kchip2  (Alomone Labs)


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    Structured Review

    Alomone Labs kchip2
    I to recovery from inactivation. A) The recovery kinetics was tested by a double-pulse protocol with interpulse time varying from 50 ms to 15 sec (n=12 RV and 7 LV cells from n=3 hearts). B) The amplitudes of the slow and fast inactivating components of I to (I to,si and I I to,fi ) as a function of inter-pulse interval were determined by fitting the time course of I to decay during the second pulse to a double exponential function. The x-axis of inter-pulse intervals is in a logarithmic scale. C) The amplitudes of I to,fi and I to,si from RV and LV. Fast and slow-inactivating components (I to,fi and I to,si ) of each I to,f and I to,s were calculated as described in Methods and represented as a stacked column plot. D) Western blots of Kv4.2, Kv1.4, and <t>KChIP2</t> from LQT1 hearts. E). The accessory unit of I to , KChIP2, known to affect inactivation and recovery kinetics, was twofold higher in RV (ANOVA, p .
    Kchip2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    kchip2 - by Bioz Stars, 2022-11
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    Images

    1) Product Images from "Transient Outward K+ Current (Ito) Underlies the Right Ventricular Initiation of Polymorphic Ventricular Tachycardia in a Transgenic Rabbit Model of Long QT Type 1"

    Article Title: Transient Outward K+ Current (Ito) Underlies the Right Ventricular Initiation of Polymorphic Ventricular Tachycardia in a Transgenic Rabbit Model of Long QT Type 1

    Journal: Circulation. Arrhythmia and electrophysiology

    doi: 10.1161/CIRCEP.117.005414

    I to recovery from inactivation. A) The recovery kinetics was tested by a double-pulse protocol with interpulse time varying from 50 ms to 15 sec (n=12 RV and 7 LV cells from n=3 hearts). B) The amplitudes of the slow and fast inactivating components of I to (I to,si and I I to,fi ) as a function of inter-pulse interval were determined by fitting the time course of I to decay during the second pulse to a double exponential function. The x-axis of inter-pulse intervals is in a logarithmic scale. C) The amplitudes of I to,fi and I to,si from RV and LV. Fast and slow-inactivating components (I to,fi and I to,si ) of each I to,f and I to,s were calculated as described in Methods and represented as a stacked column plot. D) Western blots of Kv4.2, Kv1.4, and KChIP2 from LQT1 hearts. E). The accessory unit of I to , KChIP2, known to affect inactivation and recovery kinetics, was twofold higher in RV (ANOVA, p .
    Figure Legend Snippet: I to recovery from inactivation. A) The recovery kinetics was tested by a double-pulse protocol with interpulse time varying from 50 ms to 15 sec (n=12 RV and 7 LV cells from n=3 hearts). B) The amplitudes of the slow and fast inactivating components of I to (I to,si and I I to,fi ) as a function of inter-pulse interval were determined by fitting the time course of I to decay during the second pulse to a double exponential function. The x-axis of inter-pulse intervals is in a logarithmic scale. C) The amplitudes of I to,fi and I to,si from RV and LV. Fast and slow-inactivating components (I to,fi and I to,si ) of each I to,f and I to,s were calculated as described in Methods and represented as a stacked column plot. D) Western blots of Kv4.2, Kv1.4, and KChIP2 from LQT1 hearts. E). The accessory unit of I to , KChIP2, known to affect inactivation and recovery kinetics, was twofold higher in RV (ANOVA, p .

    Techniques Used: Mass Spectrometry, Size-exclusion Chromatography, Western Blot

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    Alomone Labs anti kchip2 antibody
    Protein expression and relative density of Kv4.3 and <t>KChiP2</t> subunits determined by Western blot and immunocytochemical techniques in sedentary and trained dog. Two bar diagrams on the left show the relative protein expression of Kv4.3 and KChiP2 subunits determined by Western blot in sedentary (n=12 dogs) and trained dog (n=12) left ventricular samples. Bottom panels indicates the representative Kv4.3 and KChIP2 bands and their corresponding loading control (GAPDH). Two bar diagrams on the right panels show the relative density of dog cardiomyocytes with Kv4.3 and KChiP2 immunolabelling obtained from the sedentary (n=30 cells/6 dogs) and trained (n=30 cells/6 dogs) groups. Bottom panels on the right show original immunofluorescent images of dog cardiomyocytes with Kv4.3 and KChiP2 immunolabelling. Figure 6–Source Data 1 Protein expression of Kv4.3 subunit determined by Western blot technique in sedentary and trained dogs. Figure 6–Source Data 2 Protein expression of KChiP2 subunit determined by Western blot technique in sedentary and trained dogs. Figure 6–Source Data 3 Relative density of Kv4.3 subunit determined by immunocytochemical technique in sedentary and trained dogs. Figure 6–Source Data 4 Relative density of KChiP2 subunit determined by immunocytochemical technique in sedentary and trained dogs. Figure 6–Source Data 5 Original, unedited membranes of western blots with the relevant bands clearly labelled. Figure 6–Source Data 6 Original files of the full raw unedited membranes of western blots.
    Anti Kchip2 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
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    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti kchip2 antibody - by Bioz Stars, 2022-11
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    Protein expression and relative density of Kv4.3 and KChiP2 subunits determined by Western blot and immunocytochemical techniques in sedentary and trained dog. Two bar diagrams on the left show the relative protein expression of Kv4.3 and KChiP2 subunits determined by Western blot in sedentary (n=12 dogs) and trained dog (n=12) left ventricular samples. Bottom panels indicates the representative Kv4.3 and KChIP2 bands and their corresponding loading control (GAPDH). Two bar diagrams on the right panels show the relative density of dog cardiomyocytes with Kv4.3 and KChiP2 immunolabelling obtained from the sedentary (n=30 cells/6 dogs) and trained (n=30 cells/6 dogs) groups. Bottom panels on the right show original immunofluorescent images of dog cardiomyocytes with Kv4.3 and KChiP2 immunolabelling. Figure 6–Source Data 1 Protein expression of Kv4.3 subunit determined by Western blot technique in sedentary and trained dogs. Figure 6–Source Data 2 Protein expression of KChiP2 subunit determined by Western blot technique in sedentary and trained dogs. Figure 6–Source Data 3 Relative density of Kv4.3 subunit determined by immunocytochemical technique in sedentary and trained dogs. Figure 6–Source Data 4 Relative density of KChiP2 subunit determined by immunocytochemical technique in sedentary and trained dogs. Figure 6–Source Data 5 Original, unedited membranes of western blots with the relevant bands clearly labelled. Figure 6–Source Data 6 Original files of the full raw unedited membranes of western blots.

    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: Protein expression and relative density of Kv4.3 and KChiP2 subunits determined by Western blot and immunocytochemical techniques in sedentary and trained dog. Two bar diagrams on the left show the relative protein expression of Kv4.3 and KChiP2 subunits determined by Western blot in sedentary (n=12 dogs) and trained dog (n=12) left ventricular samples. Bottom panels indicates the representative Kv4.3 and KChIP2 bands and their corresponding loading control (GAPDH). Two bar diagrams on the right panels show the relative density of dog cardiomyocytes with Kv4.3 and KChiP2 immunolabelling obtained from the sedentary (n=30 cells/6 dogs) and trained (n=30 cells/6 dogs) groups. Bottom panels on the right show original immunofluorescent images of dog cardiomyocytes with Kv4.3 and KChiP2 immunolabelling. Figure 6–Source Data 1 Protein expression of Kv4.3 subunit determined by Western blot technique in sedentary and trained dogs. Figure 6–Source Data 2 Protein expression of KChiP2 subunit determined by Western blot technique in sedentary and trained dogs. Figure 6–Source Data 3 Relative density of Kv4.3 subunit determined by immunocytochemical technique in sedentary and trained dogs. Figure 6–Source Data 4 Relative density of KChiP2 subunit determined by immunocytochemical technique in sedentary and trained dogs. Figure 6–Source Data 5 Original, unedited membranes of western blots with the relevant bands clearly labelled. Figure 6–Source Data 6 Original files of the full raw unedited membranes of western blots.

    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, Western Blot

    Increasing I to,f density with bicistronic Kv4.3/KChIP2.1 expression affects cardiomyocyte AP waveform. Panel A shows APs recorded from 2 day cultured (untransduced black), and transduced myocytes with increasing I to,f current densities at a cycle length of 1 s. Introduction of I to,f (lower panel traces show exemplar records for pulses to −30, +10 and + 40 mV) resulted in a prominent AP phase 1 in all transduced myocytes. As I to,f density increased, there was a progressive change in AP morphology that caused the AP to resemble that recorded in other species. B. Increasing density of I to,f (at +40 mV) decreased APD20. APD90 (right panel) decreased approximately exponentially (solid line) with increasing I to,f except when I to,f was between ~12 and ~ 17 pA/pF (deviation highlighted as dashed line) where emergence of a marked ‘spike-and-dome’ morphology developed (as shown center right in A). All trend curves drawn by eye. C. Representative traces of I to,f recorded in untransduced (Control) iPSC-CMs and iPSC-CMs expressing bicistronic Kv4.3-mCherry/KChIP2.1 under a cTnT promoter. After a brief step to −40 mV to inactivate Na + channels, subsequent membrane depolarizations to −30 mV, −10 mV, +10 mV, +30 mV and + 50 mV were used to elicit I to in control and transduced iPSC-CMs. D. Three examplar AP waveforms of iPSC-CMs without (black traces) or with expressed I to,f currents (green lower traces). I to,f densities in the exemplar transduced iPSC-CMs were 5–10 pA/pF at +40 mV. APs were elicited at a frequency of 1 Hz. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing Ito,f and phase 1 repolarization of the cardiac action potential with a Kv4.3/KChIP2.1 bicistronic transgene

    doi: 10.1016/j.yjmcc.2021.11.004

    Figure Lengend Snippet: Increasing I to,f density with bicistronic Kv4.3/KChIP2.1 expression affects cardiomyocyte AP waveform. Panel A shows APs recorded from 2 day cultured (untransduced black), and transduced myocytes with increasing I to,f current densities at a cycle length of 1 s. Introduction of I to,f (lower panel traces show exemplar records for pulses to −30, +10 and + 40 mV) resulted in a prominent AP phase 1 in all transduced myocytes. As I to,f density increased, there was a progressive change in AP morphology that caused the AP to resemble that recorded in other species. B. Increasing density of I to,f (at +40 mV) decreased APD20. APD90 (right panel) decreased approximately exponentially (solid line) with increasing I to,f except when I to,f was between ~12 and ~ 17 pA/pF (deviation highlighted as dashed line) where emergence of a marked ‘spike-and-dome’ morphology developed (as shown center right in A). All trend curves drawn by eye. C. Representative traces of I to,f recorded in untransduced (Control) iPSC-CMs and iPSC-CMs expressing bicistronic Kv4.3-mCherry/KChIP2.1 under a cTnT promoter. After a brief step to −40 mV to inactivate Na + channels, subsequent membrane depolarizations to −30 mV, −10 mV, +10 mV, +30 mV and + 50 mV were used to elicit I to in control and transduced iPSC-CMs. D. Three examplar AP waveforms of iPSC-CMs without (black traces) or with expressed I to,f currents (green lower traces). I to,f densities in the exemplar transduced iPSC-CMs were 5–10 pA/pF at +40 mV. APs were elicited at a frequency of 1 Hz. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Samples were then labelled with primary antibodies including anti-Caveolin 3 (anti-Cav3; BD Bioscience, San Jose, USA; 1/500 dilution) anti-KChIP2 (Alomone, Israel; 1/500 dilution) overnight at 4 °C.

    Techniques: Expressing, Cell Culture

    A. Plasmid vector for bicistronic for Kv4.3 and KChIP2.1 with amino acids shown in black (linkers in brown). A CMV or cardiac-specific troponin T promoter (cTnT) was used in different cell types. B. Western blot of KChIP2.1 expression by the bicistronic transgene in HEK293 cells. A single band corresponding to the estimated molecular weight of KChIP2.1 or KChIP2.1-Amcyan was detected in lysates from bicistronic transgene transfected cells but not from cells transfected with Kv4.3-mCherry alone. C Expression of Kv4.3-mCherry upstream of the P2A sequence was detected at an apparent molecular weight of ~80 kDa while expression of Kv4.3 alone was detected at ~60 kDa. These data are consistent with the expected weights of Kv4.3 (71 kDa) and mCherry (20 kDa), given a − 20% gel shift for K channel protein [ 61 ]. Additional higher molecular weight bands possibly reflect multimeric forms of Kv4.3. Lysates of cells transfected with untagged Kv4.3 and Amcyan-P2A-mCherry were used as positive and negative controls respectively and SYPRO® staining was used as internal loading control. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing Ito,f and phase 1 repolarization of the cardiac action potential with a Kv4.3/KChIP2.1 bicistronic transgene

    doi: 10.1016/j.yjmcc.2021.11.004

    Figure Lengend Snippet: A. Plasmid vector for bicistronic for Kv4.3 and KChIP2.1 with amino acids shown in black (linkers in brown). A CMV or cardiac-specific troponin T promoter (cTnT) was used in different cell types. B. Western blot of KChIP2.1 expression by the bicistronic transgene in HEK293 cells. A single band corresponding to the estimated molecular weight of KChIP2.1 or KChIP2.1-Amcyan was detected in lysates from bicistronic transgene transfected cells but not from cells transfected with Kv4.3-mCherry alone. C Expression of Kv4.3-mCherry upstream of the P2A sequence was detected at an apparent molecular weight of ~80 kDa while expression of Kv4.3 alone was detected at ~60 kDa. These data are consistent with the expected weights of Kv4.3 (71 kDa) and mCherry (20 kDa), given a − 20% gel shift for K channel protein [ 61 ]. Additional higher molecular weight bands possibly reflect multimeric forms of Kv4.3. Lysates of cells transfected with untagged Kv4.3 and Amcyan-P2A-mCherry were used as positive and negative controls respectively and SYPRO® staining was used as internal loading control. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Samples were then labelled with primary antibodies including anti-Caveolin 3 (anti-Cav3; BD Bioscience, San Jose, USA; 1/500 dilution) anti-KChIP2 (Alomone, Israel; 1/500 dilution) overnight at 4 °C.

    Techniques: Plasmid Preparation, Western Blot, Expressing, Molecular Weight, Transfection, Sequencing, Electrophoretic Mobility Shift Assay, Staining

    Subcellular colocalization of Kv4.3 and KChIP2.1. A. Exemplar confocal images of living HEK293 cells expressing bicistronic Kv4.3-mCherry and KChIP2.1-AmCyan. B. Representative confocal images of a transduced rabbit ventricular cardiomyocytes expressing Kv4.3-mCherry and KChIP2 (see also Fig. S2A). Surface membranes were labelled with an anti-Cav3 antibody (top). C shows an enlarged view of the boxed regions in B and the fluorescence intensity profile from each label at bottom. D Co-localization between Kv4.3 and KChIP2.1 in different subcellular compartments (sarcolemma -SL; t-tubules TT; and remaining cytoplasm -Cyt.) measured by unbiased Pearson's correlation coefficient (n/ N = 8/3). Error bars show s.e.m.

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing Ito,f and phase 1 repolarization of the cardiac action potential with a Kv4.3/KChIP2.1 bicistronic transgene

    doi: 10.1016/j.yjmcc.2021.11.004

    Figure Lengend Snippet: Subcellular colocalization of Kv4.3 and KChIP2.1. A. Exemplar confocal images of living HEK293 cells expressing bicistronic Kv4.3-mCherry and KChIP2.1-AmCyan. B. Representative confocal images of a transduced rabbit ventricular cardiomyocytes expressing Kv4.3-mCherry and KChIP2 (see also Fig. S2A). Surface membranes were labelled with an anti-Cav3 antibody (top). C shows an enlarged view of the boxed regions in B and the fluorescence intensity profile from each label at bottom. D Co-localization between Kv4.3 and KChIP2.1 in different subcellular compartments (sarcolemma -SL; t-tubules TT; and remaining cytoplasm -Cyt.) measured by unbiased Pearson's correlation coefficient (n/ N = 8/3). Error bars show s.e.m.

    Article Snippet: Samples were then labelled with primary antibodies including anti-Caveolin 3 (anti-Cav3; BD Bioscience, San Jose, USA; 1/500 dilution) anti-KChIP2 (Alomone, Israel; 1/500 dilution) overnight at 4 °C.

    Techniques: Expressing, Fluorescence

    Biophysical properties of I to,f currents produced by Kv4.3 alone (-KChIP2.1) and with KChIP2.1 added via the bicistronic vector in HEK293 cells. A. Exemplar whole-cell currents elicited by 500 ms-depolarization pulses from −60 mV to +40 mV in 10 mV increments from a holding potential of −80 mV. B. The peak current at all potentials was increased by bicistronic addition of KChIP2.1 and the current activated at ~ − 30 mV as expected for Kv4.3 in the presence of KChIP2.1. C. The fast time constant of I to,f inactivation as a function of test potential (Kv4.3 alone: 7.66 ± 1.5 ms, n = 5 vs. Bicistronic Kv4.3/KChIP2.1: 21.2 ± 1.6 ms, n = 18 at +40 mV; p

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing Ito,f and phase 1 repolarization of the cardiac action potential with a Kv4.3/KChIP2.1 bicistronic transgene

    doi: 10.1016/j.yjmcc.2021.11.004

    Figure Lengend Snippet: Biophysical properties of I to,f currents produced by Kv4.3 alone (-KChIP2.1) and with KChIP2.1 added via the bicistronic vector in HEK293 cells. A. Exemplar whole-cell currents elicited by 500 ms-depolarization pulses from −60 mV to +40 mV in 10 mV increments from a holding potential of −80 mV. B. The peak current at all potentials was increased by bicistronic addition of KChIP2.1 and the current activated at ~ − 30 mV as expected for Kv4.3 in the presence of KChIP2.1. C. The fast time constant of I to,f inactivation as a function of test potential (Kv4.3 alone: 7.66 ± 1.5 ms, n = 5 vs. Bicistronic Kv4.3/KChIP2.1: 21.2 ± 1.6 ms, n = 18 at +40 mV; p

    Article Snippet: Samples were then labelled with primary antibodies including anti-Caveolin 3 (anti-Cav3; BD Bioscience, San Jose, USA; 1/500 dilution) anti-KChIP2 (Alomone, Israel; 1/500 dilution) overnight at 4 °C.

    Techniques: Produced, Plasmid Preparation

    Characterization of I to,f currents encoded by the bicistronic Kv4.3/KChIP2.1construct in rabbit ventricular cardiomycytes. A. Typical patch-clamp recordings of I to currents from freshly isolated cardiomyocytes and 40 h after transduction. Currents were evoked by step depolarizations to potentials between −30 and + 40 mV (in 10 mV increments). B. The left panel shows current-voltage relationships of intrinsic I to (n/ N = 7/3) and exogenous I to,f (n/ N = 16/8) and the fast time constant of I to,f inactivation (right hand panel). C. Concentration-dependence of the I to,f block by 4-AP block (n/N = 7/4). Exemplar recordings of the I to,f currents at +30 mV before and after application of 1 mmol/l of 4-AP are shown in the inset. D. Exemplar I to,f traces recorded from a transduced myocyte under basal conditions and in the presence of NS5806 (5 μmol/l). The right hand panel shows the augmentation of the mean peak I to,f current-voltage relationship by 5 μmol/l NS5806 ( p

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing Ito,f and phase 1 repolarization of the cardiac action potential with a Kv4.3/KChIP2.1 bicistronic transgene

    doi: 10.1016/j.yjmcc.2021.11.004

    Figure Lengend Snippet: Characterization of I to,f currents encoded by the bicistronic Kv4.3/KChIP2.1construct in rabbit ventricular cardiomycytes. A. Typical patch-clamp recordings of I to currents from freshly isolated cardiomyocytes and 40 h after transduction. Currents were evoked by step depolarizations to potentials between −30 and + 40 mV (in 10 mV increments). B. The left panel shows current-voltage relationships of intrinsic I to (n/ N = 7/3) and exogenous I to,f (n/ N = 16/8) and the fast time constant of I to,f inactivation (right hand panel). C. Concentration-dependence of the I to,f block by 4-AP block (n/N = 7/4). Exemplar recordings of the I to,f currents at +30 mV before and after application of 1 mmol/l of 4-AP are shown in the inset. D. Exemplar I to,f traces recorded from a transduced myocyte under basal conditions and in the presence of NS5806 (5 μmol/l). The right hand panel shows the augmentation of the mean peak I to,f current-voltage relationship by 5 μmol/l NS5806 ( p

    Article Snippet: Samples were then labelled with primary antibodies including anti-Caveolin 3 (anti-Cav3; BD Bioscience, San Jose, USA; 1/500 dilution) anti-KChIP2 (Alomone, Israel; 1/500 dilution) overnight at 4 °C.

    Techniques: Patch Clamp, Isolation, Transduction, Concentration Assay, Blocking Assay