kv1 5  (Alomone Labs)


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    Structured Review

    Alomone Labs kv1 5
    Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of <t>Kv1.5</t> protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p
    Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 80/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5/product/Alomone Labs
    Average 80 stars, based on 24 article reviews
    Price from $9.99 to $1999.99
    kv1 5 - by Bioz Stars, 2022-08
    80/100 stars

    Images

    1) Product Images from "Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes"

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    Journal: Molecular Biology Reports

    doi: 10.1007/s11033-022-07378-1

    Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p
    Figure Legend Snippet: Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p

    Techniques Used: Activation Assay, Expressing, Transfection

    Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p
    Figure Legend Snippet: Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p

    Techniques Used: Activation Assay, Incubation, Enzyme-linked Immunosorbent Assay

    Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p
    Figure Legend Snippet: Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p

    Techniques Used: Concentration Assay, Activation Assay

    MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p
    Figure Legend Snippet: MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Techniques Used: Expressing

    Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p
    Figure Legend Snippet: Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Techniques Used: Concentration Assay

    2) Product Images from "Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily"

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    Journal: bioRxiv

    doi: 10.1101/2020.10.06.328237

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Techniques Used: Immunohistochemistry, Staining

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Techniques Used: Immunohistochemistry, Staining

    3) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

    4) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

    5) Product Images from "Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily"

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    Journal: bioRxiv

    doi: 10.1101/2020.10.06.328237

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Techniques Used: Immunohistochemistry, Staining

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Techniques Used: Immunohistochemistry, Staining

    6) Product Images from "Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes"

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    Journal: Molecular Biology Reports

    doi: 10.1007/s11033-022-07378-1

    Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p
    Figure Legend Snippet: Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p

    Techniques Used: Activation Assay, Expressing, Transfection

    Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p
    Figure Legend Snippet: Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p

    Techniques Used: Activation Assay, Incubation, Enzyme-linked Immunosorbent Assay

    Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p
    Figure Legend Snippet: Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p

    Techniques Used: Concentration Assay, Activation Assay

    MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p
    Figure Legend Snippet: MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Techniques Used: Expressing

    Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p
    Figure Legend Snippet: Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Techniques Used: Concentration Assay

    7) Product Images from "Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes"

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    Journal: Molecular Biology Reports

    doi: 10.1007/s11033-022-07378-1

    Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p
    Figure Legend Snippet: Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p

    Techniques Used: Activation Assay, Expressing, Transfection

    Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p
    Figure Legend Snippet: Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p

    Techniques Used: Activation Assay, Incubation, Enzyme-linked Immunosorbent Assay

    Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p
    Figure Legend Snippet: Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p

    Techniques Used: Concentration Assay, Activation Assay

    MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p
    Figure Legend Snippet: MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Techniques Used: Expressing

    Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p
    Figure Legend Snippet: Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Techniques Used: Concentration Assay

    8) Product Images from "Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats"

    Article Title: Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats

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

    doi: 10.1161/JAHA.118.010456

    miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P
    Figure Legend Snippet: miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P

    Techniques Used: Inhibition, In Vivo, Expressing, Quantitative RT-PCR

    miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P
    Figure Legend Snippet: miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P

    Techniques Used: Inhibition, Cell Culture, Expressing

    9) Product Images from "Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats"

    Article Title: Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats

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

    doi: 10.1161/JAHA.118.010456

    miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P
    Figure Legend Snippet: miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P

    Techniques Used: Inhibition, In Vivo, Expressing, Quantitative RT-PCR

    miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P
    Figure Legend Snippet: miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P

    Techniques Used: Inhibition, Cell Culture, Expressing

    10) Product Images from "Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily"

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    Journal: bioRxiv

    doi: 10.1101/2020.10.06.328237

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Techniques Used: Immunohistochemistry, Staining

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Techniques Used: Immunohistochemistry, Staining

    11) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

    12) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

    13) Product Images from "Interactions between the C-terminus of Kv1.5 and Kv? regulate pyridine nucleotide-dependent changes in channel gating"

    Article Title: Interactions between the C-terminus of Kv1.5 and Kv? regulate pyridine nucleotide-dependent changes in channel gating

    Journal: Pflugers Archiv

    doi: 10.1007/s00424-012-1093-z

    Binding of the C-terminal domain of Kv to Kvβ (a)  Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing  E.coli  (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST;  (b)  Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P
    Figure Legend Snippet: Binding of the C-terminal domain of Kv to Kvβ (a) Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing E.coli (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST; (b) Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P

    Techniques Used: Binding Assay, Western Blot, Incubation, Expressing, SDS Page

    14) Product Images from "Molecular evidence for a role of Shaw (Kv3) potassium channel subunits in potassium currents of dog atrium"

    Article Title: Molecular evidence for a role of Shaw (Kv3) potassium channel subunits in potassium currents of dog atrium

    Journal: The Journal of Physiology

    doi: 10.1111/j.1469-7793.2000.00467.x

    Protein studies in dog atrium A, Western blots of membrane proteins prepared from dog atrium (lane 1, DA1) and isolated dog atrial myocytes (lane 2, DA2) probed with a Kv3.1 antibody. Lane 3, dog atrial membrane preparation after pre-incubation of antibody with Kv3.1 peptide (Pre-inc). B, Western blots with Kv1.5 antibody obtained with human atrial (HA) and dog atrial (DA) tissues.
    Figure Legend Snippet: Protein studies in dog atrium A, Western blots of membrane proteins prepared from dog atrium (lane 1, DA1) and isolated dog atrial myocytes (lane 2, DA2) probed with a Kv3.1 antibody. Lane 3, dog atrial membrane preparation after pre-incubation of antibody with Kv3.1 peptide (Pre-inc). B, Western blots with Kv1.5 antibody obtained with human atrial (HA) and dog atrial (DA) tissues.

    Techniques Used: Western Blot, Isolation, Incubation

    15) Product Images from "Metabolic regulation of Kv channels and cardiac repolarization by Kvβ2 subunits"

    Article Title: Metabolic regulation of Kv channels and cardiac repolarization by Kvβ2 subunits

    Journal: Journal of molecular and cellular cardiology

    doi: 10.1016/j.yjmcc.2019.09.013

    Myocardial Kvβ2 associates with Kv1 and Kv4 proteins. ( A ) Representative blot images showing immunoreactive bands for Kv1.4, Kv1.5, Kv4.2, Kv4.3 and Kvβ2 in whole heart lysates and Kvβ2 immunoprecipitates. Absence of immunoreactive bands at expected molecular weights for each protein is also shown for mouse IgG immunoprecipitates as a negative control. Representative of 3 independent experiments. ( B ) Representative blot image showing immunoreactivity for Kvβ2 (predicted molecular weight, ~37 kDa) in Kvβ2 immunoprecipitates from heart lysates of wild type and Kvβ2 −/− animals. ( C ) Differential interference contrast (DIC) and proximity ligation assay (PLA)-associated fluorescence images of isolated adult ventricular myocytes from wild type and Kvβ2 −/− animals after PLA targeting of Kvβ2 complexes using mouse and rabbit-derived anti-Kvβ2 primary antibodies. PLA images are shown as flattened 2D maximum intensity z-projections from z-series captured for each cell. ( D ) PLA images of isolated ventricular myocytes treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1 anti-Kv4.2, anti-Kv4.3. ( E ) Summary of fluorescent PLA-associated punctae, normalized to cell footprint area, for cells treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1, anti-Kv4.2 and anti-Kv4.3 primary antibodies (n = 6–10). *P
    Figure Legend Snippet: Myocardial Kvβ2 associates with Kv1 and Kv4 proteins. ( A ) Representative blot images showing immunoreactive bands for Kv1.4, Kv1.5, Kv4.2, Kv4.3 and Kvβ2 in whole heart lysates and Kvβ2 immunoprecipitates. Absence of immunoreactive bands at expected molecular weights for each protein is also shown for mouse IgG immunoprecipitates as a negative control. Representative of 3 independent experiments. ( B ) Representative blot image showing immunoreactivity for Kvβ2 (predicted molecular weight, ~37 kDa) in Kvβ2 immunoprecipitates from heart lysates of wild type and Kvβ2 −/− animals. ( C ) Differential interference contrast (DIC) and proximity ligation assay (PLA)-associated fluorescence images of isolated adult ventricular myocytes from wild type and Kvβ2 −/− animals after PLA targeting of Kvβ2 complexes using mouse and rabbit-derived anti-Kvβ2 primary antibodies. PLA images are shown as flattened 2D maximum intensity z-projections from z-series captured for each cell. ( D ) PLA images of isolated ventricular myocytes treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1 anti-Kv4.2, anti-Kv4.3. ( E ) Summary of fluorescent PLA-associated punctae, normalized to cell footprint area, for cells treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1, anti-Kv4.2 and anti-Kv4.3 primary antibodies (n = 6–10). *P

    Techniques Used: Negative Control, Molecular Weight, Proximity Ligation Assay, Fluorescence, Isolation, Derivative Assay

    Kvβ2 promotes Kv1 and Kv4 surface expression in cardiac myocytes. ( A ) Differential interference contrast (DIC) and confocal images showing Kvβ2-associated fluorescence (red) in isolated cardiac myocytes from wild type (wt) and Kvβ2 −/− animals. Nuclei (dapi) are shown in blue. ( B ) Western blots showing immunoreactive bands for Kv pore-forming and auxiliary subunits at respective predicted molecular weights as indicated in heart lysates from wt (n = 3) and Kvβ2 −/− (n = 3) animals. As a representative loading control, immunoreactive bands for GAPDH are shown for each lane of Kv1.5 blot. ( C ) Summarized densitometric data for Kv1.4, Kv1.5, Kv2.1, Kv4.2, Kv4.3, Kvβ1.1, Kvβ1.2, Kvβ2, and KChIP2 proteins in heart lysates of wt animals. Data are normalized to GAPDH (run for each blot) and expressed relative to wt controls. *P
    Figure Legend Snippet: Kvβ2 promotes Kv1 and Kv4 surface expression in cardiac myocytes. ( A ) Differential interference contrast (DIC) and confocal images showing Kvβ2-associated fluorescence (red) in isolated cardiac myocytes from wild type (wt) and Kvβ2 −/− animals. Nuclei (dapi) are shown in blue. ( B ) Western blots showing immunoreactive bands for Kv pore-forming and auxiliary subunits at respective predicted molecular weights as indicated in heart lysates from wt (n = 3) and Kvβ2 −/− (n = 3) animals. As a representative loading control, immunoreactive bands for GAPDH are shown for each lane of Kv1.5 blot. ( C ) Summarized densitometric data for Kv1.4, Kv1.5, Kv2.1, Kv4.2, Kv4.3, Kvβ1.1, Kvβ1.2, Kvβ2, and KChIP2 proteins in heart lysates of wt animals. Data are normalized to GAPDH (run for each blot) and expressed relative to wt controls. *P

    Techniques Used: Expressing, Fluorescence, Isolation, Western Blot

    16) Product Images from "Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily"

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    Journal: bioRxiv

    doi: 10.1101/2020.10.06.328237

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Techniques Used: Immunohistochemistry, Staining

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Techniques Used: Immunohistochemistry, Staining

    17) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

    18) Product Images from "Metabolic regulation of Kv channels and cardiac repolarization by Kvβ2 subunits"

    Article Title: Metabolic regulation of Kv channels and cardiac repolarization by Kvβ2 subunits

    Journal: Journal of molecular and cellular cardiology

    doi: 10.1016/j.yjmcc.2019.09.013

    Myocardial Kvβ2 associates with Kv1 and Kv4 proteins. ( A ) Representative blot images showing immunoreactive bands for Kv1.4, Kv1.5, Kv4.2, Kv4.3 and Kvβ2 in whole heart lysates and Kvβ2 immunoprecipitates. Absence of immunoreactive bands at expected molecular weights for each protein is also shown for mouse IgG immunoprecipitates as a negative control. Representative of 3 independent experiments. ( B ) Representative blot image showing immunoreactivity for Kvβ2 (predicted molecular weight, ~37 kDa) in Kvβ2 immunoprecipitates from heart lysates of wild type and Kvβ2 −/− animals. ( C ) Differential interference contrast (DIC) and proximity ligation assay (PLA)-associated fluorescence images of isolated adult ventricular myocytes from wild type and Kvβ2 −/− animals after PLA targeting of Kvβ2 complexes using mouse and rabbit-derived anti-Kvβ2 primary antibodies. PLA images are shown as flattened 2D maximum intensity z-projections from z-series captured for each cell. ( D ) PLA images of isolated ventricular myocytes treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1 anti-Kv4.2, anti-Kv4.3. ( E ) Summary of fluorescent PLA-associated punctae, normalized to cell footprint area, for cells treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1, anti-Kv4.2 and anti-Kv4.3 primary antibodies (n = 6–10). *P
    Figure Legend Snippet: Myocardial Kvβ2 associates with Kv1 and Kv4 proteins. ( A ) Representative blot images showing immunoreactive bands for Kv1.4, Kv1.5, Kv4.2, Kv4.3 and Kvβ2 in whole heart lysates and Kvβ2 immunoprecipitates. Absence of immunoreactive bands at expected molecular weights for each protein is also shown for mouse IgG immunoprecipitates as a negative control. Representative of 3 independent experiments. ( B ) Representative blot image showing immunoreactivity for Kvβ2 (predicted molecular weight, ~37 kDa) in Kvβ2 immunoprecipitates from heart lysates of wild type and Kvβ2 −/− animals. ( C ) Differential interference contrast (DIC) and proximity ligation assay (PLA)-associated fluorescence images of isolated adult ventricular myocytes from wild type and Kvβ2 −/− animals after PLA targeting of Kvβ2 complexes using mouse and rabbit-derived anti-Kvβ2 primary antibodies. PLA images are shown as flattened 2D maximum intensity z-projections from z-series captured for each cell. ( D ) PLA images of isolated ventricular myocytes treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1 anti-Kv4.2, anti-Kv4.3. ( E ) Summary of fluorescent PLA-associated punctae, normalized to cell footprint area, for cells treated with anti-Kvβ2 only, or anti-Kvβ2 with anti-Kv1.4, anti-Kv1.5, anti-Kv2.1, anti-Kv4.2 and anti-Kv4.3 primary antibodies (n = 6–10). *P

    Techniques Used: Negative Control, Molecular Weight, Proximity Ligation Assay, Fluorescence, Isolation, Derivative Assay

    Kvβ2 promotes Kv1 and Kv4 surface expression in cardiac myocytes. ( A ) Differential interference contrast (DIC) and confocal images showing Kvβ2-associated fluorescence (red) in isolated cardiac myocytes from wild type (wt) and Kvβ2 −/− animals. Nuclei (dapi) are shown in blue. ( B ) Western blots showing immunoreactive bands for Kv pore-forming and auxiliary subunits at respective predicted molecular weights as indicated in heart lysates from wt (n = 3) and Kvβ2 −/− (n = 3) animals. As a representative loading control, immunoreactive bands for GAPDH are shown for each lane of Kv1.5 blot. ( C ) Summarized densitometric data for Kv1.4, Kv1.5, Kv2.1, Kv4.2, Kv4.3, Kvβ1.1, Kvβ1.2, Kvβ2, and KChIP2 proteins in heart lysates of wt animals. Data are normalized to GAPDH (run for each blot) and expressed relative to wt controls. *P
    Figure Legend Snippet: Kvβ2 promotes Kv1 and Kv4 surface expression in cardiac myocytes. ( A ) Differential interference contrast (DIC) and confocal images showing Kvβ2-associated fluorescence (red) in isolated cardiac myocytes from wild type (wt) and Kvβ2 −/− animals. Nuclei (dapi) are shown in blue. ( B ) Western blots showing immunoreactive bands for Kv pore-forming and auxiliary subunits at respective predicted molecular weights as indicated in heart lysates from wt (n = 3) and Kvβ2 −/− (n = 3) animals. As a representative loading control, immunoreactive bands for GAPDH are shown for each lane of Kv1.5 blot. ( C ) Summarized densitometric data for Kv1.4, Kv1.5, Kv2.1, Kv4.2, Kv4.3, Kvβ1.1, Kvβ1.2, Kvβ2, and KChIP2 proteins in heart lysates of wt animals. Data are normalized to GAPDH (run for each blot) and expressed relative to wt controls. *P

    Techniques Used: Expressing, Fluorescence, Isolation, Western Blot

    19) Product Images from "Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily"

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    Journal: bioRxiv

    doi: 10.1101/2020.10.06.328237

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Techniques Used: Immunohistochemistry, Staining

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.
    Figure Legend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Techniques Used: Immunohistochemistry, Staining

    20) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

    21) Product Images from "Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats"

    Article Title: Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats

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

    doi: 10.1161/JAHA.118.010456

    miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P
    Figure Legend Snippet: miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P

    Techniques Used: Inhibition, In Vivo, Expressing, Quantitative RT-PCR

    miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P
    Figure Legend Snippet: miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P

    Techniques Used: Inhibition, Cell Culture, Expressing

    22) Product Images from "Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats"

    Article Title: Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats

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

    doi: 10.1161/JAHA.118.010456

    miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P
    Figure Legend Snippet: miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P

    Techniques Used: Inhibition, In Vivo, Expressing, Quantitative RT-PCR

    miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P
    Figure Legend Snippet: miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P

    Techniques Used: Inhibition, Cell Culture, Expressing

    23) Product Images from "Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats"

    Article Title: Increased Expression of MicroRNA‐206 Inhibits Potassium Voltage‐Gated Channel Subfamily A Member 5 in Pulmonary Arterial Smooth Muscle Cells and Is Related to Exaggerated Pulmonary Artery Hypertension Following Intrauterine Growth Retardation in Rats

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

    doi: 10.1161/JAHA.118.010456

    miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P
    Figure Legend Snippet: miR‐206 inhibition in vivo increased Kv1.5 channel expression to restore CH ‐ PAH of IUGR rats. A , Fold‐change of miR‐206 expression by qRT ‐ PCR in PA smooth muscle and mesenteric artery smooth muscle of different groups. n=5 per group of CON , IUGR , CON ‐ CH and IUGR ‐ CH ; n=8 per group of CON ‐ CH ‐Anti206, IUGR ‐ CH ‐Anti206, CON ‐Anti206, and IUGR ‐Anti206;* P

    Techniques Used: Inhibition, In Vivo, Expressing, Quantitative RT-PCR

    miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P
    Figure Legend Snippet: miR‐206 inhibition in primary cultured PASMC s regulates Kv1.5 channel expression and prevents overproliferation of PASMC s from IUGR ‐ CH ‐ PAH rats. A , Fold‐change of miR‐206 in PASMC s of different groups. B , Fold‐change of mRNA of KCNA 5 in PASMC s of different groups. C and D , Representative images of immunoblotting and quantitative analysis of Kv1.5 α‐protein in PASMC s. Data in ( A , B , D ) are presented as means± SEM . * P

    Techniques Used: Inhibition, Cell Culture, Expressing

    24) Product Images from "Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)"

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    Journal: Bosnian Journal of Basic Medical Sciences

    doi:

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Techniques Used: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified
    Figure Legend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Techniques Used: Expressing, Western Blot, Incubation, Affinity Purification

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    Alomone Labs kv1 5
    Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of <t>Kv1.5</t> protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p
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    Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: Effects of a siRNA against Hsp70 and heat shock (HS) on MSU-induced NLRP3 inflammasome activation and the expression of Kv1.5 protein. The LPS-primed J774.1 cells treated with MSU 24 h after the introduction of either a scramble siRNA or a siRNA against Hsp70 ( a ) (n = 4–5) or pre-treated at 42 °C for 1 h ( b ) (n = 5–9). Representative blots are shown. Image densities were normalized to those in the MSU-untreated cells transfected with a scramble siRNA or non-HS control cells. † p

    Article Snippet: Kv1.5 may be a potential therapeutic target for gout-related inflammation and AF.

    Techniques: Activation Assay, Expressing, Transfection

    Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: Effects of the CM from LPS-primed and MSU-stimulated macrophages on activation of NLRP3 inflammasome and Kv1.5 in HL-1 atrial myocytes. HL-1 cells were incubated with Claycomb, the CM from J774.1 cells treated with vehicle (LPS/MSU−) or the CM from LPS-primed MSU-treated cells (LPS/MSU+) overnight. Shown are representative IBs ( a ) (n = 5–8). b IL-1β concentrations in the cell lysates measured by ELISA (n = 4–11). HL-1 cells were treated with DPO-1 (1 μM) or a vehicle 30 min before the incubation with CM + LPDS + MSU overnight. Show are representative blots ( c ) (n = 9) and IL-1β concentrations in the cell lysates measured by ELISA ( d ) (n = 6). * p

    Article Snippet: Kv1.5 may be a potential therapeutic target for gout-related inflammation and AF.

    Techniques: Activation Assay, Incubation, Enzyme-linked Immunosorbent Assay

    Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: Concentration dependent effects of DPO-1 and Kv.1.5 knockdown on MSU-induced NLRP3 inflammasome activation in J774.1 cells. DPO-1 (0–100 μM) were added 30 min before the addition of MSU ( a ). 24 h after the introduction of one of two siRNAs against Kv1.5 (Kv1.5-1 and Kv1.5-2) or a scramble siRNA, LPS-primed cells were stimulated by MSU ( c ). Shown are representative blots. (n = 4). * p

    Article Snippet: Kv1.5 may be a potential therapeutic target for gout-related inflammation and AF.

    Techniques: Concentration Assay, Activation Assay

    MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Article Snippet: Kv1.5 may be a potential therapeutic target for gout-related inflammation and AF.

    Techniques: Expressing

    Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Article Snippet: Kv1.5 may be a potential therapeutic target for gout-related inflammation and AF.

    Techniques: Concentration Assay

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Journal: bioRxiv

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    doi: 10.1101/2020.10.06.328237

    Figure Lengend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar cortex. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 immunoreactivity was predominantly found in the Purkinje cell bodies in mouse, using both antibodies, as well as in monkey and human, using Alomone antibodies. Weaker Purkinje cell bodies staining was noted in human and the weakest in monkey, using Santa Cruz antibodies. m: molecular layer; p: Purkinje cell layer; g: granular layer; * denotes Golgi cells type II. Scale bar=50μm.

    Article Snippet: Anti-Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5 and Kv1.6 antibodies were made against proteins listed below: Kv1.1, residues 416-495, HRETE GEEQA QLLHV SSPNL ASDSD LSRRS SSTIS KSEYM EIEED MNNSI AHYRQ ANIRT GNCTT ADQNC VNKSK LLTDV; Kv1.2, residues 417-499, YHRET EGEEQ AQYLQ VTSCP KIPSS PDLKK SRSAS TISKS DYMEI QEGVN NSNED FREEN LKTAN CTLAN TNYVN ITKML TDV; Kv1.3, residues 471-523, TLSKS EYMVI EEGGM NHSAF PQTPF KTGNS TATCT TNNNP NSCVN IKKIF TDV; Kv1.4, residues 589-655, PYLPS NLLKK FRSST SSSLG DKSEY LEMEE GVKES LCGKE EKCQG KGDDS ETDKN NCSNA KAVET DV; Kv1.5, residues 513-602, HRETD HEEQA ALKEE QGIQR RESGL DTGGQ RKVSC SKASF HKTGG PLEST DSIRR GSCPL EKCHL KAKSN VDLRR SLYAL CLDTS RETDL; Kv1.6, residues 463-530, NYFYH RETEQ EEQGQ YTHVT CGQPT PDLKA TDNGL GKPDF AEASR ERRSS YLPTP HRAYA EKRML TEV (manufacturer’s datasheet).

    Techniques: Immunohistochemistry, Staining

    Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Journal: bioRxiv

    Article Title: Species differences in the cerebellar distribution of six members of the Kv1 channel subfamily

    doi: 10.1101/2020.10.06.328237

    Figure Lengend Snippet: Cellular localizations of Kv1.5 subunit in the mouse (A, B); monkey (C, D) and human (E, F) cerebellar nuclei. Immunohistochemistry was obtained using Alomone (A, C, E) and Santa Cruz (B, D, F) anti-Kv1.5 subunit antibodies. Kv1.5 proteins were clearly detected in the cell bodies of cerebellar output neurons in all three species, using Alomone antibodies (A, C, E). Similar, although weaker, cell soma staining pattern was observed in mouse (B) and monkey (D), and the weakest in human (F), using Santa Cruz antibodies. Some staining in the surrounding neuropil was also observed. Scale bar=100μm in (B), otherwise scale bar=125μm.

    Article Snippet: Anti-Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5 and Kv1.6 antibodies were made against proteins listed below: Kv1.1, residues 416-495, HRETE GEEQA QLLHV SSPNL ASDSD LSRRS SSTIS KSEYM EIEED MNNSI AHYRQ ANIRT GNCTT ADQNC VNKSK LLTDV; Kv1.2, residues 417-499, YHRET EGEEQ AQYLQ VTSCP KIPSS PDLKK SRSAS TISKS DYMEI QEGVN NSNED FREEN LKTAN CTLAN TNYVN ITKML TDV; Kv1.3, residues 471-523, TLSKS EYMVI EEGGM NHSAF PQTPF KTGNS TATCT TNNNP NSCVN IKKIF TDV; Kv1.4, residues 589-655, PYLPS NLLKK FRSST SSSLG DKSEY LEMEE GVKES LCGKE EKCQG KGDDS ETDKN NCSNA KAVET DV; Kv1.5, residues 513-602, HRETD HEEQA ALKEE QGIQR RESGL DTGGQ RKVSC SKASF HKTGG PLEST DSIRR GSCPL EKCHL KAKSN VDLRR SLYAL CLDTS RETDL; Kv1.6, residues 463-530, NYFYH RETEQ EEQGQ YTHVT CGQPT PDLKA TDNGL GKPDF AEASR ERRSS YLPTP HRAYA EKRML TEV (manufacturer’s datasheet).

    Techniques: Immunohistochemistry, Staining

    HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Journal: Bosnian Journal of Basic Medical Sciences

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    doi:

    Figure Lengend Snippet: HIF-1 regulates hypoxia induced Kv channels (Kv1.2 Kv1.5, Kv2.1, and Kv9.3) mRNA expression in PASMCs. PCR amplified products are displayed in agarose gel for Kv1.2 (295 bp, A), Kv1.5 (340bp, B), Kv2.1 (451bp, C), Kv9.3 (568 bp, D) and β-actin

    Article Snippet: Since the Kv9.3 antibody was not available, only Kv1.2, Kv1.5, and Kv2.1 protein levels were examined.

    Techniques: Expressing, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis

    HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Journal: Bosnian Journal of Basic Medical Sciences

    Article Title: Hypoxia induces voltage-gated K+ (Kv) channel expression in pulmonary arterial smooth muscle cells through hypoxia-inducible factor-1 (HIF-1)

    doi:

    Figure Lengend Snippet: HIF-1 regulates hypoxia induced Kv channel (Kv1.2, Kv1.5, and Kv2.1) protein expression in PASMCs. Western blotting analysis of Kv1.2 (A), Kv1.5 (B) and Kv2.1 (C) channel proteins. Immunoblots of rat PASMCs proteins were incubated with affinity-purified

    Article Snippet: Since the Kv9.3 antibody was not available, only Kv1.2, Kv1.5, and Kv2.1 protein levels were examined.

    Techniques: Expressing, Western Blot, Incubation, Affinity Purification