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  • 93
    Alomone Labs anti kchip2 antibody
    A. Plasmid vector for bicistronic for Kv4.3 and <t>KChIP2.1</t> 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 . 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.)
    Anti Kchip2 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
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    91
    Santa Cruz Biotechnology anti kchip2
    A. Plasmid vector for bicistronic for Kv4.3 and <t>KChIP2.1</t> 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 . 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.)
    Anti Kchip2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti kchip2/product/Santa Cruz Biotechnology
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    86
    NeuroMab kchip2
    (A) Triple staining of the neuronal marker UCHL1 and two different TRPV1 antibodies derived from rabbit and goat, respectively, to facilitate the analysis of various targets. The staining intensities obtained with both TRPV1 antibodies correlated significantly (Spearmans ρ = 0.96, p<2.2e-16). (B-E, G) Co-labeling of TRPV1 and CART (B), Nos1 (C), KChIP1 (D), <t>KChIP2</t> (E), and CaMKIIα (G). Plots of respective controls are shown in . (F) Average fluorescence intensities of TRPV1 and the indicated targets in TRPV1-negative (grey) and -positive (black) neurons. Signal intensities of all analyzed targets were significantly higher within the TRPV1(+) population (n = 3 with>3000 analyzed neurons per experiment, paired two-tailed t-tests).
    Kchip2, supplied by NeuroMab, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Abcam kchip2
    (A) Triple staining of the neuronal marker UCHL1 and two different TRPV1 antibodies derived from rabbit and goat, respectively, to facilitate the analysis of various targets. The staining intensities obtained with both TRPV1 antibodies correlated significantly (Spearmans ρ = 0.96, p<2.2e-16). (B-E, G) Co-labeling of TRPV1 and CART (B), Nos1 (C), KChIP1 (D), <t>KChIP2</t> (E), and CaMKIIα (G). Plots of respective controls are shown in . (F) Average fluorescence intensities of TRPV1 and the indicated targets in TRPV1-negative (grey) and -positive (black) neurons. Signal intensities of all analyzed targets were significantly higher within the TRPV1(+) population (n = 3 with>3000 analyzed neurons per experiment, paired two-tailed t-tests).
    Kchip2, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher kchip2
    Primers for PCR analysis
    Kchip2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    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 . 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 I to,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 . 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: Specificity controls for KChIP2 labelling in transduced myocytes were performed by pre-incubating the anti-KChIP2 antibody with an immunizing peptide (Alomone) comprised of the amino acid sequences corresponding to the KChIP2 epitope at a 1:10 ratio (wt:wt) overnight at 4 °C (see Fig. S2A,B).

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

    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 < 0.002 Students t -test). D. Time-dependent recovery from inactivation at −80 mV. To calculate the recovery rate from inactivation, normalised tail peak current amplitudes were recorded at +40 mV and plotted as a function of the inter-pulse interval (Δt) (protocol illustrated in the inset). Error bars show mean ± s.e.m.

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing I to,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 < 0.002 Students t -test). D. Time-dependent recovery from inactivation at −80 mV. To calculate the recovery rate from inactivation, normalised tail peak current amplitudes were recorded at +40 mV and plotted as a function of the inter-pulse interval (Δt) (protocol illustrated in the inset). Error bars show mean ± s.e.m.

    Article Snippet: Specificity controls for KChIP2 labelling in transduced myocytes were performed by pre-incubating the anti-KChIP2 antibody with an immunizing peptide (Alomone) comprised of the amino acid sequences corresponding to the KChIP2 epitope at a 1:10 ratio (wt:wt) overnight at 4 °C (see Fig. S2A,B).

    Techniques: Produced, Plasmid Preparation

    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 I to,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: Specificity controls for KChIP2 labelling in transduced myocytes were performed by pre-incubating the anti-KChIP2 antibody with an immunizing peptide (Alomone) comprised of the amino acid sequences corresponding to the KChIP2 epitope at a 1:10 ratio (wt:wt) overnight at 4 °C (see Fig. S2A,B).

    Techniques: Expressing, Fluorescence

    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 < 0.001, n/N = 7/3, matched pair t-test). The cells used for these experiments were cultured for 48 h (40 h in A,B) to further increase peak I to,f to minimise the contribution from NS5806-augmented native I to (typically 3 pA/pF ). Error bars show mean ± s.e.m.

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing I to,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 < 0.001, n/N = 7/3, matched pair t-test). The cells used for these experiments were cultured for 48 h (40 h in A,B) to further increase peak I to,f to minimise the contribution from NS5806-augmented native I to (typically 3 pA/pF ). Error bars show mean ± s.e.m.

    Article Snippet: Specificity controls for KChIP2 labelling in transduced myocytes were performed by pre-incubating the anti-KChIP2 antibody with an immunizing peptide (Alomone) comprised of the amino acid sequences corresponding to the KChIP2 epitope at a 1:10 ratio (wt:wt) overnight at 4 °C (see Fig. S2A,B).

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

    Electrophysiological effects of culture and viral bicistronic transduction in cardiomyocytes.

    Journal: Journal of Molecular and Cellular Cardiology

    Article Title: Inducing I to,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: Electrophysiological effects of culture and viral bicistronic transduction in cardiomyocytes.

    Article Snippet: Specificity controls for KChIP2 labelling in transduced myocytes were performed by pre-incubating the anti-KChIP2 antibody with an immunizing peptide (Alomone) comprised of the amino acid sequences corresponding to the KChIP2 epitope at a 1:10 ratio (wt:wt) overnight at 4 °C (see Fig. S2A,B).

    Techniques: Transduction, Isolation

    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 I to,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: Specificity controls for KChIP2 labelling in transduced myocytes were performed by pre-incubating the anti-KChIP2 antibody with an immunizing peptide (Alomone) comprised of the amino acid sequences corresponding to the KChIP2 epitope at a 1:10 ratio (wt:wt) overnight at 4 °C (see Fig. S2A,B).

    Techniques: Expressing, Cell Culture

    (A) Triple staining of the neuronal marker UCHL1 and two different TRPV1 antibodies derived from rabbit and goat, respectively, to facilitate the analysis of various targets. The staining intensities obtained with both TRPV1 antibodies correlated significantly (Spearmans ρ = 0.96, p<2.2e-16). (B-E, G) Co-labeling of TRPV1 and CART (B), Nos1 (C), KChIP1 (D), KChIP2 (E), and CaMKIIα (G). Plots of respective controls are shown in . (F) Average fluorescence intensities of TRPV1 and the indicated targets in TRPV1-negative (grey) and -positive (black) neurons. Signal intensities of all analyzed targets were significantly higher within the TRPV1(+) population (n = 3 with>3000 analyzed neurons per experiment, paired two-tailed t-tests).

    Journal: PLoS ONE

    Article Title: Subgroup-Elimination Transcriptomics Identifies Signaling Proteins that Define Subclasses of TRPV1-Positive Neurons and a Novel Paracrine Circuit

    doi: 10.1371/journal.pone.0115731

    Figure Lengend Snippet: (A) Triple staining of the neuronal marker UCHL1 and two different TRPV1 antibodies derived from rabbit and goat, respectively, to facilitate the analysis of various targets. The staining intensities obtained with both TRPV1 antibodies correlated significantly (Spearmans ρ = 0.96, p<2.2e-16). (B-E, G) Co-labeling of TRPV1 and CART (B), Nos1 (C), KChIP1 (D), KChIP2 (E), and CaMKIIα (G). Plots of respective controls are shown in . (F) Average fluorescence intensities of TRPV1 and the indicated targets in TRPV1-negative (grey) and -positive (black) neurons. Signal intensities of all analyzed targets were significantly higher within the TRPV1(+) population (n = 3 with>3000 analyzed neurons per experiment, paired two-tailed t-tests).

    Article Snippet: The following antibodies were used in this study: chicken polyclonal anti-UCHL1 (1∶2000, Novus, Cambridge, UK, #NB110-58872), rabbit polyclonal anti-TRPV1 (1∶1000, Alomone labs, Jerusalem, Israel, # ACC-030), goat polyclonal anti-TRPV1 (1∶500, R&D Systems, #AF3066), mouse monoclonal anti hCART, (1∶3000, R&D Systems, #MAB163), rabbit monoclonal anti NOS1 (1∶500, clone C7D7, Cell Signaling, Danvers, MA, #4231), mouse monoclonal anti CaMKIIα (1∶2000, clone 6G9, Thermo Scientific, #MA1-048), rabbit monoclonal anti CaMKIV (1∶500, Millipore, clone EP2564Y, #04-1081), mouse monoclonal anti KChIP1 (1∶500, Abcam, Cambridge, UK, #ab99013), mouse monoclonal anti KChIP2 (1∶1000, UC Davis/NIH NeuroMab Facility, Clone K60/73, #75-004), rabbit monoclonal anti phospho RIIα (S96) (1∶1000, clone 151, Abcam, # ab32390), mouse monoclonal anti phospho-p44/42 MAPK (T202/Y204) (1∶250, clone E10, Cell Signaling, #9106), rabbit monoclonal anti-Prostaglandin D Synthase (1∶1000, clone E12357, Abcam, ab182141), mouse monoclonal anti-NF200 (1∶2000, clone N52, Sigma-Aldrich, Munich, Germany, #N0142), highly cross-adsorbed Alexa 647, 594, and 488 conjugated secondary antibodies (Invitrogen, Carlsbad, CA).

    Techniques: Staining, Marker, Derivative Assay, Labeling, Fluorescence, Two Tailed Test

    Primers for PCR analysis

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Notch signaling modulates the electrical behavior of cardiomyocytes

    doi: 10.1152/ajpheart.00587.2016

    Figure Lengend Snippet: Primers for PCR analysis

    Article Snippet: Thin sections of the left ventricle (LV) were indirectly immunolabeled for the detection of GFP (Anti-GFP Antibody, catalog no. ab5450, Abcam) and KChIP2 (KCNIP2 Polyclonal Antibody, catalog no. PA5-41075, ThermoFisher Scientific).

    Techniques:

    Notch signaling activation reduces Kv channel-interacting protein 2 (KChIP2) expression in cardiomyocytes. A: KChIP2 (white) expression in the left ventricular (LV) myocardium of a MCM-WT mouse. Nuclei are stained by DAPI. Autofluorescence (AF) in the green channel was collected to visualize the structure of myocardial tissue. The green channel is omitted at right. B: green fluorescent protein (GFP; green) and KChIP2 (white) expression in the LV myocardium of a MCM-NICD-GFP mouse. Nuclei are stained by DAPI. The green channel is omitted at right. C: quantification of KChIP2 levels in myocytes in LV tissue of MCM-WT mice [wild type (WT), n = 2 mice] and MCM-NICD-GFP mice [Notch1 intracellular domain (NICD), n = 3 mice]. For each acquired image, the intensity of the fluorescent signal (F) from individual myocytes was normalized with respect to the signal of the myocyte presenting the highest fluorescent intensity (Fmax). Normalized data are presented as F/Fmax. *P < 0.001 vs. WT. D: quantification of relative KChIP2 levels in NICD-GFP-negative and NICD-GFP-positive myocytes in the myocardium of the MCM-NICD-GFP mice (NICD) shown in C. *P < 0.001 vs. NICD-GFP negative.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Notch signaling modulates the electrical behavior of cardiomyocytes

    doi: 10.1152/ajpheart.00587.2016

    Figure Lengend Snippet: Notch signaling activation reduces Kv channel-interacting protein 2 (KChIP2) expression in cardiomyocytes. A: KChIP2 (white) expression in the left ventricular (LV) myocardium of a MCM-WT mouse. Nuclei are stained by DAPI. Autofluorescence (AF) in the green channel was collected to visualize the structure of myocardial tissue. The green channel is omitted at right. B: green fluorescent protein (GFP; green) and KChIP2 (white) expression in the LV myocardium of a MCM-NICD-GFP mouse. Nuclei are stained by DAPI. The green channel is omitted at right. C: quantification of KChIP2 levels in myocytes in LV tissue of MCM-WT mice [wild type (WT), n = 2 mice] and MCM-NICD-GFP mice [Notch1 intracellular domain (NICD), n = 3 mice]. For each acquired image, the intensity of the fluorescent signal (F) from individual myocytes was normalized with respect to the signal of the myocyte presenting the highest fluorescent intensity (Fmax). Normalized data are presented as F/Fmax. *P < 0.001 vs. WT. D: quantification of relative KChIP2 levels in NICD-GFP-negative and NICD-GFP-positive myocytes in the myocardium of the MCM-NICD-GFP mice (NICD) shown in C. *P < 0.001 vs. NICD-GFP negative.

    Article Snippet: Thin sections of the left ventricle (LV) were indirectly immunolabeled for the detection of GFP (Anti-GFP Antibody, catalog no. ab5450, Abcam) and KChIP2 (KCNIP2 Polyclonal Antibody, catalog no. PA5-41075, ThermoFisher Scientific).

    Techniques: Activation Assay, Expressing, Staining