girk2  (Alomone Labs)


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    Alomone Labs girk2
    Acute cocaine decreases the density of <t>Girk2</t> on the plasma membrane of VTA DA neurons
    Girk2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/girk2/product/Alomone Labs
    Average 88 stars, based on 1 article reviews
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    girk2 - by Bioz Stars, 2022-12
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    1) Product Images from "Acute cocaine exposure weakens GABAB receptor-dependent Girk signaling in dopamine neurons of the ventral tegmental area"

    Article Title: Acute cocaine exposure weakens GABAB receptor-dependent Girk signaling in dopamine neurons of the ventral tegmental area

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    doi: 10.1523/JNEUROSCI.0494-11.2011

    Acute cocaine decreases the density of Girk2 on the plasma membrane of VTA DA neurons
    Figure Legend Snippet: Acute cocaine decreases the density of Girk2 on the plasma membrane of VTA DA neurons

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    Alomone Labs girk2
    Acute cocaine decreases the density of <t>Girk2</t> on the plasma membrane of VTA DA neurons
    Girk2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/girk2/product/Alomone Labs
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    girk2 - by Bioz Stars, 2022-12
    88/100 stars
      Buy from Supplier

    90
    Alomone Labs kvlqt1
    HERG and <t>KvLQT1</t> coimmunoprecipitations. A : immunoblots for HERG and KvLQT1 proteins. CHO cells were transiently transfected with expression vectors encoding wild-type, pore mutant, and respective Flag-tagged forms of HERG and KvLQT1, as shown. Left , cell lysates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-KvLQT1 ( bottom ) antisera. Right , cell lysates were immunoprecipitated with anti-Flag/protein A/G PLUS-agarose (*) or IgG/protein A/G PLUS-agarose (o). Immunoprecipitates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-KvLQT1 ( bottom ) antisera. B : immunoblots for HERG and Flag-tagged KvLQT1 and Kir2.1 proteins. CHO cells stably expressing HA-HERG were transiently transfected with the following expression plasmids: pcDNA3 ( lane 1 ), pcDNA3-Flag-KvLQT1 ( lane 2 ), pcDNA3-KvLQT1-Y315S ( lane 3 ), or pcDNA3-Flag-Kir2.1 ( lane 4 ). Left , cell lysates were separated by SDS-PAGE, blotted, and probed with anti-HERG antisera. Right , cell lysates were immunoprecipitated with anti-Flag/protein A/G PLUS-agarose. Immunoprecipitates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-Flag ( bottom ) antisera . All experiments were carried out in triplicate. Shown are representative immunoblots.
    Kvlqt1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 1 article reviews
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    Acute cocaine decreases the density of Girk2 on the plasma membrane of VTA DA neurons

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Acute cocaine exposure weakens GABAB receptor-dependent Girk signaling in dopamine neurons of the ventral tegmental area

    doi: 10.1523/JNEUROSCI.0494-11.2011

    Figure Lengend Snippet: Acute cocaine decreases the density of Girk2 on the plasma membrane of VTA DA neurons

    Article Snippet: We did, however, detect a significant cocaine-induced decrease in the density of Girk2 ( , median immunoparticles/μm2 ; saline: 1.9 vs. cocaine: 0.7, n=49-54; U=593, P < 0.001) but not GABAB R1 (not shown, median immunoparticles/μm2 ; saline: 1.1 vs. cocaine: 1.1, n=52-54; U=1376, P =0.9) proteins in the plasma membrane of TH+ dendrites of the VTA.

    Techniques:

    HERG and KvLQT1 coimmunoprecipitations. A : immunoblots for HERG and KvLQT1 proteins. CHO cells were transiently transfected with expression vectors encoding wild-type, pore mutant, and respective Flag-tagged forms of HERG and KvLQT1, as shown. Left , cell lysates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-KvLQT1 ( bottom ) antisera. Right , cell lysates were immunoprecipitated with anti-Flag/protein A/G PLUS-agarose (*) or IgG/protein A/G PLUS-agarose (o). Immunoprecipitates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-KvLQT1 ( bottom ) antisera. B : immunoblots for HERG and Flag-tagged KvLQT1 and Kir2.1 proteins. CHO cells stably expressing HA-HERG were transiently transfected with the following expression plasmids: pcDNA3 ( lane 1 ), pcDNA3-Flag-KvLQT1 ( lane 2 ), pcDNA3-KvLQT1-Y315S ( lane 3 ), or pcDNA3-Flag-Kir2.1 ( lane 4 ). Left , cell lysates were separated by SDS-PAGE, blotted, and probed with anti-HERG antisera. Right , cell lysates were immunoprecipitated with anti-Flag/protein A/G PLUS-agarose. Immunoprecipitates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-Flag ( bottom ) antisera . All experiments were carried out in triplicate. Shown are representative immunoblots.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: HERG and KvLQT1 coimmunoprecipitations. A : immunoblots for HERG and KvLQT1 proteins. CHO cells were transiently transfected with expression vectors encoding wild-type, pore mutant, and respective Flag-tagged forms of HERG and KvLQT1, as shown. Left , cell lysates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-KvLQT1 ( bottom ) antisera. Right , cell lysates were immunoprecipitated with anti-Flag/protein A/G PLUS-agarose (*) or IgG/protein A/G PLUS-agarose (o). Immunoprecipitates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-KvLQT1 ( bottom ) antisera. B : immunoblots for HERG and Flag-tagged KvLQT1 and Kir2.1 proteins. CHO cells stably expressing HA-HERG were transiently transfected with the following expression plasmids: pcDNA3 ( lane 1 ), pcDNA3-Flag-KvLQT1 ( lane 2 ), pcDNA3-KvLQT1-Y315S ( lane 3 ), or pcDNA3-Flag-Kir2.1 ( lane 4 ). Left , cell lysates were separated by SDS-PAGE, blotted, and probed with anti-HERG antisera. Right , cell lysates were immunoprecipitated with anti-Flag/protein A/G PLUS-agarose. Immunoprecipitates were separated by SDS-PAGE, blotted, and probed with anti-HERG ( top ) or anti-Flag ( bottom ) antisera . All experiments were carried out in triplicate. Shown are representative immunoblots.

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: Western Blot, Transfection, Expressing, Mutagenesis, SDS Page, Immunoprecipitation, Stable Transfection

    Cell surface expression of HERG. A : immunostaining analysis of transfected CHO cells. A CHO cell line stably expressing hemagluttinin (HA)-tagged HERG was transiently transfected with an expression vector for Flag-KvLQT1 ( left ) or Flag-Kir2.1 ( right ). Two days after transfection, cells were fixed with paraformaldehyde and probed with anti-HA monoclonal antibody for surface HERG channel staining. After unbound antibodies were washed out, cells were permeabilized and incubated with polyclonal antibody against the Flag epitope. CHO cells were immunolabeled with anti-HA ( a and d ) or anti-Flag ( b and e ) using Alexa fluor 488-conjugated goat anti-mouse and Alexa fluor 594-conjugated goat anti-rabbit secondary antibodies, respectively. Merged patterns of a and b are shown in c ; merged patterns of d and e are shown in f . B : fluorescence intensity measurements. Elements software was used to semiquantitate green and red fluorescence signals of Flag-KvLQT1- and Flag-Kir2.1-positive cells. Fluorescence intensity signals (means ± SE) for KvLQT1-transfected ( n = 12) and Kir2.1-transfected ( n = 8) cells are shown.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: Cell surface expression of HERG. A : immunostaining analysis of transfected CHO cells. A CHO cell line stably expressing hemagluttinin (HA)-tagged HERG was transiently transfected with an expression vector for Flag-KvLQT1 ( left ) or Flag-Kir2.1 ( right ). Two days after transfection, cells were fixed with paraformaldehyde and probed with anti-HA monoclonal antibody for surface HERG channel staining. After unbound antibodies were washed out, cells were permeabilized and incubated with polyclonal antibody against the Flag epitope. CHO cells were immunolabeled with anti-HA ( a and d ) or anti-Flag ( b and e ) using Alexa fluor 488-conjugated goat anti-mouse and Alexa fluor 594-conjugated goat anti-rabbit secondary antibodies, respectively. Merged patterns of a and b are shown in c ; merged patterns of d and e are shown in f . B : fluorescence intensity measurements. Elements software was used to semiquantitate green and red fluorescence signals of Flag-KvLQT1- and Flag-Kir2.1-positive cells. Fluorescence intensity signals (means ± SE) for KvLQT1-transfected ( n = 12) and Kir2.1-transfected ( n = 8) cells are shown.

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: Expressing, Immunostaining, Transfection, Stable Transfection, Plasmid Preparation, Staining, Incubation, FLAG-tag, Immunolabeling, Fluorescence, Software

    Expression of HERG- and KvLQT1-minK-encoded currents. A : original recordings of stable HERG CHO cells transfected with expression vectors for green fluorescent protein (GFP; left ), KvLQT1-Y315S ( middle ), and KvLQT1 ( right ). No KvLQT1 inhibitor was added in this experiment. The holding potential was at −70 mV, and test potentials ranged from −60 to +50 mV. Tail currents were recorded when the test potential had returned to −50 mV. B : current-voltage ( I - V ) relationships at the end of the test pulse. CHO cells expressing HERG and GFP ( n = 17), HERG and KvLQT1-Y315S ( n = 10), and HERG and KvLQT1 ( n = 20) were tested. All currents were normalized to cell capacitance. C : normalized peak tail current analysis of the aforementioned three groups. D : original recordings of stable KvLQT1-minK CHO cells transfected with expression vectors for GFP ( left ), HERG-G628S ( middle ), and HERG ( right ). No HERG inhibitor was added in this experiment. E : I - V relationships at the end of the test pulse. CHO cells expressing KvLQT1-minK and GFP ( n = 14), KvLQT1-minK and HERG-G628S ( n = 10), and KvLQT1-minK and HERG ( n = 10) were tested. F : normalized peak tail current analysis of the aforementioned three groups. Data are expressed as means ± SE. ANOVA was applied to analyze the data. P values of

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: Expression of HERG- and KvLQT1-minK-encoded currents. A : original recordings of stable HERG CHO cells transfected with expression vectors for green fluorescent protein (GFP; left ), KvLQT1-Y315S ( middle ), and KvLQT1 ( right ). No KvLQT1 inhibitor was added in this experiment. The holding potential was at −70 mV, and test potentials ranged from −60 to +50 mV. Tail currents were recorded when the test potential had returned to −50 mV. B : current-voltage ( I - V ) relationships at the end of the test pulse. CHO cells expressing HERG and GFP ( n = 17), HERG and KvLQT1-Y315S ( n = 10), and HERG and KvLQT1 ( n = 20) were tested. All currents were normalized to cell capacitance. C : normalized peak tail current analysis of the aforementioned three groups. D : original recordings of stable KvLQT1-minK CHO cells transfected with expression vectors for GFP ( left ), HERG-G628S ( middle ), and HERG ( right ). No HERG inhibitor was added in this experiment. E : I - V relationships at the end of the test pulse. CHO cells expressing KvLQT1-minK and GFP ( n = 14), KvLQT1-minK and HERG-G628S ( n = 10), and KvLQT1-minK and HERG ( n = 10) were tested. F : normalized peak tail current analysis of the aforementioned three groups. Data are expressed as means ± SE. ANOVA was applied to analyze the data. P values of

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: Expressing, Transfection

    Creation of Chinese hamster ovary (CHO) cell lines stably expressing HERG and KvLQT1-minK. Immunoblots of stable CHO cell lines expressing HERG or KvLQT1-minK1 are shown. Left : 25 μg of membrane proteins from nontransfected CHO cells and a CHO clone stably expressing Flag-HERG were subjected to Western blot analysis using anti-HERG antiserum. The core-glycosylated immature band of 135 kDa and the fully mature channel protein at 155 kDa are indicated by arrows. Right : 50 μg of membrane proteins from nontransfected CHO cells and a CHO clone stably expressing KvLQT1-minK were analyzed using an immunoblot based on polyclonal anti-KvLQT1 antiserum.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: Creation of Chinese hamster ovary (CHO) cell lines stably expressing HERG and KvLQT1-minK. Immunoblots of stable CHO cell lines expressing HERG or KvLQT1-minK1 are shown. Left : 25 μg of membrane proteins from nontransfected CHO cells and a CHO clone stably expressing Flag-HERG were subjected to Western blot analysis using anti-HERG antiserum. The core-glycosylated immature band of 135 kDa and the fully mature channel protein at 155 kDa are indicated by arrows. Right : 50 μg of membrane proteins from nontransfected CHO cells and a CHO clone stably expressing KvLQT1-minK were analyzed using an immunoblot based on polyclonal anti-KvLQT1 antiserum.

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: Stable Transfection, Expressing, Western Blot

    Expression of HERG- and KvLQT1-minK-encoded currents in stable cell lines transiently expressing Kir2.1. A : original recording of stable HERG CHO cells transfected with expression vectors for Kir2.1. The holding potential was at −70, and test potentials ranged from −100 to +50 mV. Tail currents were recorded when the test potential had returned to −50 mV. B : I - V relationships at the end of the test pulse. CHO cells expressing HERG and GFP ( n = 7) or HERG and Kir2.1 ( n = 7) were tested. Inward rectifier K + current was noticeable only at potentials below −40 mV and was not evaluated. C : normalized peak tail current analysis of the aforementioned two groups. D : original recording of stable KvLQT1-minK CHO cells transfected with expression vectors for Kir2.1. E : I - V relationships at the end of the test pulse. CHO cells expressing KvLQT1-minK and GFP ( n = 7) or KvLQT1-minK and Kir2.1 ( n = 7) were tested. F : normalized peak tail current analysis of the aforementioned two groups.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: Expression of HERG- and KvLQT1-minK-encoded currents in stable cell lines transiently expressing Kir2.1. A : original recording of stable HERG CHO cells transfected with expression vectors for Kir2.1. The holding potential was at −70, and test potentials ranged from −100 to +50 mV. Tail currents were recorded when the test potential had returned to −50 mV. B : I - V relationships at the end of the test pulse. CHO cells expressing HERG and GFP ( n = 7) or HERG and Kir2.1 ( n = 7) were tested. Inward rectifier K + current was noticeable only at potentials below −40 mV and was not evaluated. C : normalized peak tail current analysis of the aforementioned two groups. D : original recording of stable KvLQT1-minK CHO cells transfected with expression vectors for Kir2.1. E : I - V relationships at the end of the test pulse. CHO cells expressing KvLQT1-minK and GFP ( n = 7) or KvLQT1-minK and Kir2.1 ( n = 7) were tested. F : normalized peak tail current analysis of the aforementioned two groups.

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: Expressing, Stable Transfection, Transfection

    Expression of HERG-encoded currents in human embryonic kidney (HEK)-293 cells. A : original recordings of stable HERG cells transfected with expression vectors for GFP ( left ) and KvLQT1-Y315S ( right ). The holding potential was at −80 mV, and test potentials ranged from −70 to +40 mV. Tail currents were recorded when the test potential had returned to −60 mV. B : I - V relationships at the end of the test pulse. HERG cells expressing HERG and GFP ( n = 12), HERG and KvLQT1-Y315S ( n = 9), HERG and KvLQT1 ( n = 12), and HERG and tKvLQT1 ( n = 9) were tested. All currents were normalized to cell capacitance. C : normalized peak tail current analysis of the aforementioned three groups. 293B (50 μM ) was added when HERG currents were measured in stable HERG cells transiently expressing KvLQT1.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: Expression of HERG-encoded currents in human embryonic kidney (HEK)-293 cells. A : original recordings of stable HERG cells transfected with expression vectors for GFP ( left ) and KvLQT1-Y315S ( right ). The holding potential was at −80 mV, and test potentials ranged from −70 to +40 mV. Tail currents were recorded when the test potential had returned to −60 mV. B : I - V relationships at the end of the test pulse. HERG cells expressing HERG and GFP ( n = 12), HERG and KvLQT1-Y315S ( n = 9), HERG and KvLQT1 ( n = 12), and HERG and tKvLQT1 ( n = 9) were tested. All currents were normalized to cell capacitance. C : normalized peak tail current analysis of the aforementioned three groups. 293B (50 μM ) was added when HERG currents were measured in stable HERG cells transiently expressing KvLQT1.

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: Expressing, Transfection

    Surface plasmon resonance (SPR) analysis of KvLQT1-HERG associations. A : Commassie blue-stained gel showing the results of purification of maltose-binding protein (MBP)-KCNQ1-CT and MBP-HERG-14 cytoplasmic domains. B : representative SPR tracing of KCNQ1-CT interacting with immobilized HERG-14. Each trace represents the SPR response to a different concentration (between 0.31 and 20 μM) of soluble KCNQ1-CT flowing across immobilized HERG-14-MBP. C : representative SPR tracing of MBP applied to immobilized HERG-14. The same concentration range of soluble MBP as the analyte was used as in B . No resonance changes were observed for MBP and HERG-14. R max , binding capacity.

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    Article Title: Pore mutants of HERG and KvLQT1 downregulate the reciprocal currents in stable cell lines

    doi: 10.1152/ajpheart.00479.2009

    Figure Lengend Snippet: Surface plasmon resonance (SPR) analysis of KvLQT1-HERG associations. A : Commassie blue-stained gel showing the results of purification of maltose-binding protein (MBP)-KCNQ1-CT and MBP-HERG-14 cytoplasmic domains. B : representative SPR tracing of KCNQ1-CT interacting with immobilized HERG-14. Each trace represents the SPR response to a different concentration (between 0.31 and 20 μM) of soluble KCNQ1-CT flowing across immobilized HERG-14-MBP. C : representative SPR tracing of MBP applied to immobilized HERG-14. The same concentration range of soluble MBP as the analyte was used as in B . No resonance changes were observed for MBP and HERG-14. R max , binding capacity.

    Article Snippet: In addition, we noted differences in the voltage dependence of activation of cells expressing HERG or HERG and KvLQT1 ( V 1/2 of −4.75 ± 0.54 and −12.45 ± 0.28 mV, P < 0.05) as well as cells expressing KvLQT1-minK or KvLQT1-minK and HERG ( V 1/2 of 8.16 ± 0.27 and 10.72 ± 0.39 mV).

    Techniques: SPR Assay, Staining, Purification, Binding Assay, Concentration Assay