–Source Data 1 Effect of chronic training on HCN4 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 2 Effect of chronic training on HCN1 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 3 Effect of chronic training on HCN2 protein expression determined by immunocytochemical technique in sedentary and trained dogs.
    Anti Hcn2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Cardiac electrophysiological remodeling associated with enhanced arrhythmia susceptibilty in a canine model of elite exercise"

    Article Title: Cardiac electrophysiological remodeling associated with enhanced arrhythmia susceptibilty in a canine model of elite exercise

    Journal: bioRxiv

    doi: 10.1101/2022.07.13.499876

    Effect of chronic training on HCN1, KCN2 and HCN4 protein expression determined by immunocytochemical techniques in sedentary and trained dog. Bar diagram on top left indicates that the relative density of dog cardiomyocytes with HCN4 immunolabelling obtained from the trained group (n=30 cells/6 dogs) is significantly increased compared to that measured in the sedentary group (n=30 cells/6 dogs). Original immunofluorescent images are shown on the left . Bottom panels indicate lack of effect of chronic training on the relative density of dog cardiomyocytes with HCN1 and HCN2 immunolabelling (n=30 – 30 cells/6 – 6 dogs for sedentary and trained groups, respectively). Figure 7–Source Data 1 Effect of chronic training on HCN4 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 2 Effect of chronic training on HCN1 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 3 Effect of chronic training on HCN2 protein expression determined by immunocytochemical technique in sedentary and trained dogs.
    Figure Legend Snippet: Effect of chronic training on HCN1, KCN2 and HCN4 protein expression determined by immunocytochemical techniques in sedentary and trained dog. Bar diagram on top left indicates that the relative density of dog cardiomyocytes with HCN4 immunolabelling obtained from the trained group (n=30 cells/6 dogs) is significantly increased compared to that measured in the sedentary group (n=30 cells/6 dogs). Original immunofluorescent images are shown on the left . Bottom panels indicate lack of effect of chronic training on the relative density of dog cardiomyocytes with HCN1 and HCN2 immunolabelling (n=30 – 30 cells/6 – 6 dogs for sedentary and trained groups, respectively). Figure 7–Source Data 1 Effect of chronic training on HCN4 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 2 Effect of chronic training on HCN1 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 3 Effect of chronic training on HCN2 protein expression determined by immunocytochemical technique in sedentary and trained dogs.

    Techniques Used: Expressing

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    Alomone Labs hcn2
    MTg-AMO as an improved AMO approach for miRNA target finding. ( A and B ) Western blot analysis of the protein levels of TGFBI, APC BCL2L11, <t>HCN2</t> and Cav1.2. For MTg-AMO 21/155/17 , human breast cancer MCF-7 cells were used and for MTg-AMO 1/133 , cultured neonatal rat ventricular myocytes were used. NC and NC MTg-AMO: negative control MTg-AMO. The relevant miRNA for each target mRNA is specified above the name of the target mRNA in western blot images. * P
    Hcn2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hcn2/product/Alomone Labs
    Average 94 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    hcn2 - by Bioz Stars, 2022-09
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      Buy from Supplier

    95
    Alomone Labs anti hcn2 antibody
    Effect of chronic training on HCN1, KCN2 and HCN4 protein expression determined by immunocytochemical techniques in sedentary and trained dog. Bar diagram on top left indicates that the relative density of dog cardiomyocytes with HCN4 immunolabelling obtained from the trained group (n=30 cells/6 dogs) is significantly increased compared to that measured in the sedentary group (n=30 cells/6 dogs). Original immunofluorescent images are shown on the left . Bottom panels indicate lack of effect of chronic training on the relative density of dog cardiomyocytes with HCN1 and <t>HCN2</t> immunolabelling (n=30 – 30 cells/6 – 6 dogs for sedentary and trained groups, respectively). Figure 7–Source Data 1 Effect of chronic training on HCN4 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 2 Effect of chronic training on HCN1 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 3 Effect of chronic training on HCN2 protein expression determined by immunocytochemical technique in sedentary and trained dogs.
    Anti Hcn2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti hcn2 antibody/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti hcn2 antibody - by Bioz Stars, 2022-09
    95/100 stars
      Buy from Supplier

    Image Search Results


    MTg-AMO as an improved AMO approach for miRNA target finding. ( A and B ) Western blot analysis of the protein levels of TGFBI, APC BCL2L11, HCN2 and Cav1.2. For MTg-AMO 21/155/17 , human breast cancer MCF-7 cells were used and for MTg-AMO 1/133 , cultured neonatal rat ventricular myocytes were used. NC and NC MTg-AMO: negative control MTg-AMO. The relevant miRNA for each target mRNA is specified above the name of the target mRNA in western blot images. * P

    Journal: Nucleic Acids Research

    Article Title: A single anti-microRNA antisense oligodeoxyribonucleotide (AMO) targeting multiple microRNAs offers an improved approach for microRNA interference

    doi: 10.1093/nar/gkn1053

    Figure Lengend Snippet: MTg-AMO as an improved AMO approach for miRNA target finding. ( A and B ) Western blot analysis of the protein levels of TGFBI, APC BCL2L11, HCN2 and Cav1.2. For MTg-AMO 21/155/17 , human breast cancer MCF-7 cells were used and for MTg-AMO 1/133 , cultured neonatal rat ventricular myocytes were used. NC and NC MTg-AMO: negative control MTg-AMO. The relevant miRNA for each target mRNA is specified above the name of the target mRNA in western blot images. * P

    Article Snippet: The sample was incubated overnight at 4°C with primary antibodies for TGFBI, APC and BCL2L11 (Santa Cruz), and for HCN2 and Cav1.2 (Alomone Labs).

    Techniques: Western Blot, Cell Culture, Negative Control

    Domains mediating the interaction of VAPB with HCN2. A ) Schematic illustration of a HCN subunit. The CNBD and some of the truncation constructs studied are indicated. B ) All truncation constructs exhibited a positive interaction, evident from growth on -LWHA dropout medium. C ) Representative current traces and the relative currents for different C-terminal deletions expressed alone or with VAPB. D ) Representative current traces and the relative current amplitudes for the N-terminal truncated NTK HCN2 expressed alone or with VAPB. E ) Relative current amplitudes of NTK HCN2 HA Ex (extracellular HA-tag) expressed alone or with VAPB. F ) Relative surface expression of NTK HCN2 HA Ex expressed alone or with VAPB analyzed as relative light units (RLUs). G ) Schematic illustration, representative traces, and currents of a HCN2 channel chimera with the N terminus of HCN4 ( HCN4-N HCN2) expressed alone or with VAPB. H ) Relative currents of HCN2 expressed alone or coexpressed with VAPB (1.7 ± 0.1), TM VAPB (1.6 ± 0.2), the MSP domain (MSP VAPB ), the MSP with half of the CC domain (MSP-CC 0.5 VAPB ), or with the complete CC domain (MSP-CC VAPB ). I , J ) Relative current amplitudes of HCN2 HA Ex expressed alone or with TM VAPB (1.3 ± 0.1) ( I ) and the respective changes in the relative surface membrane expression analyzed as RLUs, using a single cell chemiluminescence assay (TM VAPB 1.8 ± 0.2) ( J ). All data are presented as means ± sem . The number of experiments ( n ) is indicated in the respective bar graphs. N.s., not significant. * P

    Journal: The FASEB Journal

    Article Title: The VAMP-associated protein VAPB is required for cardiac and neuronal pacemaker channel function

    doi: 10.1096/fj.201800246R

    Figure Lengend Snippet: Domains mediating the interaction of VAPB with HCN2. A ) Schematic illustration of a HCN subunit. The CNBD and some of the truncation constructs studied are indicated. B ) All truncation constructs exhibited a positive interaction, evident from growth on -LWHA dropout medium. C ) Representative current traces and the relative currents for different C-terminal deletions expressed alone or with VAPB. D ) Representative current traces and the relative current amplitudes for the N-terminal truncated NTK HCN2 expressed alone or with VAPB. E ) Relative current amplitudes of NTK HCN2 HA Ex (extracellular HA-tag) expressed alone or with VAPB. F ) Relative surface expression of NTK HCN2 HA Ex expressed alone or with VAPB analyzed as relative light units (RLUs). G ) Schematic illustration, representative traces, and currents of a HCN2 channel chimera with the N terminus of HCN4 ( HCN4-N HCN2) expressed alone or with VAPB. H ) Relative currents of HCN2 expressed alone or coexpressed with VAPB (1.7 ± 0.1), TM VAPB (1.6 ± 0.2), the MSP domain (MSP VAPB ), the MSP with half of the CC domain (MSP-CC 0.5 VAPB ), or with the complete CC domain (MSP-CC VAPB ). I , J ) Relative current amplitudes of HCN2 HA Ex expressed alone or with TM VAPB (1.3 ± 0.1) ( I ) and the respective changes in the relative surface membrane expression analyzed as RLUs, using a single cell chemiluminescence assay (TM VAPB 1.8 ± 0.2) ( J ). All data are presented as means ± sem . The number of experiments ( n ) is indicated in the respective bar graphs. N.s., not significant. * P

    Article Snippet: Untagged HCN2 protein was detected with rabbit α-HCN2 antibody (APC-030, 1:300; Alomone Labs, Jerusalem, Israel) and peroxidase-conjugated goat α-rabbit IgG antibody (32460, 1:2000; Thermo Fisher Scientific) as the secondary antibody.

    Techniques: Construct, Expressing, Chemiluminescence Immunoassay

    VAPB determines surface expression and dendritic localization of HCN2. A ) Live cell imaging of HeLa cells transfected with an N-terminally EGFP-tagged HCN2 carrying an extracellular HA-epitope ( EGFP HCN2 HA Ex ) alone or cotransfected with VAPB or the TM segment of VAPB (TM VAPB ). B ) Chemiluminescence assays of fixed non-permeabilized HeLa cells, analyzing the surface expression as relative light units (RLUs) for EGFP HCN2 HA Ex alone and after cotransfection with VAPB (1.6 ± 0.1). Upper inset illustrates a representative control Western blot showing an unaltered HCN2 prote in expression. C ) Chemiluminescence surface expression assay as in B , but using TM VAPB (1.6 ± 0.1). D ) Immunocytochemistry of HA VAPB transfected cortical neurons. Endogenous HCN2 (green) is colocalizing (white) with HA VAPB (magenta) in the soma and dendrites. Anti–MAP2-staining illustrating an intact neuronal network and dendrites (blue). E ) Immunocytochemistry experiment as in D , but transfecting the ALS8 mutation HA VAPB P56S (magenta), leading to an aggregation of VAPB P56S in the soma of the neurons. Also, HCN2 fluorescence (green) was focused in the soma and dendritic localization was lost, despite an intact neuronal network (α-MAP2, blue). Scale bars, 20 µm ( A , D , E ). All data are presented as means ± sem . The number of experiments ( n ) is indicated in the respective bar graphs. ** P

    Journal: The FASEB Journal

    Article Title: The VAMP-associated protein VAPB is required for cardiac and neuronal pacemaker channel function

    doi: 10.1096/fj.201800246R

    Figure Lengend Snippet: VAPB determines surface expression and dendritic localization of HCN2. A ) Live cell imaging of HeLa cells transfected with an N-terminally EGFP-tagged HCN2 carrying an extracellular HA-epitope ( EGFP HCN2 HA Ex ) alone or cotransfected with VAPB or the TM segment of VAPB (TM VAPB ). B ) Chemiluminescence assays of fixed non-permeabilized HeLa cells, analyzing the surface expression as relative light units (RLUs) for EGFP HCN2 HA Ex alone and after cotransfection with VAPB (1.6 ± 0.1). Upper inset illustrates a representative control Western blot showing an unaltered HCN2 prote in expression. C ) Chemiluminescence surface expression assay as in B , but using TM VAPB (1.6 ± 0.1). D ) Immunocytochemistry of HA VAPB transfected cortical neurons. Endogenous HCN2 (green) is colocalizing (white) with HA VAPB (magenta) in the soma and dendrites. Anti–MAP2-staining illustrating an intact neuronal network and dendrites (blue). E ) Immunocytochemistry experiment as in D , but transfecting the ALS8 mutation HA VAPB P56S (magenta), leading to an aggregation of VAPB P56S in the soma of the neurons. Also, HCN2 fluorescence (green) was focused in the soma and dendritic localization was lost, despite an intact neuronal network (α-MAP2, blue). Scale bars, 20 µm ( A , D , E ). All data are presented as means ± sem . The number of experiments ( n ) is indicated in the respective bar graphs. ** P

    Article Snippet: Untagged HCN2 protein was detected with rabbit α-HCN2 antibody (APC-030, 1:300; Alomone Labs, Jerusalem, Israel) and peroxidase-conjugated goat α-rabbit IgG antibody (32460, 1:2000; Thermo Fisher Scientific) as the secondary antibody.

    Techniques: Expressing, Live Cell Imaging, Transfection, Cotransfection, Western Blot, Immunocytochemistry, Staining, Mutagenesis, Fluorescence

    Codistribution of VAPs with HCN2 and contribution to thalamic I h . A – E ), Distribution of HCN2, VAPB, and VAPA mRNA in mouse brain and spinal cord. ISH analysis of HCN2, VAPB, and VAPA using DIG-labeled riboprobes, revealing mRNA expression of VAPB in cortical areas ( A ), hippocampus ( B ), thalamus ( C ), cerebellum ( D ) (arrows point to interneurons in the granular layer), and spinal cord ( E ). Note the overlapping distribution of VAPB with HCN2 and VAPA mRNA. Am, amygdala; CA, cornu ammonis; DG, dentate gyrus; DH, dorsal horn; gcl, granule cell layer; Hb, habenulae; ic, internal capsule; LG, lateral geniculate ncl.; m, molecular cell layer; pcl, Purkinje cell layer; RTh, reticular thalamic ncl.; Sth, subthalamic ncl.; VB, ventrobasal thalamus; Th, thalamus; VH, ventral horn. F ) Representative current traces elicited in slice patch-clamp experiments of the ventrobasal thalamus (VB) of wild-type animals (control) and VAPB −/− mice. G ) The I h current was significantly reduced in VAPB −/− mice (15.4 ± 1.1 pA/pF) compared with control animals (22.2 ± 2.3 pA/pF). H ) Average activation curves of the VB I h current for control and VAPB −/− mice. V 1/2 of activation for control (−91.6 ± 1.3 mV, n = 8) and VAPB −/− (−87.5 ± 1.2 mV, n = 7). Scale bars: 500 µm ( A–C , E ), 100 µm ( D ). All data are presented as means ± sem . The number of experiments ( n ) is indicated in the respective bar graphs. * P

    Journal: The FASEB Journal

    Article Title: The VAMP-associated protein VAPB is required for cardiac and neuronal pacemaker channel function

    doi: 10.1096/fj.201800246R

    Figure Lengend Snippet: Codistribution of VAPs with HCN2 and contribution to thalamic I h . A – E ), Distribution of HCN2, VAPB, and VAPA mRNA in mouse brain and spinal cord. ISH analysis of HCN2, VAPB, and VAPA using DIG-labeled riboprobes, revealing mRNA expression of VAPB in cortical areas ( A ), hippocampus ( B ), thalamus ( C ), cerebellum ( D ) (arrows point to interneurons in the granular layer), and spinal cord ( E ). Note the overlapping distribution of VAPB with HCN2 and VAPA mRNA. Am, amygdala; CA, cornu ammonis; DG, dentate gyrus; DH, dorsal horn; gcl, granule cell layer; Hb, habenulae; ic, internal capsule; LG, lateral geniculate ncl.; m, molecular cell layer; pcl, Purkinje cell layer; RTh, reticular thalamic ncl.; Sth, subthalamic ncl.; VB, ventrobasal thalamus; Th, thalamus; VH, ventral horn. F ) Representative current traces elicited in slice patch-clamp experiments of the ventrobasal thalamus (VB) of wild-type animals (control) and VAPB −/− mice. G ) The I h current was significantly reduced in VAPB −/− mice (15.4 ± 1.1 pA/pF) compared with control animals (22.2 ± 2.3 pA/pF). H ) Average activation curves of the VB I h current for control and VAPB −/− mice. V 1/2 of activation for control (−91.6 ± 1.3 mV, n = 8) and VAPB −/− (−87.5 ± 1.2 mV, n = 7). Scale bars: 500 µm ( A–C , E ), 100 µm ( D ). All data are presented as means ± sem . The number of experiments ( n ) is indicated in the respective bar graphs. * P

    Article Snippet: Untagged HCN2 protein was detected with rabbit α-HCN2 antibody (APC-030, 1:300; Alomone Labs, Jerusalem, Israel) and peroxidase-conjugated goat α-rabbit IgG antibody (32460, 1:2000; Thermo Fisher Scientific) as the secondary antibody.

    Techniques: In Situ Hybridization, Labeling, Expressing, Patch Clamp, Mouse Assay, Activation Assay

    VAPB selectively increases HCN1 and HCN2 currents. A ) Y2H direct interaction assay. Transformation control (-LW), leucine, and tryptophan dropout. Interaction read-out (-LWHA), additional dropout of histidine and adenine. pAL-Alg5, positive control. pPR3-N, negative control. B ) Topology of VAPB. C ) GST VAPB pull-down of HCN2 EGFP using transfected HeLa cells. D ) GST VAPA, GST VAMP1, or GST VAMP2 pull-down of HCN2 EGFP using transfected HeLa cells. E ) GST VAPA pull-down of HCN2 and endogenous VAPB, using HCN2 EGFP transfected HeLa cells. F ) Pull-down of in vitro translated HCN2 (untagged). G ) Pull-down of HCN2 from rat brain lysates. H , I ) Representative currents ( H ) of HCN2 expressed in oocytes alone or with VAPB and the relative current amplitudes ( I ) analyzed over 3 d. J ) Relative currents of HCN1, HCN2, and HCN4 alone or coexpressed with VAPB. K , L ) Relative currents of different potassium channels ( K ) coexpressed with VAPB and of HCN2 ( L ) coexpressed with VAPA, VAPB, or VAPC. M ) Relative currents of HCN2 coexpressed with a mixture of VAPA/B (1:1). N ) Representative macropatch recordings in different configurations: on cell (o.c.), inside-out after patch excision (i.o.), and after application of 100 µM cAMP (i.o.+100 µM cAMP). O , P ) Activation curves for HCN2 alone ( n = 6) ( O ), recorded as in N , or after coexpression with VAPB ( n = 8) ( P ). Q ) V 1/2 values for HCN2 expressed alone or with VAPB in different patch modes. R ) Relative currents of HCN2 HA Ex alone or with VAPB. S ) Relative surface expression of HCN2 HA Ex expressed alone or with VAPB, analyzed as relative light units (RLUs). T ) Relative currents of HCN2 expressed alone or with VAPB or VAPB P56S . All data are presented as means ± sem . The number of cells ( n ) is indicated in the bar graphs. N.s., not significant. * P

    Journal: The FASEB Journal

    Article Title: The VAMP-associated protein VAPB is required for cardiac and neuronal pacemaker channel function

    doi: 10.1096/fj.201800246R

    Figure Lengend Snippet: VAPB selectively increases HCN1 and HCN2 currents. A ) Y2H direct interaction assay. Transformation control (-LW), leucine, and tryptophan dropout. Interaction read-out (-LWHA), additional dropout of histidine and adenine. pAL-Alg5, positive control. pPR3-N, negative control. B ) Topology of VAPB. C ) GST VAPB pull-down of HCN2 EGFP using transfected HeLa cells. D ) GST VAPA, GST VAMP1, or GST VAMP2 pull-down of HCN2 EGFP using transfected HeLa cells. E ) GST VAPA pull-down of HCN2 and endogenous VAPB, using HCN2 EGFP transfected HeLa cells. F ) Pull-down of in vitro translated HCN2 (untagged). G ) Pull-down of HCN2 from rat brain lysates. H , I ) Representative currents ( H ) of HCN2 expressed in oocytes alone or with VAPB and the relative current amplitudes ( I ) analyzed over 3 d. J ) Relative currents of HCN1, HCN2, and HCN4 alone or coexpressed with VAPB. K , L ) Relative currents of different potassium channels ( K ) coexpressed with VAPB and of HCN2 ( L ) coexpressed with VAPA, VAPB, or VAPC. M ) Relative currents of HCN2 coexpressed with a mixture of VAPA/B (1:1). N ) Representative macropatch recordings in different configurations: on cell (o.c.), inside-out after patch excision (i.o.), and after application of 100 µM cAMP (i.o.+100 µM cAMP). O , P ) Activation curves for HCN2 alone ( n = 6) ( O ), recorded as in N , or after coexpression with VAPB ( n = 8) ( P ). Q ) V 1/2 values for HCN2 expressed alone or with VAPB in different patch modes. R ) Relative currents of HCN2 HA Ex alone or with VAPB. S ) Relative surface expression of HCN2 HA Ex expressed alone or with VAPB, analyzed as relative light units (RLUs). T ) Relative currents of HCN2 expressed alone or with VAPB or VAPB P56S . All data are presented as means ± sem . The number of cells ( n ) is indicated in the bar graphs. N.s., not significant. * P

    Article Snippet: Untagged HCN2 protein was detected with rabbit α-HCN2 antibody (APC-030, 1:300; Alomone Labs, Jerusalem, Israel) and peroxidase-conjugated goat α-rabbit IgG antibody (32460, 1:2000; Thermo Fisher Scientific) as the secondary antibody.

    Techniques: Transformation Assay, Positive Control, Negative Control, Transfection, In Vitro, Activation Assay, Expressing

    Effect of over-expression of AC isoforms on HCN2 current. A . Original recordings of HCN2. The current was evoked by applying hyperpolarizing voltages from −25 to −85 mV for 5 seconds. B. Average fractional activation of measured HCN2 current. The solid lines are the fits to the Boltzmann function. AC1 activation relation differs from GFP and AC6 (p

    Journal: Journal of molecular and cellular cardiology

    Article Title: CA2+-ACTIVATED ADENYLYL CYCLASE 1 INTRODUCES CA2+-DEPENDENCE TO BETA-ADRENERGIC STIMULATION OF HCN2 CURRENT

    doi: 10.1016/j.yjmcc.2012.03.010

    Figure Lengend Snippet: Effect of over-expression of AC isoforms on HCN2 current. A . Original recordings of HCN2. The current was evoked by applying hyperpolarizing voltages from −25 to −85 mV for 5 seconds. B. Average fractional activation of measured HCN2 current. The solid lines are the fits to the Boltzmann function. AC1 activation relation differs from GFP and AC6 (p

    Article Snippet: To explore the possibility of direct interaction with HCN2 channels, we immunoprecipitated AC with anti-FLAG antibodies, separated the obtained proteins by PAGE and probed with anti-HCN2 antibodies ( ; middle panel).

    Techniques: Over Expression, Activation Assay

    A. Expression of recombinant adenylyl cyclase in NRVM. Cultures were co-infected with AdmHCN2 and one of the following: AdGFP, FLAG-tagged AdAC1 or FLAG-tagged AdAC6. 72 hours later cells were harvested, and the soluble membrane fraction was isolated. Soluble membranes from cultures infected with AdGFP, AdAC1 or AdAC6 were incubated with anti-FLAG or anti-HCN2 antibodies, separated by PAGE and probed with appropriate antibodies. B . Expression of endogenous HCN2 in NRVM and its co-immunoprecipitation with overexpressed adenylyl cyclases. The top panel shows detection of HCN2 in membrane fraction and the bottom panel – in anti-FLAG-immunoprecipitates.

    Journal: Journal of molecular and cellular cardiology

    Article Title: CA2+-ACTIVATED ADENYLYL CYCLASE 1 INTRODUCES CA2+-DEPENDENCE TO BETA-ADRENERGIC STIMULATION OF HCN2 CURRENT

    doi: 10.1016/j.yjmcc.2012.03.010

    Figure Lengend Snippet: A. Expression of recombinant adenylyl cyclase in NRVM. Cultures were co-infected with AdmHCN2 and one of the following: AdGFP, FLAG-tagged AdAC1 or FLAG-tagged AdAC6. 72 hours later cells were harvested, and the soluble membrane fraction was isolated. Soluble membranes from cultures infected with AdGFP, AdAC1 or AdAC6 were incubated with anti-FLAG or anti-HCN2 antibodies, separated by PAGE and probed with appropriate antibodies. B . Expression of endogenous HCN2 in NRVM and its co-immunoprecipitation with overexpressed adenylyl cyclases. The top panel shows detection of HCN2 in membrane fraction and the bottom panel – in anti-FLAG-immunoprecipitates.

    Article Snippet: To explore the possibility of direct interaction with HCN2 channels, we immunoprecipitated AC with anti-FLAG antibodies, separated the obtained proteins by PAGE and probed with anti-HCN2 antibodies ( ; middle panel).

    Techniques: Expressing, Recombinant, Infection, Isolation, Incubation, Polyacrylamide Gel Electrophoresis, Immunoprecipitation

    Effect of chronic training on HCN1, KCN2 and HCN4 protein expression determined by immunocytochemical techniques in sedentary and trained dog. Bar diagram on top left indicates that the relative density of dog cardiomyocytes with HCN4 immunolabelling obtained from the trained group (n=30 cells/6 dogs) is significantly increased compared to that measured in the sedentary group (n=30 cells/6 dogs). Original immunofluorescent images are shown on the left . Bottom panels indicate lack of effect of chronic training on the relative density of dog cardiomyocytes with HCN1 and HCN2 immunolabelling (n=30 – 30 cells/6 – 6 dogs for sedentary and trained groups, respectively). Figure 7–Source Data 1 Effect of chronic training on HCN4 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 2 Effect of chronic training on HCN1 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 3 Effect of chronic training on HCN2 protein expression determined by immunocytochemical technique in sedentary and trained dogs.

    Journal: bioRxiv

    Article Title: Cardiac electrophysiological remodeling associated with enhanced arrhythmia susceptibilty in a canine model of elite exercise

    doi: 10.1101/2022.07.13.499876

    Figure Lengend Snippet: Effect of chronic training on HCN1, KCN2 and HCN4 protein expression determined by immunocytochemical techniques in sedentary and trained dog. Bar diagram on top left indicates that the relative density of dog cardiomyocytes with HCN4 immunolabelling obtained from the trained group (n=30 cells/6 dogs) is significantly increased compared to that measured in the sedentary group (n=30 cells/6 dogs). Original immunofluorescent images are shown on the left . Bottom panels indicate lack of effect of chronic training on the relative density of dog cardiomyocytes with HCN1 and HCN2 immunolabelling (n=30 – 30 cells/6 – 6 dogs for sedentary and trained groups, respectively). Figure 7–Source Data 1 Effect of chronic training on HCN4 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 2 Effect of chronic training on HCN1 protein expression determined by immunocytochemical technique in sedentary and trained dogs. Figure 7–Source Data 3 Effect of chronic training on HCN2 protein expression determined by immunocytochemical technique in sedentary and trained dogs.

    Article Snippet: After the incubation period, cells were labelled overnight at 4°C with anti-KChIP2 (Alomone, #APC-142, RRID:AB_2756744), anti-Kv4.3 (Alomone, #APC-017, RRID:AB_2040178), anti-HCN1 (Alomone, #APC-056, RRID:AB_2039900), anti-HCN2 (Alomone, #APC-030, RRID:AB_2313726) and anti-HCN4 (Alomone, #APC-052, RRID:AB_2039906) primary antibody diluted to 1:50.

    Techniques: Expressing