kv1 5 antibody  (Alomone Labs)


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    Alomone Labs kv1 5 antibody
    (A) Meth significantly increased the <t>Kv1.3</t> mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on <t>Kv1.5</t> mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Kv1 5 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kv1 5 antibody - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3"

    Article Title: Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0088642

    (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Figure Legend Snippet: (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Techniques Used: Expressing

    Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Figure Legend Snippet: Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Techniques Used: Incubation, Western Blot, Concentration Assay, Expressing

    kv1 5 antibody  (Alomone Labs)


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    Alomone Labs kv1 5 antibody
    (A) Meth significantly increased the <t>Kv1.3</t> mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on <t>Kv1.5</t> mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Kv1 5 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kv1 5 antibody - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3"

    Article Title: Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0088642

    (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Figure Legend Snippet: (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Techniques Used: Expressing

    Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Figure Legend Snippet: Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Techniques Used: Incubation, Western Blot, Concentration Assay, Expressing

    kv1 5  (Alomone Labs)


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    Alomone Labs kv1 5
    Kv channel α subunit proteins are expressed in mouse myometrium . Results obtained from Western blots demonstrating the presence of immunoreactive bands for <t>Kv1.1,</t> Kv1.2, Kv1.3, Kv1.4, <t>Kv1.5,</t> Kv1.6, and Kv4.2 α-subunits in myometrium from nonpregnant (NP) and term-pregnant (P20) mice. Kv4.3 α-subunits were detected in the NP samples, but were undetectable in the term-pregnant mouse myometrium. Apparent molecular weights of each protein species are indicated at right. Different lanes contain samples from different animals, and each lane was loaded with 20 μg protein; 4–7 animals were assayed for each Kv channel α subunit protein.
    Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kv1 5 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "The role of voltage-gated potassium channels in the regulation of mouse uterine contractility"

    Article Title: The role of voltage-gated potassium channels in the regulation of mouse uterine contractility

    Journal: Reproductive biology and endocrinology : RB&E

    doi: 10.1186/1477-7827-5-41

    Kv channel α subunit proteins are expressed in mouse myometrium . Results obtained from Western blots demonstrating the presence of immunoreactive bands for Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, and Kv4.2 α-subunits in myometrium from nonpregnant (NP) and term-pregnant (P20) mice. Kv4.3 α-subunits were detected in the NP samples, but were undetectable in the term-pregnant mouse myometrium. Apparent molecular weights of each protein species are indicated at right. Different lanes contain samples from different animals, and each lane was loaded with 20 μg protein; 4–7 animals were assayed for each Kv channel α subunit protein.
    Figure Legend Snippet: Kv channel α subunit proteins are expressed in mouse myometrium . Results obtained from Western blots demonstrating the presence of immunoreactive bands for Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, and Kv4.2 α-subunits in myometrium from nonpregnant (NP) and term-pregnant (P20) mice. Kv4.3 α-subunits were detected in the NP samples, but were undetectable in the term-pregnant mouse myometrium. Apparent molecular weights of each protein species are indicated at right. Different lanes contain samples from different animals, and each lane was loaded with 20 μg protein; 4–7 animals were assayed for each Kv channel α subunit protein.

    Techniques Used: Western Blot

    Time course of loss of 4-AP responsiveness and Kv4.3 expression in pregnant mouse myometrium . Myometrial samples were obtained from nonpregnant (NP, n = 5), 7 days pregnant (P7, n = 3), 10 days pregnant (P10, n = 3), 15 days pregnant (P15, n = 4) and term-pregnant (P20, n = 5) mice. Panel A: Results from non-cumulative concentration-response experiments are presented as mean percentages of the maximal response to 4-AP in NP tissues. Panel B: Densitometry of Kv4.3 expression in the same samples evaluated in panel (A) and typical Western blot results demonstrating expression of Kv4.3 as well as Kv1.4 and γ-actin to confirm equal protein loading. Band densities are expressed in graph as a percentage of the maximal band density on each film; asterisks denote a significant difference (P = 0.01) between average NP and term-pregnant sample band densities.
    Figure Legend Snippet: Time course of loss of 4-AP responsiveness and Kv4.3 expression in pregnant mouse myometrium . Myometrial samples were obtained from nonpregnant (NP, n = 5), 7 days pregnant (P7, n = 3), 10 days pregnant (P10, n = 3), 15 days pregnant (P15, n = 4) and term-pregnant (P20, n = 5) mice. Panel A: Results from non-cumulative concentration-response experiments are presented as mean percentages of the maximal response to 4-AP in NP tissues. Panel B: Densitometry of Kv4.3 expression in the same samples evaluated in panel (A) and typical Western blot results demonstrating expression of Kv4.3 as well as Kv1.4 and γ-actin to confirm equal protein loading. Band densities are expressed in graph as a percentage of the maximal band density on each film; asterisks denote a significant difference (P = 0.01) between average NP and term-pregnant sample band densities.

    Techniques Used: Expressing, Concentration Assay, Western Blot

    polyclonal kv1 5 antibody  (Alomone Labs)


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    Alomone Labs polyclonal kv1 5 antibody
    A. qPCR analysis of <t>Kv1.1,</t> 1.3, 1.4 and 1.5 expression in preoptic area from GAD65-GFP and Kv4.2−/−;GAD65-GFP mice (n = 6 mice each). For normalization GAPDH was selected as housekeeping gene. Bars represent averaged normalized concentrations ±SD. ** represents significant differences between GAD65-GFP and Kv4.2−/−;GAD65-GFP groups P<0.01 (t-test). B. Western blot analysis of the expression of <t>Kv1.5</t> subunits. (A) Lysates prepared from the preoptic area of GAD65-GFP or Kv4.2−/−;GAD65-GFP mice (n = 6 animals for each genotype) were fractionated, transferred to PVDF membranes and probed with a specific anti-Kv1.5 antibody. Blots were also probed with antibodies against GAPDH to confirm equal loading of proteins. In each lane, anti-Kv1.5 antibody signals were quantified and normalized to the anti-GAPDH antibody signals. C. In Kv4.2−/−;GAD65-GFP preoptic area, the mean ±S.D. expression levels of Kv1.5 protein were significantly (**, p<0.01) higher than in GAD65-GFP preoptic area. Molecular masses are indicated on the blots by arrows.
    Polyclonal Kv1 5 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal kv1 5 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal kv1 5 antibody - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Electrical Remodeling of Preoptic GABAergic Neurons Involves the Kv1.5 Subunit"

    Article Title: Electrical Remodeling of Preoptic GABAergic Neurons Involves the Kv1.5 Subunit

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0096643

    A. qPCR analysis of Kv1.1, 1.3, 1.4 and 1.5 expression in preoptic area from GAD65-GFP and Kv4.2−/−;GAD65-GFP mice (n = 6 mice each). For normalization GAPDH was selected as housekeeping gene. Bars represent averaged normalized concentrations ±SD. ** represents significant differences between GAD65-GFP and Kv4.2−/−;GAD65-GFP groups P<0.01 (t-test). B. Western blot analysis of the expression of Kv1.5 subunits. (A) Lysates prepared from the preoptic area of GAD65-GFP or Kv4.2−/−;GAD65-GFP mice (n = 6 animals for each genotype) were fractionated, transferred to PVDF membranes and probed with a specific anti-Kv1.5 antibody. Blots were also probed with antibodies against GAPDH to confirm equal loading of proteins. In each lane, anti-Kv1.5 antibody signals were quantified and normalized to the anti-GAPDH antibody signals. C. In Kv4.2−/−;GAD65-GFP preoptic area, the mean ±S.D. expression levels of Kv1.5 protein were significantly (**, p<0.01) higher than in GAD65-GFP preoptic area. Molecular masses are indicated on the blots by arrows.
    Figure Legend Snippet: A. qPCR analysis of Kv1.1, 1.3, 1.4 and 1.5 expression in preoptic area from GAD65-GFP and Kv4.2−/−;GAD65-GFP mice (n = 6 mice each). For normalization GAPDH was selected as housekeeping gene. Bars represent averaged normalized concentrations ±SD. ** represents significant differences between GAD65-GFP and Kv4.2−/−;GAD65-GFP groups P<0.01 (t-test). B. Western blot analysis of the expression of Kv1.5 subunits. (A) Lysates prepared from the preoptic area of GAD65-GFP or Kv4.2−/−;GAD65-GFP mice (n = 6 animals for each genotype) were fractionated, transferred to PVDF membranes and probed with a specific anti-Kv1.5 antibody. Blots were also probed with antibodies against GAPDH to confirm equal loading of proteins. In each lane, anti-Kv1.5 antibody signals were quantified and normalized to the anti-GAPDH antibody signals. C. In Kv4.2−/−;GAD65-GFP preoptic area, the mean ±S.D. expression levels of Kv1.5 protein were significantly (**, p<0.01) higher than in GAD65-GFP preoptic area. Molecular masses are indicated on the blots by arrows.

    Techniques Used: Expressing, Western Blot

    antibodies against kv1 5  (Alomone Labs)


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    Alomone Labs antibodies against kv1 5
    HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the <t>Kv1.5</t> protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P <0.05, ** P <0.01 vs. control; $ P <0.05, # P <0.01 vs. Ang II group.
    Antibodies Against Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against kv1 5/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibodies against kv1 5 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury"

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0049758

    HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the Kv1.5 protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P <0.05, ** P <0.01 vs. control; $ P <0.05, # P <0.01 vs. Ang II group.
    Figure Legend Snippet: HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the Kv1.5 protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P <0.05, ** P <0.01 vs. control; $ P <0.05, # P <0.01 vs. Ang II group.

    Techniques Used: Incubation, Concentration Assay, Expressing, Fluorescence

    ( A ). HPAECs were treated with 2.5, 5, 10 nM Kv1.5 siRNA for 48 h and Kv1.5 protein expression was analyzed by western blot. * P <0.05, ** P <0.01 vs. Vehicle control, n = 3. ( B ). HPAECs were infected with adnovirus containing KCNA5 (Ad-Kv1.5) and control–adnovirus (Ad-con) for 12, 24, 48 h. * P <0.05, ** P <0.01 vs. Ad-con at corresponding time points, n = 3.
    Figure Legend Snippet: ( A ). HPAECs were treated with 2.5, 5, 10 nM Kv1.5 siRNA for 48 h and Kv1.5 protein expression was analyzed by western blot. * P <0.05, ** P <0.01 vs. Vehicle control, n = 3. ( B ). HPAECs were infected with adnovirus containing KCNA5 (Ad-Kv1.5) and control–adnovirus (Ad-con) for 12, 24, 48 h. * P <0.05, ** P <0.01 vs. Ad-con at corresponding time points, n = 3.

    Techniques Used: Expressing, Western Blot, Infection

    HPAECs were transfected with Kv1.5 siRNA (10 nM) or control siRNA for 48 h, or infected with adnovirus containing KCNA5 and control–adnovirus for 24 h, then treated with oxLDL (150 µg/ml) for further 24 h. The oxLDL-induced EC injury was detected by optical microscopy and DAPI staining. The optical microscope observation (A) and DAPI staining (B) show the morphological changes in Kv1.5 siRNA pretreated HPAECs. The mean values of percentages of apoptotic cells were summarized after DAPI staining in Kv1.5 siRNA (C)- and KCNA5 adnovirus- pretreated (D) HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.
    Figure Legend Snippet: HPAECs were transfected with Kv1.5 siRNA (10 nM) or control siRNA for 48 h, or infected with adnovirus containing KCNA5 and control–adnovirus for 24 h, then treated with oxLDL (150 µg/ml) for further 24 h. The oxLDL-induced EC injury was detected by optical microscopy and DAPI staining. The optical microscope observation (A) and DAPI staining (B) show the morphological changes in Kv1.5 siRNA pretreated HPAECs. The mean values of percentages of apoptotic cells were summarized after DAPI staining in Kv1.5 siRNA (C)- and KCNA5 adnovirus- pretreated (D) HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Techniques Used: Transfection, Infection, Microscopy, Staining

    Intracellular ROS levels were detected using DCFH-DA staining in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) & ( B ). Kv1.5 siRNA significantly attenuated oxLDL-induced endothelial ROS overproduction in HPAECs, as demonstrated by representative images from laser scanning confocal microscopy and bar graph showing fluorescence intensity measured in Multi-Mode Microplate Reader. ( C ). Bar graph shows that adnoviral KCNA5 gene transfer exaggerated oxLDL-induced endothelial ROS overproduction in HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.
    Figure Legend Snippet: Intracellular ROS levels were detected using DCFH-DA staining in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) & ( B ). Kv1.5 siRNA significantly attenuated oxLDL-induced endothelial ROS overproduction in HPAECs, as demonstrated by representative images from laser scanning confocal microscopy and bar graph showing fluorescence intensity measured in Multi-Mode Microplate Reader. ( C ). Bar graph shows that adnoviral KCNA5 gene transfer exaggerated oxLDL-induced endothelial ROS overproduction in HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Techniques Used: Staining, Transfection, Infection, Confocal Microscopy, Fluorescence

    The mitochondrial ROS generation was detected using MitoSOX reagents in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) The representative images from laser scanning confocal microscopy Kv1.5 siRNA significantly attenuated oxLDL-induced mitochondrial superoxide production in HPAECs. ( B ) & ( C ). The mitochondrial ROS levels in HPAECs transfected with Kv1.5 siRNA (B) or infected with adnovirus overexpression of Kv1.5 (C) were quantified by the fluorescent plate reader and expressed as the ratio of MitoSOX to Mitotracker. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.
    Figure Legend Snippet: The mitochondrial ROS generation was detected using MitoSOX reagents in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) The representative images from laser scanning confocal microscopy Kv1.5 siRNA significantly attenuated oxLDL-induced mitochondrial superoxide production in HPAECs. ( B ) & ( C ). The mitochondrial ROS levels in HPAECs transfected with Kv1.5 siRNA (B) or infected with adnovirus overexpression of Kv1.5 (C) were quantified by the fluorescent plate reader and expressed as the ratio of MitoSOX to Mitotracker. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Techniques Used: Transfection, Infection, Confocal Microscopy, Over Expression

    The UCP2 protein expression was detected by western blot in HPAECs transfected with Kv1.5-siRNA (A) and or infected with adnovirus containing KCNA5 (B). Digital photographs showing UCP2 protein expression are on the top panel and bar graph showing quantitative analysis of the total protein are on the lower panel. The values are presented as means ± SEM of 6 independent experiments. ** P <0.01 vs. corresponding control group; # P <0.01 vs. oxLDL group.
    Figure Legend Snippet: The UCP2 protein expression was detected by western blot in HPAECs transfected with Kv1.5-siRNA (A) and or infected with adnovirus containing KCNA5 (B). Digital photographs showing UCP2 protein expression are on the top panel and bar graph showing quantitative analysis of the total protein are on the lower panel. The values are presented as means ± SEM of 6 independent experiments. ** P <0.01 vs. corresponding control group; # P <0.01 vs. oxLDL group.

    Techniques Used: Expressing, Western Blot, Transfection, Infection

    anti kv1 5  (Alomone Labs)


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    Alomone Labs anti kv1 5
    Co-immunolocalization of <t>Kv1.5</t> (green) and SAP-97(red) in an aggregate of NZPCs.
    Anti Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti kv1 5/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti kv1 5 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "SAP97 and Cortactin Remodeling in Arrhythmogenic Purkinje Cells"

    Article Title: SAP97 and Cortactin Remodeling in Arrhythmogenic Purkinje Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0106830

    Co-immunolocalization of Kv1.5 (green) and SAP-97(red) in an aggregate of NZPCs.
    Figure Legend Snippet: Co-immunolocalization of Kv1.5 (green) and SAP-97(red) in an aggregate of NZPCs.

    Techniques Used:

    B , Costaining of the subcellular surface for Kv1.5 (green) and SAP-97 (red) in an NZPC. C , Localization of Kv1.5 (green) and SAP97 (red) in the cell ID area of an NZPC. D . Analyses of the merged image of Figure 3B illustrating the lack of true colocalization between SAP-97 (red) and Kv1.5 (green).Note the near absence of yellow signals. Scales were inset.
    Figure Legend Snippet: B , Costaining of the subcellular surface for Kv1.5 (green) and SAP-97 (red) in an NZPC. C , Localization of Kv1.5 (green) and SAP97 (red) in the cell ID area of an NZPC. D . Analyses of the merged image of Figure 3B illustrating the lack of true colocalization between SAP-97 (red) and Kv1.5 (green).Note the near absence of yellow signals. Scales were inset.

    Techniques Used:

    C , Enlarged image showing the colocalization of Kv1.5 and SAP-97 in IDs. D , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) in the center of an IZPC. E , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) at the subcellular surface of an IZPC. Compare to . Scales were inset.
    Figure Legend Snippet: C , Enlarged image showing the colocalization of Kv1.5 and SAP-97 in IDs. D , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) in the center of an IZPC. E , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) at the subcellular surface of an IZPC. Compare to . Scales were inset.

    Techniques Used:

    kv1 5  (Alomone Labs)


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    Alomone Labs kv1 5
    KMUP-1 restores 5-HT inhibited <t>Kv1.5</t> expression in PASMCs. Confocal immunofluorescence images of PASMCs stained with Kv1.5 proteins. PASMCs were incubated with 5-HT (10 μM) or 5-HT (10 μM) + KMUP-1 (1 μM). α-Actin was indicated by FITC-conjugated antibody (green) and Alexa Fluor ® 555-conjugated antibody was used to detect Kv1.5 (red). Images were obtained using the same laser intensity.
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    Images

    1) Product Images from "The Xanthine Derivative KMUP-1 Attenuates Serotonin-Induced Vasoconstriction and K + -Channel Inhibitory Activity via the PKC Pathway in Pulmonary Arteries"

    Article Title: The Xanthine Derivative KMUP-1 Attenuates Serotonin-Induced Vasoconstriction and K + -Channel Inhibitory Activity via the PKC Pathway in Pulmonary Arteries

    Journal: International Journal of Biological Sciences

    doi: 10.7150/ijbs.11127

    KMUP-1 restores 5-HT inhibited Kv1.5 expression in PASMCs. Confocal immunofluorescence images of PASMCs stained with Kv1.5 proteins. PASMCs were incubated with 5-HT (10 μM) or 5-HT (10 μM) + KMUP-1 (1 μM). α-Actin was indicated by FITC-conjugated antibody (green) and Alexa Fluor ® 555-conjugated antibody was used to detect Kv1.5 (red). Images were obtained using the same laser intensity.
    Figure Legend Snippet: KMUP-1 restores 5-HT inhibited Kv1.5 expression in PASMCs. Confocal immunofluorescence images of PASMCs stained with Kv1.5 proteins. PASMCs were incubated with 5-HT (10 μM) or 5-HT (10 μM) + KMUP-1 (1 μM). α-Actin was indicated by FITC-conjugated antibody (green) and Alexa Fluor ® 555-conjugated antibody was used to detect Kv1.5 (red). Images were obtained using the same laser intensity.

    Techniques Used: Expressing, Immunofluorescence, Staining, Incubation

    KMUP-1 (01, 1, 10 μM) reversed 5-HT (10 μM) inhibited (A) Kv1.5, (B) Kv2.1 and (C) BK Ca channel proteins in a dose-dependent manner in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone.
    Figure Legend Snippet: KMUP-1 (01, 1, 10 μM) reversed 5-HT (10 μM) inhibited (A) Kv1.5, (B) Kv2.1 and (C) BK Ca channel proteins in a dose-dependent manner in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone.

    Techniques Used: Protein Quantitation

    KMUP-1 activates AC/PKA-increased Kv1.5 proteins directly but does not modulate the 5-HT-mediated PKA pathway. 5-HT (10 μM) inhibition of Kv1.5 protein was not affected by the PKA inhibitor KT5720 (1 μM). 5-HT inhibition of Kv1.5 expression was reversed by KMUP-1 (1 μM), 8-Br-cAMP (100 μM), KMUP-1+KT5720 (1 μM) or KMUP-1+8-Br-cAMP in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. # P < 0.05, ## P < 0.01 compared with control; ** P < 0.01 compared with 5-HT alone. AC: Adenylate cyclase; NS: Not significant.
    Figure Legend Snippet: KMUP-1 activates AC/PKA-increased Kv1.5 proteins directly but does not modulate the 5-HT-mediated PKA pathway. 5-HT (10 μM) inhibition of Kv1.5 protein was not affected by the PKA inhibitor KT5720 (1 μM). 5-HT inhibition of Kv1.5 expression was reversed by KMUP-1 (1 μM), 8-Br-cAMP (100 μM), KMUP-1+KT5720 (1 μM) or KMUP-1+8-Br-cAMP in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. # P < 0.05, ## P < 0.01 compared with control; ** P < 0.01 compared with 5-HT alone. AC: Adenylate cyclase; NS: Not significant.

    Techniques Used: Inhibition, Expressing, Protein Quantitation

    KMUP-1 modulates 5-HT-inhibited Kv1.5 proteins via the PKC pathway. 5-HT inhibition of Kv1.5 protein was reversed by KMUP-1 (1 μM), chelerythrine (1 μM), KMUP-1+PMA (1 μM) or KMUP-1+chelerythrine, but not affected by the PKC activator PMA (1 μM). KMUP-1 reversed 5-HT-inhibited Kv1.5 protein and this effect was attenuated significantly by co-incubation with the PKC activator PMA, suggesting that KMUP-1 modulates the 5-HT-mediated PKC pathway. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone; ψ P < 0.05 5-HT+KMUP-1 compared with 5-HT+KMUP-1+PMA. PMA: Phorbol 12-myristate 13-acetate; NS: Not significant.
    Figure Legend Snippet: KMUP-1 modulates 5-HT-inhibited Kv1.5 proteins via the PKC pathway. 5-HT inhibition of Kv1.5 protein was reversed by KMUP-1 (1 μM), chelerythrine (1 μM), KMUP-1+PMA (1 μM) or KMUP-1+chelerythrine, but not affected by the PKC activator PMA (1 μM). KMUP-1 reversed 5-HT-inhibited Kv1.5 protein and this effect was attenuated significantly by co-incubation with the PKC activator PMA, suggesting that KMUP-1 modulates the 5-HT-mediated PKC pathway. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone; ψ P < 0.05 5-HT+KMUP-1 compared with 5-HT+KMUP-1+PMA. PMA: Phorbol 12-myristate 13-acetate; NS: Not significant.

    Techniques Used: Inhibition, Incubation, Protein Quantitation

    kv1 5  (Alomone Labs)


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    Alomone Labs kv1 5
    KMUP-1 restores 5-HT inhibited <t>Kv1.5</t> expression in PASMCs. Confocal immunofluorescence images of PASMCs stained with Kv1.5 proteins. PASMCs were incubated with 5-HT (10 μM) or 5-HT (10 μM) + KMUP-1 (1 μM). α-Actin was indicated by FITC-conjugated antibody (green) and Alexa Fluor ® 555-conjugated antibody was used to detect Kv1.5 (red). Images were obtained using the same laser intensity.
    Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "The Xanthine Derivative KMUP-1 Attenuates Serotonin-Induced Vasoconstriction and K + -Channel Inhibitory Activity via the PKC Pathway in Pulmonary Arteries"

    Article Title: The Xanthine Derivative KMUP-1 Attenuates Serotonin-Induced Vasoconstriction and K + -Channel Inhibitory Activity via the PKC Pathway in Pulmonary Arteries

    Journal: International Journal of Biological Sciences

    doi: 10.7150/ijbs.11127

    KMUP-1 restores 5-HT inhibited Kv1.5 expression in PASMCs. Confocal immunofluorescence images of PASMCs stained with Kv1.5 proteins. PASMCs were incubated with 5-HT (10 μM) or 5-HT (10 μM) + KMUP-1 (1 μM). α-Actin was indicated by FITC-conjugated antibody (green) and Alexa Fluor ® 555-conjugated antibody was used to detect Kv1.5 (red). Images were obtained using the same laser intensity.
    Figure Legend Snippet: KMUP-1 restores 5-HT inhibited Kv1.5 expression in PASMCs. Confocal immunofluorescence images of PASMCs stained with Kv1.5 proteins. PASMCs were incubated with 5-HT (10 μM) or 5-HT (10 μM) + KMUP-1 (1 μM). α-Actin was indicated by FITC-conjugated antibody (green) and Alexa Fluor ® 555-conjugated antibody was used to detect Kv1.5 (red). Images were obtained using the same laser intensity.

    Techniques Used: Expressing, Immunofluorescence, Staining, Incubation

    KMUP-1 (01, 1, 10 μM) reversed 5-HT (10 μM) inhibited (A) Kv1.5, (B) Kv2.1 and (C) BK Ca channel proteins in a dose-dependent manner in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone.
    Figure Legend Snippet: KMUP-1 (01, 1, 10 μM) reversed 5-HT (10 μM) inhibited (A) Kv1.5, (B) Kv2.1 and (C) BK Ca channel proteins in a dose-dependent manner in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone.

    Techniques Used: Protein Quantitation

    KMUP-1 activates AC/PKA-increased Kv1.5 proteins directly but does not modulate the 5-HT-mediated PKA pathway. 5-HT (10 μM) inhibition of Kv1.5 protein was not affected by the PKA inhibitor KT5720 (1 μM). 5-HT inhibition of Kv1.5 expression was reversed by KMUP-1 (1 μM), 8-Br-cAMP (100 μM), KMUP-1+KT5720 (1 μM) or KMUP-1+8-Br-cAMP in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. # P < 0.05, ## P < 0.01 compared with control; ** P < 0.01 compared with 5-HT alone. AC: Adenylate cyclase; NS: Not significant.
    Figure Legend Snippet: KMUP-1 activates AC/PKA-increased Kv1.5 proteins directly but does not modulate the 5-HT-mediated PKA pathway. 5-HT (10 μM) inhibition of Kv1.5 protein was not affected by the PKA inhibitor KT5720 (1 μM). 5-HT inhibition of Kv1.5 expression was reversed by KMUP-1 (1 μM), 8-Br-cAMP (100 μM), KMUP-1+KT5720 (1 μM) or KMUP-1+8-Br-cAMP in PASMCs. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. # P < 0.05, ## P < 0.01 compared with control; ** P < 0.01 compared with 5-HT alone. AC: Adenylate cyclase; NS: Not significant.

    Techniques Used: Inhibition, Expressing, Protein Quantitation

    KMUP-1 modulates 5-HT-inhibited Kv1.5 proteins via the PKC pathway. 5-HT inhibition of Kv1.5 protein was reversed by KMUP-1 (1 μM), chelerythrine (1 μM), KMUP-1+PMA (1 μM) or KMUP-1+chelerythrine, but not affected by the PKC activator PMA (1 μM). KMUP-1 reversed 5-HT-inhibited Kv1.5 protein and this effect was attenuated significantly by co-incubation with the PKC activator PMA, suggesting that KMUP-1 modulates the 5-HT-mediated PKC pathway. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone; ψ P < 0.05 5-HT+KMUP-1 compared with 5-HT+KMUP-1+PMA. PMA: Phorbol 12-myristate 13-acetate; NS: Not significant.
    Figure Legend Snippet: KMUP-1 modulates 5-HT-inhibited Kv1.5 proteins via the PKC pathway. 5-HT inhibition of Kv1.5 protein was reversed by KMUP-1 (1 μM), chelerythrine (1 μM), KMUP-1+PMA (1 μM) or KMUP-1+chelerythrine, but not affected by the PKC activator PMA (1 μM). KMUP-1 reversed 5-HT-inhibited Kv1.5 protein and this effect was attenuated significantly by co-incubation with the PKC activator PMA, suggesting that KMUP-1 modulates the 5-HT-mediated PKC pathway. Protein quantitation is shown in the lower panel. Data are means ± SE, n=6-8. ### P < 0.001 compared with control; * P < 0.05, ** P < 0.01, *** P < 0.001 compared with 5-HT alone; ψ P < 0.05 5-HT+KMUP-1 compared with 5-HT+KMUP-1+PMA. PMA: Phorbol 12-myristate 13-acetate; NS: Not significant.

    Techniques Used: Inhibition, Incubation, Protein Quantitation

    kv1 5  (Alomone Labs)


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    Alomone Labs kv1 5
    Expression of ion channels, AGE, RAGE and p16/Rb proteins in atrium of diabetic mice. (a) Representative blots and densitometry analysis of Cav1.2, K4.3, and <t>Kv1.5</t> proteins in atrial tissues from Control and DM groups ( n = 7–12). (b) Representative blots and densitometry analysis of AGE, RAGE, p16, Rb proteins in atrial tissues from Control and DM groups ( n = 6–12). * p < 0.05, ** p < 0.01 vs. Control group.
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    1) Product Images from "Advanced glycation end products induce senescence of atrial myocytes and increase susceptibility of atrial fibrillation in diabetic mice"

    Article Title: Advanced glycation end products induce senescence of atrial myocytes and increase susceptibility of atrial fibrillation in diabetic mice

    Journal: Aging Cell

    doi: 10.1111/acel.13734

    Expression of ion channels, AGE, RAGE and p16/Rb proteins in atrium of diabetic mice. (a) Representative blots and densitometry analysis of Cav1.2, K4.3, and Kv1.5 proteins in atrial tissues from Control and DM groups ( n = 7–12). (b) Representative blots and densitometry analysis of AGE, RAGE, p16, Rb proteins in atrial tissues from Control and DM groups ( n = 6–12). * p < 0.05, ** p < 0.01 vs. Control group.
    Figure Legend Snippet: Expression of ion channels, AGE, RAGE and p16/Rb proteins in atrium of diabetic mice. (a) Representative blots and densitometry analysis of Cav1.2, K4.3, and Kv1.5 proteins in atrial tissues from Control and DM groups ( n = 7–12). (b) Representative blots and densitometry analysis of AGE, RAGE, p16, Rb proteins in atrial tissues from Control and DM groups ( n = 6–12). * p < 0.05, ** p < 0.01 vs. Control group.

    Techniques Used: Expressing

    Effects of APD and ion channel currents on HL‐1 cells treated with AGEs or anti‐RAGE antibody. (a) Representative traces of APD ( n = 10–12) in HL‐1 cells treated with AGEs and anti‐RAGE antibody. (b) Representative traces (pulse protocol, inset), corresponding current–voltage ( I ‐ V ) relationship, mean data for voltage dependence activation, inactivation, and time course of recovery current for I Ca , L ( n = 6–12) in HL‐1 cells treated with AGEs or anti‐RAGE antibody. (c) Representative traces and current–voltage ( I ‐ V ) relationship for I Ku r ( n = 5–8) in HL‐1 cells treated with AGEs or anti‐RAGE antibody. (d) Representative blots and densitometry analysis of Cav1.2 and Kv1.5 proteins in HL‐1 cells treated with AGEs or anti‐RAGE antibody ( n = 4). * p < 0.05 vs. BSA group. # p < 0.05 vs. AGEs group.
    Figure Legend Snippet: Effects of APD and ion channel currents on HL‐1 cells treated with AGEs or anti‐RAGE antibody. (a) Representative traces of APD ( n = 10–12) in HL‐1 cells treated with AGEs and anti‐RAGE antibody. (b) Representative traces (pulse protocol, inset), corresponding current–voltage ( I ‐ V ) relationship, mean data for voltage dependence activation, inactivation, and time course of recovery current for I Ca , L ( n = 6–12) in HL‐1 cells treated with AGEs or anti‐RAGE antibody. (c) Representative traces and current–voltage ( I ‐ V ) relationship for I Ku r ( n = 5–8) in HL‐1 cells treated with AGEs or anti‐RAGE antibody. (d) Representative blots and densitometry analysis of Cav1.2 and Kv1.5 proteins in HL‐1 cells treated with AGEs or anti‐RAGE antibody ( n = 4). * p < 0.05 vs. BSA group. # p < 0.05 vs. AGEs group.

    Techniques Used: Activation Assay

    Alterations in senescence phenotype and expression levels of HL‐1 cells treated with AGEs, anti‐RAGE antibody, plasmid transfection. (a) SA‐β‐gal staining was used to elevate the positive rate of senescent cells treated with AGEs or anti‐RAGE antibody ( n = 4). (b) Flow cytometry was used to detect cell cycle distribution in HL‐1 cells treated with AGEs or anti‐RAGE antibody ( n = 4). (c) Representative blots and densitometry analysis of p16 and Rb proteins in HL‐1 cells treated with AGEs or anti‐RAGE antibody ( n = 4). (d) Representative blots and densitometry analysis of Cav1.2 and Kv1.5 proteins in HL‐1 cells intervene with p16 protein ( n = 3). (e) Representative blots and densitometry analysis of Cav1.2 and Kv1.5 proteins in HL‐1 cells intervene with Rb protein ( n = 3–5). * p < 0.05, ** p < 0.01 vs. BSA group or BSA + NC group. # p < 0.05, ## p < 0.01 vs. AGEs group or AGEs + NC group.
    Figure Legend Snippet: Alterations in senescence phenotype and expression levels of HL‐1 cells treated with AGEs, anti‐RAGE antibody, plasmid transfection. (a) SA‐β‐gal staining was used to elevate the positive rate of senescent cells treated with AGEs or anti‐RAGE antibody ( n = 4). (b) Flow cytometry was used to detect cell cycle distribution in HL‐1 cells treated with AGEs or anti‐RAGE antibody ( n = 4). (c) Representative blots and densitometry analysis of p16 and Rb proteins in HL‐1 cells treated with AGEs or anti‐RAGE antibody ( n = 4). (d) Representative blots and densitometry analysis of Cav1.2 and Kv1.5 proteins in HL‐1 cells intervene with p16 protein ( n = 3). (e) Representative blots and densitometry analysis of Cav1.2 and Kv1.5 proteins in HL‐1 cells intervene with Rb protein ( n = 3–5). * p < 0.05, ** p < 0.01 vs. BSA group or BSA + NC group. # p < 0.05, ## p < 0.01 vs. AGEs group or AGEs + NC group.

    Techniques Used: Expressing, Plasmid Preparation, Transfection, Staining, Flow Cytometry

    Schematic diagrams depicting proposed the mechanism of AGEs can accelerate cellular senescence of atrial myocytes through the p16/Rb pathways and increase the susceptibility to atrial fibrillation in diabetes. AGE and RAGE are accumulated in diabetes mellitus, which can accelerate cellular senescence and electrical remodeling of atrial myocytes through the p16/Rb signaling pathway. Meanwhile, reducing I Ca , L , I to and I Kur current density, extending the APD, and finally leading to atrial fibrillation. Mechanically, inhibition of RAGE can improve cellular senescence and atrial electrical remodeling; what is more, silencing p16 or Rb protein will promote atrial electrical remodeling by increasing the level of Cav1.2 and Kv1.5 proteins, revealing that RAGE or the p16/Rb pathway may be a potential therapeutic target for AF in diabetes.
    Figure Legend Snippet: Schematic diagrams depicting proposed the mechanism of AGEs can accelerate cellular senescence of atrial myocytes through the p16/Rb pathways and increase the susceptibility to atrial fibrillation in diabetes. AGE and RAGE are accumulated in diabetes mellitus, which can accelerate cellular senescence and electrical remodeling of atrial myocytes through the p16/Rb signaling pathway. Meanwhile, reducing I Ca , L , I to and I Kur current density, extending the APD, and finally leading to atrial fibrillation. Mechanically, inhibition of RAGE can improve cellular senescence and atrial electrical remodeling; what is more, silencing p16 or Rb protein will promote atrial electrical remodeling by increasing the level of Cav1.2 and Kv1.5 proteins, revealing that RAGE or the p16/Rb pathway may be a potential therapeutic target for AF in diabetes.

    Techniques Used: Inhibition

    kv1 5  (Alomone Labs)


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    Alomone Labs kv1 5
    Sequences of siRNA
    Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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

    Sequences of siRNA
    Figure Legend Snippet: Sequences of siRNA

    Techniques Used:

    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 < 0.01, † p < 0.05. IL-1β in the culture supernatant of the LPS-primed MSU-stimulated cells treated with DPO-1 ( b ) or transfected with one of the siRNAs against Kv1.5 or the scramble siRNA ( d ) were analyzed by ELISA (n = 4–6). * p < 0.01, † p < 0.05 vs.DPO-1(−)
    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 < 0.01, † p < 0.05. IL-1β in the culture supernatant of the LPS-primed MSU-stimulated cells treated with DPO-1 ( b ) or transfected with one of the siRNAs against Kv1.5 or the scramble siRNA ( d ) were analyzed by ELISA (n = 4–6). * p < 0.01, † p < 0.05 vs.DPO-1(−)

    Techniques Used: Concentration Assay, Activation Assay, Transfection, Enzyme-linked Immunosorbent Assay

    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 < 0.01, † p < 0.05; NS : not statistically significant. c The LPS-primed and subsequently stimulated with MSU cells were incubated with OPTI-MEM containing different K + concentrations (0–60 mM) overnight (n = 5). Shown are the representative blot. * p < 0.01 vs. LPS + MSU (+) & K + 0 mM. d IBs of disuccinimidyl suberate (DSS)-crosslinked ASC oligomers in lysates from untreated cells and LPS-primed cells treated with DPO-1 (1 μM) or vehicle 30 min before MSU stimulation (n = 5). e Representative immunofluorescence images of ASC speck formation in LPS-primed MSU-stimulated cells with and without DPO-1 (1 μM) treatment. Arrows denote ASC specks. Averaged numbers of specked cells (% total) are shown by the bar graph (n = 5–6 fields). * p < 0.01
    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 < 0.01, † p < 0.05; NS : not statistically significant. c The LPS-primed and subsequently stimulated with MSU cells were incubated with OPTI-MEM containing different K + concentrations (0–60 mM) overnight (n = 5). Shown are the representative blot. * p < 0.01 vs. LPS + MSU (+) & K + 0 mM. d IBs of disuccinimidyl suberate (DSS)-crosslinked ASC oligomers in lysates from untreated cells and LPS-primed cells treated with DPO-1 (1 μM) or vehicle 30 min before MSU stimulation (n = 5). e Representative immunofluorescence images of ASC speck formation in LPS-primed MSU-stimulated cells with and without DPO-1 (1 μM) treatment. Arrows denote ASC specks. Averaged numbers of specked cells (% total) are shown by the bar graph (n = 5–6 fields). * p < 0.01

    Techniques Used: Concentration Assay, Incubation, Immunofluorescence

    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 < 0.01. c Effects of MSU on Kv1.5 channel currents measured as DPO-1-sensitive currents. Whole-cell membrane currents were recorded from a single J774.1 cell without LPS and MSU treatments (none) and that with LPS priming and MSU stimulation (LPS + MSU). Shown are representative DPO-1-sensitive currents that were obtained by digital subtraction. Current–voltage relationships of currents are also shown (n = 6–8). * p < 0.01, † p < 0.05 vs. None
    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 < 0.01. c Effects of MSU on Kv1.5 channel currents measured as DPO-1-sensitive currents. Whole-cell membrane currents were recorded from a single J774.1 cell without LPS and MSU treatments (none) and that with LPS priming and MSU stimulation (LPS + MSU). Shown are representative DPO-1-sensitive currents that were obtained by digital subtraction. Current–voltage relationships of currents are also shown (n = 6–8). * p < 0.01, † p < 0.05 vs. None

    Techniques Used: Expressing

    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 < 0.05, * p < 0.01
    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 < 0.05, * p < 0.01

    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 < 0.01. HL-1 cells were transfected with a scramble siRNA or a siRNA against Kv1.5 24 h before incubation with CM + LPS + MSU. Show are representative blots ( e ) (n = 5–11) and IL-1β concentrations measured by ELISA ( f ) (n = 6). † p < 0.05, * p < 0.01
    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 < 0.01. HL-1 cells were transfected with a scramble siRNA or a siRNA against Kv1.5 24 h before incubation with CM + LPS + MSU. Show are representative blots ( e ) (n = 5–11) and IL-1β concentrations measured by ELISA ( f ) (n = 6). † p < 0.05, * p < 0.01

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

    rabbit anti mouse nav1 5  (Alomone Labs)


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    Alomone Labs rabbit anti mouse nav1 5
    Rabbit Anti Mouse Nav1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Alomone Labs kv1 5 antibody
    (A) Meth significantly increased the <t>Kv1.3</t> mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on <t>Kv1.5</t> mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.
    Kv1 5 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    kv1 5 antibody - by Bioz Stars, 2023-01
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    94
    Alomone Labs kv1 5
    Kv channel α subunit proteins are expressed in mouse myometrium . Results obtained from Western blots demonstrating the presence of immunoreactive bands for <t>Kv1.1,</t> Kv1.2, Kv1.3, Kv1.4, <t>Kv1.5,</t> Kv1.6, and Kv4.2 α-subunits in myometrium from nonpregnant (NP) and term-pregnant (P20) mice. Kv4.3 α-subunits were detected in the NP samples, but were undetectable in the term-pregnant mouse myometrium. Apparent molecular weights of each protein species are indicated at right. Different lanes contain samples from different animals, and each lane was loaded with 20 μg protein; 4–7 animals were assayed for each Kv channel α subunit protein.
    Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5/product/Alomone Labs
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    Alomone Labs polyclonal kv1 5 antibody
    A. qPCR analysis of <t>Kv1.1,</t> 1.3, 1.4 and 1.5 expression in preoptic area from GAD65-GFP and Kv4.2−/−;GAD65-GFP mice (n = 6 mice each). For normalization GAPDH was selected as housekeeping gene. Bars represent averaged normalized concentrations ±SD. ** represents significant differences between GAD65-GFP and Kv4.2−/−;GAD65-GFP groups P<0.01 (t-test). B. Western blot analysis of the expression of <t>Kv1.5</t> subunits. (A) Lysates prepared from the preoptic area of GAD65-GFP or Kv4.2−/−;GAD65-GFP mice (n = 6 animals for each genotype) were fractionated, transferred to PVDF membranes and probed with a specific anti-Kv1.5 antibody. Blots were also probed with antibodies against GAPDH to confirm equal loading of proteins. In each lane, anti-Kv1.5 antibody signals were quantified and normalized to the anti-GAPDH antibody signals. C. In Kv4.2−/−;GAD65-GFP preoptic area, the mean ±S.D. expression levels of Kv1.5 protein were significantly (**, p<0.01) higher than in GAD65-GFP preoptic area. Molecular masses are indicated on the blots by arrows.
    Polyclonal Kv1 5 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal kv1 5 antibody/product/Alomone Labs
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    Alomone Labs antibodies against kv1 5
    HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the <t>Kv1.5</t> protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P <0.05, ** P <0.01 vs. control; $ P <0.05, # P <0.01 vs. Ang II group.
    Antibodies Against Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibodies against kv1 5/product/Alomone Labs
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    Alomone Labs anti kv1 5
    Co-immunolocalization of <t>Kv1.5</t> (green) and SAP-97(red) in an aggregate of NZPCs.
    Anti Kv1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Alomone Labs rabbit anti mouse nav1 5
    Co-immunolocalization of <t>Kv1.5</t> (green) and SAP-97(red) in an aggregate of NZPCs.
    Rabbit Anti Mouse Nav1 5, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti mouse nav1 5/product/Alomone Labs
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    Image Search Results


    (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Journal: PLoS ONE

    Article Title: Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3

    doi: 10.1371/journal.pone.0088642

    Figure Lengend Snippet: (A) Meth significantly increased the Kv1.3 mRNA expression, while MgTx ameliorated the expression of Kv1.3 mediated by Meth. (B) Meth showed no obvious impact on Kv1.5 mRNA expression. Each data point represents mean±SD of mRNA levels from at least three separate experiments in which treatments were performed in triplicates.* and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Article Snippet: After blocking with 5% nonfat milk, the membranes were incubated with the polyclonal Kv1.3, Kv1.5 antibody (Alomone Labs,Israel).

    Techniques: Expressing

    Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Journal: PLoS ONE

    Article Title: Effect of Methamphetamine on the Microglial Damage: Role of Potassium Channel Kv1.3

    doi: 10.1371/journal.pone.0088642

    Figure Lengend Snippet: Microglial cells were incubated with Meth, and the level of Kv1.3, Kv1.5 proteins were detected by western-blot. (A) Meth (0, 100,300 µM) up-regulated Kv1.3 protein in a concentration dependent manner. (B) Meth (300 µM) obviously up-regulated Kv1.3 protein expression in 12, 24 and 48 h, and displayed a time-dependent way. (C) Meth mediated up-regulation of Kv1.3 protein level was partly attenuated by MgTx (10 nM). (D) and (E) Meth (300 µM) showed no impact on Kv1.5 protein level. * and # indicate significant differences compared with the control and condition stimulated by Meth respectively (p<0.05 by ANOVA), each data represents mean±SD at least three separate experiments.

    Article Snippet: After blocking with 5% nonfat milk, the membranes were incubated with the polyclonal Kv1.3, Kv1.5 antibody (Alomone Labs,Israel).

    Techniques: Incubation, Western Blot, Concentration Assay, Expressing

    Kv channel α subunit proteins are expressed in mouse myometrium . Results obtained from Western blots demonstrating the presence of immunoreactive bands for Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, and Kv4.2 α-subunits in myometrium from nonpregnant (NP) and term-pregnant (P20) mice. Kv4.3 α-subunits were detected in the NP samples, but were undetectable in the term-pregnant mouse myometrium. Apparent molecular weights of each protein species are indicated at right. Different lanes contain samples from different animals, and each lane was loaded with 20 μg protein; 4–7 animals were assayed for each Kv channel α subunit protein.

    Journal: Reproductive biology and endocrinology : RB&E

    Article Title: The role of voltage-gated potassium channels in the regulation of mouse uterine contractility

    doi: 10.1186/1477-7827-5-41

    Figure Lengend Snippet: Kv channel α subunit proteins are expressed in mouse myometrium . Results obtained from Western blots demonstrating the presence of immunoreactive bands for Kv1.1, Kv1.2, Kv1.3, Kv1.4, Kv1.5, Kv1.6, and Kv4.2 α-subunits in myometrium from nonpregnant (NP) and term-pregnant (P20) mice. Kv4.3 α-subunits were detected in the NP samples, but were undetectable in the term-pregnant mouse myometrium. Apparent molecular weights of each protein species are indicated at right. Different lanes contain samples from different animals, and each lane was loaded with 20 μg protein; 4–7 animals were assayed for each Kv channel α subunit protein.

    Article Snippet: Incubations with primary antibodies (all purchased from Alomone Labs, Jerusalem: Kv1.1 (cat. #AN-03), Kv1.2 (cat. #AN-04), Kv1.3 (cat. #AN-03), Kv1.4 (cat. #AN-06), Kv1.5 (cat. #AN-04), Kv1.6 (cat. #AN-03), Kv4.2 (cat. #AN-04) and Kv4.3 (cat. #AN-04)) at dilutions of 1:200-500 were performed in Tris-saline solution containing nonfat milk at 0.05% (w/v), Tween 20 at 0.05% (v/v) and sodium azide at 0.02% (w/v) for 1.5 hours at room temperature with rocking.

    Techniques: Western Blot

    Time course of loss of 4-AP responsiveness and Kv4.3 expression in pregnant mouse myometrium . Myometrial samples were obtained from nonpregnant (NP, n = 5), 7 days pregnant (P7, n = 3), 10 days pregnant (P10, n = 3), 15 days pregnant (P15, n = 4) and term-pregnant (P20, n = 5) mice. Panel A: Results from non-cumulative concentration-response experiments are presented as mean percentages of the maximal response to 4-AP in NP tissues. Panel B: Densitometry of Kv4.3 expression in the same samples evaluated in panel (A) and typical Western blot results demonstrating expression of Kv4.3 as well as Kv1.4 and γ-actin to confirm equal protein loading. Band densities are expressed in graph as a percentage of the maximal band density on each film; asterisks denote a significant difference (P = 0.01) between average NP and term-pregnant sample band densities.

    Journal: Reproductive biology and endocrinology : RB&E

    Article Title: The role of voltage-gated potassium channels in the regulation of mouse uterine contractility

    doi: 10.1186/1477-7827-5-41

    Figure Lengend Snippet: Time course of loss of 4-AP responsiveness and Kv4.3 expression in pregnant mouse myometrium . Myometrial samples were obtained from nonpregnant (NP, n = 5), 7 days pregnant (P7, n = 3), 10 days pregnant (P10, n = 3), 15 days pregnant (P15, n = 4) and term-pregnant (P20, n = 5) mice. Panel A: Results from non-cumulative concentration-response experiments are presented as mean percentages of the maximal response to 4-AP in NP tissues. Panel B: Densitometry of Kv4.3 expression in the same samples evaluated in panel (A) and typical Western blot results demonstrating expression of Kv4.3 as well as Kv1.4 and γ-actin to confirm equal protein loading. Band densities are expressed in graph as a percentage of the maximal band density on each film; asterisks denote a significant difference (P = 0.01) between average NP and term-pregnant sample band densities.

    Article Snippet: Incubations with primary antibodies (all purchased from Alomone Labs, Jerusalem: Kv1.1 (cat. #AN-03), Kv1.2 (cat. #AN-04), Kv1.3 (cat. #AN-03), Kv1.4 (cat. #AN-06), Kv1.5 (cat. #AN-04), Kv1.6 (cat. #AN-03), Kv4.2 (cat. #AN-04) and Kv4.3 (cat. #AN-04)) at dilutions of 1:200-500 were performed in Tris-saline solution containing nonfat milk at 0.05% (w/v), Tween 20 at 0.05% (v/v) and sodium azide at 0.02% (w/v) for 1.5 hours at room temperature with rocking.

    Techniques: Expressing, Concentration Assay, Western Blot

    A. qPCR analysis of Kv1.1, 1.3, 1.4 and 1.5 expression in preoptic area from GAD65-GFP and Kv4.2−/−;GAD65-GFP mice (n = 6 mice each). For normalization GAPDH was selected as housekeeping gene. Bars represent averaged normalized concentrations ±SD. ** represents significant differences between GAD65-GFP and Kv4.2−/−;GAD65-GFP groups P<0.01 (t-test). B. Western blot analysis of the expression of Kv1.5 subunits. (A) Lysates prepared from the preoptic area of GAD65-GFP or Kv4.2−/−;GAD65-GFP mice (n = 6 animals for each genotype) were fractionated, transferred to PVDF membranes and probed with a specific anti-Kv1.5 antibody. Blots were also probed with antibodies against GAPDH to confirm equal loading of proteins. In each lane, anti-Kv1.5 antibody signals were quantified and normalized to the anti-GAPDH antibody signals. C. In Kv4.2−/−;GAD65-GFP preoptic area, the mean ±S.D. expression levels of Kv1.5 protein were significantly (**, p<0.01) higher than in GAD65-GFP preoptic area. Molecular masses are indicated on the blots by arrows.

    Journal: PLoS ONE

    Article Title: Electrical Remodeling of Preoptic GABAergic Neurons Involves the Kv1.5 Subunit

    doi: 10.1371/journal.pone.0096643

    Figure Lengend Snippet: A. qPCR analysis of Kv1.1, 1.3, 1.4 and 1.5 expression in preoptic area from GAD65-GFP and Kv4.2−/−;GAD65-GFP mice (n = 6 mice each). For normalization GAPDH was selected as housekeeping gene. Bars represent averaged normalized concentrations ±SD. ** represents significant differences between GAD65-GFP and Kv4.2−/−;GAD65-GFP groups P<0.01 (t-test). B. Western blot analysis of the expression of Kv1.5 subunits. (A) Lysates prepared from the preoptic area of GAD65-GFP or Kv4.2−/−;GAD65-GFP mice (n = 6 animals for each genotype) were fractionated, transferred to PVDF membranes and probed with a specific anti-Kv1.5 antibody. Blots were also probed with antibodies against GAPDH to confirm equal loading of proteins. In each lane, anti-Kv1.5 antibody signals were quantified and normalized to the anti-GAPDH antibody signals. C. In Kv4.2−/−;GAD65-GFP preoptic area, the mean ±S.D. expression levels of Kv1.5 protein were significantly (**, p<0.01) higher than in GAD65-GFP preoptic area. Molecular masses are indicated on the blots by arrows.

    Article Snippet: The polyclonal Kv1.5 antibody (dilution 1∶500) was from Alomone labs (#APC-004).

    Techniques: Expressing, Western Blot

    HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the Kv1.5 protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P <0.05, ** P <0.01 vs. control; $ P <0.05, # P <0.01 vs. Ang II group.

    Journal: PLoS ONE

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    doi: 10.1371/journal.pone.0049758

    Figure Lengend Snippet: HUVECs were incubated with AngII at different concentrations for different times. Ang II time (A)- or concentration (B)-dependently enhanced the Kv1.5 protein expression. Pretreatment with MT for 30 min inhibited Ang II (2 µM, 24 h)-induced increase in intracellular ROS levels in HUVECs in a concentration-dependent manner (C), as determined by DCF fluorescence. MT also significantly attenuated Ang II (2 µM, 24 h)-induced HUVEC injury. Incubation of HPAECs with oxLDL at the concentration of 37.5, 75 and 150 µg/ml significantly increased EC injury (D), intracellular ROS production (E) and Kv1.5 protein expression (F) in a concentration-dependent manner. The values were presented as ± SEM of 6 independent experiments for Ang II- or oxLDL-treatment, respectively. * P <0.05, ** P <0.01 vs. control; $ P <0.05, # P <0.01 vs. Ang II group.

    Article Snippet: The membranes were probed with antibodies against Kv1.5 (Alomone Labs, USA) or UCP2 (Biolegend, USA), respectively.

    Techniques: Incubation, Concentration Assay, Expressing, Fluorescence

    ( A ). HPAECs were treated with 2.5, 5, 10 nM Kv1.5 siRNA for 48 h and Kv1.5 protein expression was analyzed by western blot. * P <0.05, ** P <0.01 vs. Vehicle control, n = 3. ( B ). HPAECs were infected with adnovirus containing KCNA5 (Ad-Kv1.5) and control–adnovirus (Ad-con) for 12, 24, 48 h. * P <0.05, ** P <0.01 vs. Ad-con at corresponding time points, n = 3.

    Journal: PLoS ONE

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    doi: 10.1371/journal.pone.0049758

    Figure Lengend Snippet: ( A ). HPAECs were treated with 2.5, 5, 10 nM Kv1.5 siRNA for 48 h and Kv1.5 protein expression was analyzed by western blot. * P <0.05, ** P <0.01 vs. Vehicle control, n = 3. ( B ). HPAECs were infected with adnovirus containing KCNA5 (Ad-Kv1.5) and control–adnovirus (Ad-con) for 12, 24, 48 h. * P <0.05, ** P <0.01 vs. Ad-con at corresponding time points, n = 3.

    Article Snippet: The membranes were probed with antibodies against Kv1.5 (Alomone Labs, USA) or UCP2 (Biolegend, USA), respectively.

    Techniques: Expressing, Western Blot, Infection

    HPAECs were transfected with Kv1.5 siRNA (10 nM) or control siRNA for 48 h, or infected with adnovirus containing KCNA5 and control–adnovirus for 24 h, then treated with oxLDL (150 µg/ml) for further 24 h. The oxLDL-induced EC injury was detected by optical microscopy and DAPI staining. The optical microscope observation (A) and DAPI staining (B) show the morphological changes in Kv1.5 siRNA pretreated HPAECs. The mean values of percentages of apoptotic cells were summarized after DAPI staining in Kv1.5 siRNA (C)- and KCNA5 adnovirus- pretreated (D) HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Journal: PLoS ONE

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    doi: 10.1371/journal.pone.0049758

    Figure Lengend Snippet: HPAECs were transfected with Kv1.5 siRNA (10 nM) or control siRNA for 48 h, or infected with adnovirus containing KCNA5 and control–adnovirus for 24 h, then treated with oxLDL (150 µg/ml) for further 24 h. The oxLDL-induced EC injury was detected by optical microscopy and DAPI staining. The optical microscope observation (A) and DAPI staining (B) show the morphological changes in Kv1.5 siRNA pretreated HPAECs. The mean values of percentages of apoptotic cells were summarized after DAPI staining in Kv1.5 siRNA (C)- and KCNA5 adnovirus- pretreated (D) HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Article Snippet: The membranes were probed with antibodies against Kv1.5 (Alomone Labs, USA) or UCP2 (Biolegend, USA), respectively.

    Techniques: Transfection, Infection, Microscopy, Staining

    Intracellular ROS levels were detected using DCFH-DA staining in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) & ( B ). Kv1.5 siRNA significantly attenuated oxLDL-induced endothelial ROS overproduction in HPAECs, as demonstrated by representative images from laser scanning confocal microscopy and bar graph showing fluorescence intensity measured in Multi-Mode Microplate Reader. ( C ). Bar graph shows that adnoviral KCNA5 gene transfer exaggerated oxLDL-induced endothelial ROS overproduction in HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Journal: PLoS ONE

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    doi: 10.1371/journal.pone.0049758

    Figure Lengend Snippet: Intracellular ROS levels were detected using DCFH-DA staining in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) & ( B ). Kv1.5 siRNA significantly attenuated oxLDL-induced endothelial ROS overproduction in HPAECs, as demonstrated by representative images from laser scanning confocal microscopy and bar graph showing fluorescence intensity measured in Multi-Mode Microplate Reader. ( C ). Bar graph shows that adnoviral KCNA5 gene transfer exaggerated oxLDL-induced endothelial ROS overproduction in HPAECs. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Article Snippet: The membranes were probed with antibodies against Kv1.5 (Alomone Labs, USA) or UCP2 (Biolegend, USA), respectively.

    Techniques: Staining, Transfection, Infection, Confocal Microscopy, Fluorescence

    The mitochondrial ROS generation was detected using MitoSOX reagents in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) The representative images from laser scanning confocal microscopy Kv1.5 siRNA significantly attenuated oxLDL-induced mitochondrial superoxide production in HPAECs. ( B ) & ( C ). The mitochondrial ROS levels in HPAECs transfected with Kv1.5 siRNA (B) or infected with adnovirus overexpression of Kv1.5 (C) were quantified by the fluorescent plate reader and expressed as the ratio of MitoSOX to Mitotracker. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Journal: PLoS ONE

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    doi: 10.1371/journal.pone.0049758

    Figure Lengend Snippet: The mitochondrial ROS generation was detected using MitoSOX reagents in HPAECs transfected with Kv1.5 siRNA (10 nM) or infected with adnovirus containing KCNA5 , which were treated with oxLDL (150 µg/ml) for further 1 h. ( A ) The representative images from laser scanning confocal microscopy Kv1.5 siRNA significantly attenuated oxLDL-induced mitochondrial superoxide production in HPAECs. ( B ) & ( C ). The mitochondrial ROS levels in HPAECs transfected with Kv1.5 siRNA (B) or infected with adnovirus overexpression of Kv1.5 (C) were quantified by the fluorescent plate reader and expressed as the ratio of MitoSOX to Mitotracker. The values are presented as means ± SEM of 6 independent experiments. * P <0.05, ** P <0.01 vs. Vehicle control; # P <0.05, ## P <0.01 vs. Ad-con.

    Article Snippet: The membranes were probed with antibodies against Kv1.5 (Alomone Labs, USA) or UCP2 (Biolegend, USA), respectively.

    Techniques: Transfection, Infection, Confocal Microscopy, Over Expression

    The UCP2 protein expression was detected by western blot in HPAECs transfected with Kv1.5-siRNA (A) and or infected with adnovirus containing KCNA5 (B). Digital photographs showing UCP2 protein expression are on the top panel and bar graph showing quantitative analysis of the total protein are on the lower panel. The values are presented as means ± SEM of 6 independent experiments. ** P <0.01 vs. corresponding control group; # P <0.01 vs. oxLDL group.

    Journal: PLoS ONE

    Article Title: Involvement of Kv1.5 Protein in Oxidative Vascular Endothelial Cell Injury

    doi: 10.1371/journal.pone.0049758

    Figure Lengend Snippet: The UCP2 protein expression was detected by western blot in HPAECs transfected with Kv1.5-siRNA (A) and or infected with adnovirus containing KCNA5 (B). Digital photographs showing UCP2 protein expression are on the top panel and bar graph showing quantitative analysis of the total protein are on the lower panel. The values are presented as means ± SEM of 6 independent experiments. ** P <0.01 vs. corresponding control group; # P <0.01 vs. oxLDL group.

    Article Snippet: The membranes were probed with antibodies against Kv1.5 (Alomone Labs, USA) or UCP2 (Biolegend, USA), respectively.

    Techniques: Expressing, Western Blot, Transfection, Infection

    Co-immunolocalization of Kv1.5 (green) and SAP-97(red) in an aggregate of NZPCs.

    Journal: PLoS ONE

    Article Title: SAP97 and Cortactin Remodeling in Arrhythmogenic Purkinje Cells

    doi: 10.1371/journal.pone.0106830

    Figure Lengend Snippet: Co-immunolocalization of Kv1.5 (green) and SAP-97(red) in an aggregate of NZPCs.

    Article Snippet: The antibodies used in this study include rabbit anti-Kv1.5 (1∶100, Alomone labs), mouse anti-SAP97 (1∶100, Santa Cruz), mouse anti-cortactin (1∶200, Millipore), rabbit anti-cortactin (1∶100, Cell Applications), and mouse anti-N-cadherin (1∶100, BD).

    Techniques:

    B , Costaining of the subcellular surface for Kv1.5 (green) and SAP-97 (red) in an NZPC. C , Localization of Kv1.5 (green) and SAP97 (red) in the cell ID area of an NZPC. D . Analyses of the merged image of Figure 3B illustrating the lack of true colocalization between SAP-97 (red) and Kv1.5 (green).Note the near absence of yellow signals. Scales were inset.

    Journal: PLoS ONE

    Article Title: SAP97 and Cortactin Remodeling in Arrhythmogenic Purkinje Cells

    doi: 10.1371/journal.pone.0106830

    Figure Lengend Snippet: B , Costaining of the subcellular surface for Kv1.5 (green) and SAP-97 (red) in an NZPC. C , Localization of Kv1.5 (green) and SAP97 (red) in the cell ID area of an NZPC. D . Analyses of the merged image of Figure 3B illustrating the lack of true colocalization between SAP-97 (red) and Kv1.5 (green).Note the near absence of yellow signals. Scales were inset.

    Article Snippet: The antibodies used in this study include rabbit anti-Kv1.5 (1∶100, Alomone labs), mouse anti-SAP97 (1∶100, Santa Cruz), mouse anti-cortactin (1∶200, Millipore), rabbit anti-cortactin (1∶100, Cell Applications), and mouse anti-N-cadherin (1∶100, BD).

    Techniques:

    C , Enlarged image showing the colocalization of Kv1.5 and SAP-97 in IDs. D , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) in the center of an IZPC. E , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) at the subcellular surface of an IZPC. Compare to . Scales were inset.

    Journal: PLoS ONE

    Article Title: SAP97 and Cortactin Remodeling in Arrhythmogenic Purkinje Cells

    doi: 10.1371/journal.pone.0106830

    Figure Lengend Snippet: C , Enlarged image showing the colocalization of Kv1.5 and SAP-97 in IDs. D , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) in the center of an IZPC. E , Enlarged image showing the localization of Kv1.5 (green) and SAP-97 (red) at the subcellular surface of an IZPC. Compare to . Scales were inset.

    Article Snippet: The antibodies used in this study include rabbit anti-Kv1.5 (1∶100, Alomone labs), mouse anti-SAP97 (1∶100, Santa Cruz), mouse anti-cortactin (1∶200, Millipore), rabbit anti-cortactin (1∶100, Cell Applications), and mouse anti-N-cadherin (1∶100, BD).

    Techniques: