kir2 3  (Alomone Labs)


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    Alomone Labs kir2 3
    Inward rectifier K + current I K1 expression and function in transgenic atrial myocytes. Experimental animals involved wild‐type mice (WT) and transgenic mice (TG) expressing the repressor isoform of cyclic adenosine monophosphate response element modulator, CREM‐IbΔC‐X, and were distributed according to age in 6‐week‐old (WT 6w and TG 6w ) and 12‐week‐old (WT 12w and TG 12w ) groups. A , Representative traces of inward rectifiers K + channel (I K1 ) recorded in WT 12w and TG 12w myocytes before and after application of 10 μmol/L BaCl 2 using a ramp protocol (inset, scale bar 0.2 seconds). The traces show current densitiy (expressed in picoamperes/picofarads [pA/pF]) over time. ( Aa ). Current–voltage plots of I K1 averaged from traces of all cells. For WT 6w , n/N are 8/5, for TG 6w n/N are 10/6, for WT 12w n/N are 13/7, and for TG 12w n/N are 9/6 ( Ab ). B , Data show mean±SE of relative mRNA levels of atrial K + voltage‐gated channel subfamily J member 2 ( Kcnj2 ) and 4 ( Kcnj4 ) normalized to WT 6w vs Hprt1 (hypoxanthine phosphoribosyltransferase 1) as the housekeeping gene; N=8 per group. Y‐axes scale is Log2. Ca through c , Representative immunoblots ( Ca ) and quantification of K + inwardly rectifying channel subunits Kir2.1 ( Cb ) and <t>Kir2.3</t> ( Cc ) protein levels normalized to calsequestrin (CSQ). Data show mean±SE of 7 mice per group. Da through b , Representative action potentials recorded before (normal Tyrode [NT] as control) and after application of 10 μmol/L BaCl 2 in 1 atrial myocyte of each group ( Da ). Quantification of the percentages of action potential duration (APD) change in BaCl 2 vs NT at 50% (APD 50 ) and 90% (APD 90 ) repolarization. Data show mean±SE of n/N for WT 6w (7/5), TG 6w (5/5), WT 12w (11/6), and TG 12w (5/4) ( Db ). * P
    Kir2 3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Inward Rectifier K+ Currents Contribute to the Proarrhythmic Electrical Phenotype of Atria Overexpressing Cyclic Adenosine Monophosphate Response Element Modulator Isoform CREM‐IbΔC‐X"

    Article Title: Inward Rectifier K+ Currents Contribute to the Proarrhythmic Electrical Phenotype of Atria Overexpressing Cyclic Adenosine Monophosphate Response Element Modulator Isoform CREM‐IbΔC‐X

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    doi: 10.1161/JAHA.119.016144

    Inward rectifier K + current I K1 expression and function in transgenic atrial myocytes. Experimental animals involved wild‐type mice (WT) and transgenic mice (TG) expressing the repressor isoform of cyclic adenosine monophosphate response element modulator, CREM‐IbΔC‐X, and were distributed according to age in 6‐week‐old (WT 6w and TG 6w ) and 12‐week‐old (WT 12w and TG 12w ) groups. A , Representative traces of inward rectifiers K + channel (I K1 ) recorded in WT 12w and TG 12w myocytes before and after application of 10 μmol/L BaCl 2 using a ramp protocol (inset, scale bar 0.2 seconds). The traces show current densitiy (expressed in picoamperes/picofarads [pA/pF]) over time. ( Aa ). Current–voltage plots of I K1 averaged from traces of all cells. For WT 6w , n/N are 8/5, for TG 6w n/N are 10/6, for WT 12w n/N are 13/7, and for TG 12w n/N are 9/6 ( Ab ). B , Data show mean±SE of relative mRNA levels of atrial K + voltage‐gated channel subfamily J member 2 ( Kcnj2 ) and 4 ( Kcnj4 ) normalized to WT 6w vs Hprt1 (hypoxanthine phosphoribosyltransferase 1) as the housekeeping gene; N=8 per group. Y‐axes scale is Log2. Ca through c , Representative immunoblots ( Ca ) and quantification of K + inwardly rectifying channel subunits Kir2.1 ( Cb ) and Kir2.3 ( Cc ) protein levels normalized to calsequestrin (CSQ). Data show mean±SE of 7 mice per group. Da through b , Representative action potentials recorded before (normal Tyrode [NT] as control) and after application of 10 μmol/L BaCl 2 in 1 atrial myocyte of each group ( Da ). Quantification of the percentages of action potential duration (APD) change in BaCl 2 vs NT at 50% (APD 50 ) and 90% (APD 90 ) repolarization. Data show mean±SE of n/N for WT 6w (7/5), TG 6w (5/5), WT 12w (11/6), and TG 12w (5/4) ( Db ). * P
    Figure Legend Snippet: Inward rectifier K + current I K1 expression and function in transgenic atrial myocytes. Experimental animals involved wild‐type mice (WT) and transgenic mice (TG) expressing the repressor isoform of cyclic adenosine monophosphate response element modulator, CREM‐IbΔC‐X, and were distributed according to age in 6‐week‐old (WT 6w and TG 6w ) and 12‐week‐old (WT 12w and TG 12w ) groups. A , Representative traces of inward rectifiers K + channel (I K1 ) recorded in WT 12w and TG 12w myocytes before and after application of 10 μmol/L BaCl 2 using a ramp protocol (inset, scale bar 0.2 seconds). The traces show current densitiy (expressed in picoamperes/picofarads [pA/pF]) over time. ( Aa ). Current–voltage plots of I K1 averaged from traces of all cells. For WT 6w , n/N are 8/5, for TG 6w n/N are 10/6, for WT 12w n/N are 13/7, and for TG 12w n/N are 9/6 ( Ab ). B , Data show mean±SE of relative mRNA levels of atrial K + voltage‐gated channel subfamily J member 2 ( Kcnj2 ) and 4 ( Kcnj4 ) normalized to WT 6w vs Hprt1 (hypoxanthine phosphoribosyltransferase 1) as the housekeeping gene; N=8 per group. Y‐axes scale is Log2. Ca through c , Representative immunoblots ( Ca ) and quantification of K + inwardly rectifying channel subunits Kir2.1 ( Cb ) and Kir2.3 ( Cc ) protein levels normalized to calsequestrin (CSQ). Data show mean±SE of 7 mice per group. Da through b , Representative action potentials recorded before (normal Tyrode [NT] as control) and after application of 10 μmol/L BaCl 2 in 1 atrial myocyte of each group ( Da ). Quantification of the percentages of action potential duration (APD) change in BaCl 2 vs NT at 50% (APD 50 ) and 90% (APD 90 ) repolarization. Data show mean±SE of n/N for WT 6w (7/5), TG 6w (5/5), WT 12w (11/6), and TG 12w (5/4) ( Db ). * P

    Techniques Used: Expressing, Transgenic Assay, Mouse Assay, Western Blot

    2) Product Images from "Electrical and histological remodeling of the pulmonary vein in 2K1C hypertensive rats: Indication of initiation and maintenance of atrial fibrillation"

    Article Title: Electrical and histological remodeling of the pulmonary vein in 2K1C hypertensive rats: Indication of initiation and maintenance of atrial fibrillation

    Journal: Anatolian Journal of Cardiology

    doi: 10.14744/AnatolJCardiol.2017.7844

    Protein levels of the ion channel components Na v 1.5, Kir2.1, Kir2.3, and Ca v 1.2, analyzed by western blot and normalized to GAPDH Data are expressed as mean±SD. *p
    Figure Legend Snippet: Protein levels of the ion channel components Na v 1.5, Kir2.1, Kir2.3, and Ca v 1.2, analyzed by western blot and normalized to GAPDH Data are expressed as mean±SD. *p

    Techniques Used: Western Blot

    3) Product Images from "Chronic heart failure and the substrate for atrial fibrillation"

    Article Title: Chronic heart failure and the substrate for atrial fibrillation

    Journal: Cardiovascular Research

    doi: 10.1093/cvr/cvp216

    LA potassium channel subunit expression is altered, and AT-1 receptor expression is increased during HF. ( A ) Representative western blots. ( B ) Pooled data normalized to GAPDH for Kir2.1, Kir2.3, K + channel interacting protein (KChiP2), Kv4.3, Kv1.5, and
    Figure Legend Snippet: LA potassium channel subunit expression is altered, and AT-1 receptor expression is increased during HF. ( A ) Representative western blots. ( B ) Pooled data normalized to GAPDH for Kir2.1, Kir2.3, K + channel interacting protein (KChiP2), Kv4.3, Kv1.5, and

    Techniques Used: Expressing, Western Blot

    4) Product Images from "SAP97 regulates Kir2.3 channels by multiple mechanisms"

    Article Title: SAP97 regulates Kir2.3 channels by multiple mechanisms

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    doi: 10.1152/ajpheart.00638.2008

    Introduction of SAP97 in Kir2.3-expressing HEK cells increases channel protein abundance and cell surface expression. A : HEK cells were transfected with SAP97-IRES2-GFP or hemagglutinin antigen (HA)-tagged Kir2.3. Left : cells expressing SAP97-IRES2-GFP.
    Figure Legend Snippet: Introduction of SAP97 in Kir2.3-expressing HEK cells increases channel protein abundance and cell surface expression. A : HEK cells were transfected with SAP97-IRES2-GFP or hemagglutinin antigen (HA)-tagged Kir2.3. Left : cells expressing SAP97-IRES2-GFP.

    Techniques Used: Expressing, Transfection

    Transfection of myc -tagged SAP97 into Kir2.3-expressing cells results in decreased vesicular localization of the channel protein. The distribution of Kir2.3 was determined in Kir2.3 stable cells after the transient transfection of empty plasmid ( A ) or
    Figure Legend Snippet: Transfection of myc -tagged SAP97 into Kir2.3-expressing cells results in decreased vesicular localization of the channel protein. The distribution of Kir2.3 was determined in Kir2.3 stable cells after the transient transfection of empty plasmid ( A ) or

    Techniques Used: Transfection, Expressing, Plasmid Preparation

    SAP97 increases whole cell Kir2.3 currents in HEK293 cells without changing rectification or pH sensitivity. A : Kir2.3 currents were measured as barium (1 mM)-sensitive currents (control current − barium current), and membrane potentials reflect
    Figure Legend Snippet: SAP97 increases whole cell Kir2.3 currents in HEK293 cells without changing rectification or pH sensitivity. A : Kir2.3 currents were measured as barium (1 mM)-sensitive currents (control current − barium current), and membrane potentials reflect

    Techniques Used:

    Synapse-associated protein (SAP) 97 and inwardly rectifying potassium channel (Kir) 2.3 coimmunoprecipitate from sheep atrial membranes. A : the PDZ binding domain of Kir2.3, residue SAI, is found at the extreme COOH-terminal end of the polypeptide. B
    Figure Legend Snippet: Synapse-associated protein (SAP) 97 and inwardly rectifying potassium channel (Kir) 2.3 coimmunoprecipitate from sheep atrial membranes. A : the PDZ binding domain of Kir2.3, residue SAI, is found at the extreme COOH-terminal end of the polypeptide. B

    Techniques Used: Binding Assay

    Increase in Kir2.3 current requires SAP97 binding motif on channel COOH terminal. A : current density-voltage relationship of transiently transfected Kir2.3 wild-type and mutant (Kir2.3 ΔSAI) channels in HEK cells (Kir2.3 wild type N = 6; Kir2.3
    Figure Legend Snippet: Increase in Kir2.3 current requires SAP97 binding motif on channel COOH terminal. A : current density-voltage relationship of transiently transfected Kir2.3 wild-type and mutant (Kir2.3 ΔSAI) channels in HEK cells (Kir2.3 wild type N = 6; Kir2.3

    Techniques Used: Binding Assay, Transfection, Mutagenesis

    SAP97 increases the unitary conductance of Kir2.3 channels. A : representative trace of cell-attached single channel events from a control cell ( top ) and from two patches in cells in which Kir2.3 was coexpressed with SAP97 ( middle and bottom ). Scale bars
    Figure Legend Snippet: SAP97 increases the unitary conductance of Kir2.3 channels. A : representative trace of cell-attached single channel events from a control cell ( top ) and from two patches in cells in which Kir2.3 was coexpressed with SAP97 ( middle and bottom ). Scale bars

    Techniques Used:

    5) Product Images from "SAP97 regulates Kir2.3 channels by multiple mechanisms"

    Article Title: SAP97 regulates Kir2.3 channels by multiple mechanisms

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    doi: 10.1152/ajpheart.00638.2008

    Prominent endosomal localization of channel protein is seen in the Kir 2.3 stable cell line. The colocalization of channel protein (green) in the Kir 2.3 cell line with antigen markers (red) for early endosomes [early endosome antigen 1 (EEA1;  A ), middle
    Figure Legend Snippet: Prominent endosomal localization of channel protein is seen in the Kir 2.3 stable cell line. The colocalization of channel protein (green) in the Kir 2.3 cell line with antigen markers (red) for early endosomes [early endosome antigen 1 (EEA1; A ), middle

    Techniques Used: Stable Transfection

    6) Product Images from "Kir2.3 Isoform Confers pH Sensitivity to Heteromeric Kir2.1/Kir2.3 Channels in HEK293 Cells"

    Article Title: Kir2.3 Isoform Confers pH Sensitivity to Heteromeric Kir2.1/Kir2.3 Channels in HEK293 Cells

    Journal: Heart rhythm : the official journal of the Heart Rhythm Society

    doi: 10.1016/j.hrthm.2006.12.033

    Properties of Kir2.1/Kir2.3 double stables in HEK293 cells A. Western Blot showing the presence of Kir2.1 and Kir2.3 channel proteins in the double stables. B. Ramp-generated, Ba 2+ (1 mM)-sensitive currents in the double stables. Whole-cell currents are plotted as a function of command potential (n = 4).
    Figure Legend Snippet: Properties of Kir2.1/Kir2.3 double stables in HEK293 cells A. Western Blot showing the presence of Kir2.1 and Kir2.3 channel proteins in the double stables. B. Ramp-generated, Ba 2+ (1 mM)-sensitive currents in the double stables. Whole-cell currents are plotted as a function of command potential (n = 4).

    Techniques Used: Western Blot, Generated

    pH-sensitivity of heteromeric Kir2.1/Kir2.3 currents in HEK293 cells A. Acidification to pH o = 5.0 from control (pH o = 7.4) significantly inhibits whole-cell Kir2.1/Kir2.3 current. Inset: Subtracted (pH sensitive) current. B . Peak inward (filled triangles) and peak outward (open triangles) whole-cell Kir2.3 currents normalized to current values at pH o = 7.4 and plotted as a function of pH o (n = 6–10). pH o blocked whole-cell currents, with p K a of 7.5 ± 0.09 and 7.4 ± 0.06 (p = NS), respectively for inward and outward currents. C. Effects of acidification by CO 2 on whole-cell Kir2.1/Kir2.3 currents. D. Average data of peak inward whole-cell Kir2.1/Kir2.3 currents normalized to current values at pH o = 7.4 (n = 5).
    Figure Legend Snippet: pH-sensitivity of heteromeric Kir2.1/Kir2.3 currents in HEK293 cells A. Acidification to pH o = 5.0 from control (pH o = 7.4) significantly inhibits whole-cell Kir2.1/Kir2.3 current. Inset: Subtracted (pH sensitive) current. B . Peak inward (filled triangles) and peak outward (open triangles) whole-cell Kir2.3 currents normalized to current values at pH o = 7.4 and plotted as a function of pH o (n = 6–10). pH o blocked whole-cell currents, with p K a of 7.5 ± 0.09 and 7.4 ± 0.06 (p = NS), respectively for inward and outward currents. C. Effects of acidification by CO 2 on whole-cell Kir2.1/Kir2.3 currents. D. Average data of peak inward whole-cell Kir2.1/Kir2.3 currents normalized to current values at pH o = 7.4 (n = 5).

    Techniques Used:

    pH-sensitivity of Kir2.1-Kir2.3 concatamers channels in HEK293 cells A. Control (pH o = 7.4) current trace and a trace during acidification by CO 2 in the same cell. B. Average data of peak inward currents normalized to control current values at (n = 5).
    Figure Legend Snippet: pH-sensitivity of Kir2.1-Kir2.3 concatamers channels in HEK293 cells A. Control (pH o = 7.4) current trace and a trace during acidification by CO 2 in the same cell. B. Average data of peak inward currents normalized to control current values at (n = 5).

    Techniques Used:

    Properties of unitary Kir2.1 and Kir2.3 channels in HEK293 cells A . Representative cell-attached patch recordings in cells expressing Kir2.1 (top) and Kir2.3 (bottom). The solid line represents channel resting state B. Events histograms for unitary events in patches containing Kir2.1 or Kir2.3 channels.
    Figure Legend Snippet: Properties of unitary Kir2.1 and Kir2.3 channels in HEK293 cells A . Representative cell-attached patch recordings in cells expressing Kir2.1 (top) and Kir2.3 (bottom). The solid line represents channel resting state B. Events histograms for unitary events in patches containing Kir2.1 or Kir2.3 channels.

    Techniques Used: Expressing

    pH o effect on homomeric Kir2.1 and Kir2.3 channels in HEK293 cells A. Acidification to pH o = 5.0 from control (pH o = 7.4) has no significant effect on whole-cell Kir2.1 current B . Peak inward (filled squares) and peak outward (open squares) Kir2.1 whole-cell currents normalized to current values at pH o = 7.4 and plotted as a function of pH o (n = 6–10). C. Acidification to pH o = 5.0 from control (pH o = 7.4) significantly inhibits whole-cell Kir2.3 current D. Peak inward (filled circles) and peak outward (open circles) Kir2.3 whole-cell currents normalized to current values at pH o = 7.4 and plotted as a function of pH o (n = 7–11). Increases in pH o blocked whole-cell inward and outward currents. See text for details.
    Figure Legend Snippet: pH o effect on homomeric Kir2.1 and Kir2.3 channels in HEK293 cells A. Acidification to pH o = 5.0 from control (pH o = 7.4) has no significant effect on whole-cell Kir2.1 current B . Peak inward (filled squares) and peak outward (open squares) Kir2.1 whole-cell currents normalized to current values at pH o = 7.4 and plotted as a function of pH o (n = 6–10). C. Acidification to pH o = 5.0 from control (pH o = 7.4) significantly inhibits whole-cell Kir2.3 current D. Peak inward (filled circles) and peak outward (open circles) Kir2.3 whole-cell currents normalized to current values at pH o = 7.4 and plotted as a function of pH o (n = 7–11). Increases in pH o blocked whole-cell inward and outward currents. See text for details.

    Techniques Used:

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    Alomone Labs kir2 3
    Inward rectifier K + current I K1 expression and function in transgenic atrial myocytes. Experimental animals involved wild‐type mice (WT) and transgenic mice (TG) expressing the repressor isoform of cyclic adenosine monophosphate response element modulator, CREM‐IbΔC‐X, and were distributed according to age in 6‐week‐old (WT 6w and TG 6w ) and 12‐week‐old (WT 12w and TG 12w ) groups. A , Representative traces of inward rectifiers K + channel (I K1 ) recorded in WT 12w and TG 12w myocytes before and after application of 10 μmol/L BaCl 2 using a ramp protocol (inset, scale bar 0.2 seconds). The traces show current densitiy (expressed in picoamperes/picofarads [pA/pF]) over time. ( Aa ). Current–voltage plots of I K1 averaged from traces of all cells. For WT 6w , n/N are 8/5, for TG 6w n/N are 10/6, for WT 12w n/N are 13/7, and for TG 12w n/N are 9/6 ( Ab ). B , Data show mean±SE of relative mRNA levels of atrial K + voltage‐gated channel subfamily J member 2 ( Kcnj2 ) and 4 ( Kcnj4 ) normalized to WT 6w vs Hprt1 (hypoxanthine phosphoribosyltransferase 1) as the housekeeping gene; N=8 per group. Y‐axes scale is Log2. Ca through c , Representative immunoblots ( Ca ) and quantification of K + inwardly rectifying channel subunits Kir2.1 ( Cb ) and <t>Kir2.3</t> ( Cc ) protein levels normalized to calsequestrin (CSQ). Data show mean±SE of 7 mice per group. Da through b , Representative action potentials recorded before (normal Tyrode [NT] as control) and after application of 10 μmol/L BaCl 2 in 1 atrial myocyte of each group ( Da ). Quantification of the percentages of action potential duration (APD) change in BaCl 2 vs NT at 50% (APD 50 ) and 90% (APD 90 ) repolarization. Data show mean±SE of n/N for WT 6w (7/5), TG 6w (5/5), WT 12w (11/6), and TG 12w (5/4) ( Db ). * P
    Kir2 3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kir2 3/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
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    kir2 3 - by Bioz Stars, 2022-11
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    Inward rectifier K + current I K1 expression and function in transgenic atrial myocytes. Experimental animals involved wild‐type mice (WT) and transgenic mice (TG) expressing the repressor isoform of cyclic adenosine monophosphate response element modulator, CREM‐IbΔC‐X, and were distributed according to age in 6‐week‐old (WT 6w and TG 6w ) and 12‐week‐old (WT 12w and TG 12w ) groups. A , Representative traces of inward rectifiers K + channel (I K1 ) recorded in WT 12w and TG 12w myocytes before and after application of 10 μmol/L BaCl 2 using a ramp protocol (inset, scale bar 0.2 seconds). The traces show current densitiy (expressed in picoamperes/picofarads [pA/pF]) over time. ( Aa ). Current–voltage plots of I K1 averaged from traces of all cells. For WT 6w , n/N are 8/5, for TG 6w n/N are 10/6, for WT 12w n/N are 13/7, and for TG 12w n/N are 9/6 ( Ab ). B , Data show mean±SE of relative mRNA levels of atrial K + voltage‐gated channel subfamily J member 2 ( Kcnj2 ) and 4 ( Kcnj4 ) normalized to WT 6w vs Hprt1 (hypoxanthine phosphoribosyltransferase 1) as the housekeeping gene; N=8 per group. Y‐axes scale is Log2. Ca through c , Representative immunoblots ( Ca ) and quantification of K + inwardly rectifying channel subunits Kir2.1 ( Cb ) and Kir2.3 ( Cc ) protein levels normalized to calsequestrin (CSQ). Data show mean±SE of 7 mice per group. Da through b , Representative action potentials recorded before (normal Tyrode [NT] as control) and after application of 10 μmol/L BaCl 2 in 1 atrial myocyte of each group ( Da ). Quantification of the percentages of action potential duration (APD) change in BaCl 2 vs NT at 50% (APD 50 ) and 90% (APD 90 ) repolarization. Data show mean±SE of n/N for WT 6w (7/5), TG 6w (5/5), WT 12w (11/6), and TG 12w (5/4) ( Db ). * P

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    Article Title: Inward Rectifier K+ Currents Contribute to the Proarrhythmic Electrical Phenotype of Atria Overexpressing Cyclic Adenosine Monophosphate Response Element Modulator Isoform CREM‐IbΔC‐X

    doi: 10.1161/JAHA.119.016144

    Figure Lengend Snippet: Inward rectifier K + current I K1 expression and function in transgenic atrial myocytes. Experimental animals involved wild‐type mice (WT) and transgenic mice (TG) expressing the repressor isoform of cyclic adenosine monophosphate response element modulator, CREM‐IbΔC‐X, and were distributed according to age in 6‐week‐old (WT 6w and TG 6w ) and 12‐week‐old (WT 12w and TG 12w ) groups. A , Representative traces of inward rectifiers K + channel (I K1 ) recorded in WT 12w and TG 12w myocytes before and after application of 10 μmol/L BaCl 2 using a ramp protocol (inset, scale bar 0.2 seconds). The traces show current densitiy (expressed in picoamperes/picofarads [pA/pF]) over time. ( Aa ). Current–voltage plots of I K1 averaged from traces of all cells. For WT 6w , n/N are 8/5, for TG 6w n/N are 10/6, for WT 12w n/N are 13/7, and for TG 12w n/N are 9/6 ( Ab ). B , Data show mean±SE of relative mRNA levels of atrial K + voltage‐gated channel subfamily J member 2 ( Kcnj2 ) and 4 ( Kcnj4 ) normalized to WT 6w vs Hprt1 (hypoxanthine phosphoribosyltransferase 1) as the housekeeping gene; N=8 per group. Y‐axes scale is Log2. Ca through c , Representative immunoblots ( Ca ) and quantification of K + inwardly rectifying channel subunits Kir2.1 ( Cb ) and Kir2.3 ( Cc ) protein levels normalized to calsequestrin (CSQ). Data show mean±SE of 7 mice per group. Da through b , Representative action potentials recorded before (normal Tyrode [NT] as control) and after application of 10 μmol/L BaCl 2 in 1 atrial myocyte of each group ( Da ). Quantification of the percentages of action potential duration (APD) change in BaCl 2 vs NT at 50% (APD 50 ) and 90% (APD 90 ) repolarization. Data show mean±SE of n/N for WT 6w (7/5), TG 6w (5/5), WT 12w (11/6), and TG 12w (5/4) ( Db ). * P

    Article Snippet: The following rabbit polyclonal primary antibodies were used against K + voltage‐gated channels (Kv) subunits Kv4.2 (1:200, APC 023, Alomone Labs, Jerusalem, Israel), Kv4.3 (1:200, APC 017, Alomone Labs), K + channel interacting protein 2 (KChIP2) (1:200, sc‐25685, Santa Cruz Biotechnology Inc, Santa Cruz, CA), and K + inwardly rectifying channel (Kir) subunits Kir2.1 (1:200, APC 159, Alomone Labs), Kir2.3 (1:1000, APC 032, Alomone Labs), Kir3.1 (1:200, APC 005, Alomone Labs), Kir3.4 (1:200, APC 027, Alomone Labs), and as loading control calsequestrin (1:2500, PA1‐913, Thermo Fisher Scientific).

    Techniques: Expressing, Transgenic Assay, Mouse Assay, Western Blot

    Protein levels of the ion channel components Na v 1.5, Kir2.1, Kir2.3, and Ca v 1.2, analyzed by western blot and normalized to GAPDH Data are expressed as mean±SD. *p

    Journal: Anatolian Journal of Cardiology

    Article Title: Electrical and histological remodeling of the pulmonary vein in 2K1C hypertensive rats: Indication of initiation and maintenance of atrial fibrillation

    doi: 10.14744/AnatolJCardiol.2017.7844

    Figure Lengend Snippet: Protein levels of the ion channel components Na v 1.5, Kir2.1, Kir2.3, and Ca v 1.2, analyzed by western blot and normalized to GAPDH Data are expressed as mean±SD. *p

    Article Snippet: Membranes were blocked in TBST containing 5% bovine serum albumin at room temperature for 1.5 h before incubation with corresponding primary antibodies: goat polyclonal anti-Col I and rabbit polyclonal anti-MMP-2 (1:200, Santa Cruz, Japan); rabbit monoclonal anti-Ang II (1:2,000, Abcam, UK), rabbit polyclonal anti-TGF-β1 (1:500, Abcam, UK); and rabbit polyclonal anti-Kir2.1, rabbit monoclonal anti-Kir2.3, rabbit monoclonal anti-Cav1.2 and rabbit monoclonal anti-Nav1.5 (1:200, Alomone, Israel).

    Techniques: Western Blot