bkα  (Alomone Labs)


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    Structured Review

    Alomone Labs bkα
    BK channels are detected in mitochondrial fractions from normal rat kidney proximal tubular epithelial (NRK) cells. Western blot shows expression of the pore-forming <t>BKα</t> subunit in mitochondrial fractions ( a ) and cytosolic fractions ( c ) from control NRK cells and after exposure to cold storage and rewarming (CS + RW). Manganese superoxide dismutase (MnSOD) served as a mitochondrial marker and loading control for mitochondrial fractions. Proteasome subunit beta type-5 (PSMB5) was used as a cytosolic marker and β-actin was used as a standard loading control. Representative blots are shown using n = 3, where each lane is loaded with 25 μg protein corresponding to a separate experiment. Densitometry analyses for the mitochondrial ( b ) and cytosolic ( d ) fractions are next to corresponding blots; densitometry calculated from two separate blots with a total n = 6; no significant differences detected using p
    Bkα, 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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    bkα - by Bioz Stars, 2022-08
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    1) Product Images from "Specific BK Channel Activator NS11021 Protects Rat Renal Proximal Tubular Cells from Cold Storage—Induced Mitochondrial Injury In Vitro"

    Article Title: Specific BK Channel Activator NS11021 Protects Rat Renal Proximal Tubular Cells from Cold Storage—Induced Mitochondrial Injury In Vitro

    Journal: Biomolecules

    doi: 10.3390/biom9120825

    BK channels are detected in mitochondrial fractions from normal rat kidney proximal tubular epithelial (NRK) cells. Western blot shows expression of the pore-forming BKα subunit in mitochondrial fractions ( a ) and cytosolic fractions ( c ) from control NRK cells and after exposure to cold storage and rewarming (CS + RW). Manganese superoxide dismutase (MnSOD) served as a mitochondrial marker and loading control for mitochondrial fractions. Proteasome subunit beta type-5 (PSMB5) was used as a cytosolic marker and β-actin was used as a standard loading control. Representative blots are shown using n = 3, where each lane is loaded with 25 μg protein corresponding to a separate experiment. Densitometry analyses for the mitochondrial ( b ) and cytosolic ( d ) fractions are next to corresponding blots; densitometry calculated from two separate blots with a total n = 6; no significant differences detected using p
    Figure Legend Snippet: BK channels are detected in mitochondrial fractions from normal rat kidney proximal tubular epithelial (NRK) cells. Western blot shows expression of the pore-forming BKα subunit in mitochondrial fractions ( a ) and cytosolic fractions ( c ) from control NRK cells and after exposure to cold storage and rewarming (CS + RW). Manganese superoxide dismutase (MnSOD) served as a mitochondrial marker and loading control for mitochondrial fractions. Proteasome subunit beta type-5 (PSMB5) was used as a cytosolic marker and β-actin was used as a standard loading control. Representative blots are shown using n = 3, where each lane is loaded with 25 μg protein corresponding to a separate experiment. Densitometry analyses for the mitochondrial ( b ) and cytosolic ( d ) fractions are next to corresponding blots; densitometry calculated from two separate blots with a total n = 6; no significant differences detected using p

    Techniques Used: Western Blot, Expressing, Marker

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    Alomone Labs anti bkα
    BK channels and NMDARs interact via <t>BKα</t> and GluN1 in HEK-293 cells. ( A ) Reciprocal pull-down of GluN1 and BKα by anti-BKα and -GluN1 antibodies in the absence of expression of any other NMDAR subunit. IB, immunoblot; IP, immunopurification. ( B ) Pull-down of GluN2A and GluN2B by an anti-BKα antibody only in the presence of GluN1 expression. ( C ) Pull-down of BKα by an anti-GluN2A or -GluN2B antibody only in the presence of GluN1 expression. ( D ) Reciprocal pull-down assay showed that the BKα was largely defective in its association with GluN1 upon deletion of its S0–S1 loop region (residues 46–93). ( E ) Pull-down of BKα by an anti-GluN1 was interfered by a synthesized peptide of the BKα’s S0–S1 loop region (residues 46–93), but not by a scrambled peptide. The peptides were added at a concentration of 1 mg/mL to cell lysates that were equally divided from the same lysate of cells coexpressing BKα and GluN1. ( F ) Pull-down of GluN1 by an anti-BKα antibody showed that the BKα–GluN1 association was markedly decreased with the GluN1 N1/K2 C mutant in which the C-terminal part, including TM domain (residues 527–647 and 781–826) and C-terminal domain (residues 827–920), was replaced by those of GluK2. ( G ) Pull-down of the GluN1’s cytosolic regions by the BKα46–93 peptide, but not by the scrambled peptide. The peptides were biotinylated on their N termini and immobilized on streptavidin agarose. The fusion construct of the GluN1’s cytosolic regions (residues 563–587 and 813–920) was 6× His-tagged in its C terminus, expressed in E. coli , and purified with IMAC chromatography.
    Anti Bkα, 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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    BK channels and NMDARs interact via BKα and GluN1 in HEK-293 cells. ( A ) Reciprocal pull-down of GluN1 and BKα by anti-BKα and -GluN1 antibodies in the absence of expression of any other NMDAR subunit. IB, immunoblot; IP, immunopurification. ( B ) Pull-down of GluN2A and GluN2B by an anti-BKα antibody only in the presence of GluN1 expression. ( C ) Pull-down of BKα by an anti-GluN2A or -GluN2B antibody only in the presence of GluN1 expression. ( D ) Reciprocal pull-down assay showed that the BKα was largely defective in its association with GluN1 upon deletion of its S0–S1 loop region (residues 46–93). ( E ) Pull-down of BKα by an anti-GluN1 was interfered by a synthesized peptide of the BKα’s S0–S1 loop region (residues 46–93), but not by a scrambled peptide. The peptides were added at a concentration of 1 mg/mL to cell lysates that were equally divided from the same lysate of cells coexpressing BKα and GluN1. ( F ) Pull-down of GluN1 by an anti-BKα antibody showed that the BKα–GluN1 association was markedly decreased with the GluN1 N1/K2 C mutant in which the C-terminal part, including TM domain (residues 527–647 and 781–826) and C-terminal domain (residues 827–920), was replaced by those of GluK2. ( G ) Pull-down of the GluN1’s cytosolic regions by the BKα46–93 peptide, but not by the scrambled peptide. The peptides were biotinylated on their N termini and immobilized on streptavidin agarose. The fusion construct of the GluN1’s cytosolic regions (residues 563–587 and 813–920) was 6× His-tagged in its C terminus, expressed in E. coli , and purified with IMAC chromatography.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Glutamate-activated BK channel complexes formed with NMDA receptors

    doi: 10.1073/pnas.1802567115

    Figure Lengend Snippet: BK channels and NMDARs interact via BKα and GluN1 in HEK-293 cells. ( A ) Reciprocal pull-down of GluN1 and BKα by anti-BKα and -GluN1 antibodies in the absence of expression of any other NMDAR subunit. IB, immunoblot; IP, immunopurification. ( B ) Pull-down of GluN2A and GluN2B by an anti-BKα antibody only in the presence of GluN1 expression. ( C ) Pull-down of BKα by an anti-GluN2A or -GluN2B antibody only in the presence of GluN1 expression. ( D ) Reciprocal pull-down assay showed that the BKα was largely defective in its association with GluN1 upon deletion of its S0–S1 loop region (residues 46–93). ( E ) Pull-down of BKα by an anti-GluN1 was interfered by a synthesized peptide of the BKα’s S0–S1 loop region (residues 46–93), but not by a scrambled peptide. The peptides were added at a concentration of 1 mg/mL to cell lysates that were equally divided from the same lysate of cells coexpressing BKα and GluN1. ( F ) Pull-down of GluN1 by an anti-BKα antibody showed that the BKα–GluN1 association was markedly decreased with the GluN1 N1/K2 C mutant in which the C-terminal part, including TM domain (residues 527–647 and 781–826) and C-terminal domain (residues 827–920), was replaced by those of GluK2. ( G ) Pull-down of the GluN1’s cytosolic regions by the BKα46–93 peptide, but not by the scrambled peptide. The peptides were biotinylated on their N termini and immobilized on streptavidin agarose. The fusion construct of the GluN1’s cytosolic regions (residues 563–587 and 813–920) was 6× His-tagged in its C terminus, expressed in E. coli , and purified with IMAC chromatography.

    Article Snippet: Rabbit polyclonal anti-GluN1 (catalog no. G8913; Sigma-Aldrich), anti-BKα (catalog no. APC-107; Alomone Labs), anti-GluN2A (catalog no. AB1555; EMD Millipore), anti-GluN2B (catalog no. SAB2104208; Sigma-Aldrich), and anti-FLAG (catalog no. F7425; Sigma-Aldrich) and mouse monoclonal anti-BKα (catalog no. L6/60; NeuroMabs) antibodies were used for immunopurification.

    Techniques: Expressing, Immu-Puri, Pull Down Assay, Synthesized, Concentration Assay, Mutagenesis, Construct, Purification, Chromatography

    BK channels and NMDARs form complexes in rat brains. ( A ) Schematic of the sample-preparation protocols for the immunopurified NMDAR (IP-NMDAR) and BK channel (IP-BK), tandem immunopurified BK–NMDAR complex (TIP-BK/NMDAR), and negative control samples. ( B ) SDS/PAGE and silver stain analysis of the IP-NMDAR and control samples. ( C ) Tandem mass spectrometric spectra of a unique peptide of BKα identified in the IP-NMDAR sample. ( D ) Immunoblot (IB) analysis of BKα and GluN1 in the IP-NMDAR sample. ( E ) Tandem mass spectrometric spectra for a unique peptide of GluN1 identified in the IP-BK sample. ( F ) Immunoblot analysis of GluN1 and BKα in the IP-BK sample. ( G ) Immunoblot analysis of GluN2A and GluN2B in the TIP-BK/NMDAR sample. ( H ) Immunoblot analysis of BKα and GluN1 in IP-NMDAR ( Left ) and IP-BK ( Right ) samples prepared from different brain regions.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Glutamate-activated BK channel complexes formed with NMDA receptors

    doi: 10.1073/pnas.1802567115

    Figure Lengend Snippet: BK channels and NMDARs form complexes in rat brains. ( A ) Schematic of the sample-preparation protocols for the immunopurified NMDAR (IP-NMDAR) and BK channel (IP-BK), tandem immunopurified BK–NMDAR complex (TIP-BK/NMDAR), and negative control samples. ( B ) SDS/PAGE and silver stain analysis of the IP-NMDAR and control samples. ( C ) Tandem mass spectrometric spectra of a unique peptide of BKα identified in the IP-NMDAR sample. ( D ) Immunoblot (IB) analysis of BKα and GluN1 in the IP-NMDAR sample. ( E ) Tandem mass spectrometric spectra for a unique peptide of GluN1 identified in the IP-BK sample. ( F ) Immunoblot analysis of GluN1 and BKα in the IP-BK sample. ( G ) Immunoblot analysis of GluN2A and GluN2B in the TIP-BK/NMDAR sample. ( H ) Immunoblot analysis of BKα and GluN1 in IP-NMDAR ( Left ) and IP-BK ( Right ) samples prepared from different brain regions.

    Article Snippet: Rabbit polyclonal anti-GluN1 (catalog no. G8913; Sigma-Aldrich), anti-BKα (catalog no. APC-107; Alomone Labs), anti-GluN2A (catalog no. AB1555; EMD Millipore), anti-GluN2B (catalog no. SAB2104208; Sigma-Aldrich), and anti-FLAG (catalog no. F7425; Sigma-Aldrich) and mouse monoclonal anti-BKα (catalog no. L6/60; NeuroMabs) antibodies were used for immunopurification.

    Techniques: Sample Prep, Negative Control, SDS Page, Silver Staining

    In situ PLA of BKα and GluN1 colocalization in HEK-293 cells and mouse brains. ( A ) PLA signals (red dots) probed with anti-V5 and -FLAG antibodies under a nonpermeabilized condition were detected in HEK-293 cells coexpressing V5-BKα and FLAG-GluN1. ( B and C ) In situ PLA of BKα–GluN1 complexes in the hippocampal dentate gyrus of control (Nestin-Cre − /KCNMA1 fl/fl ) mice ( B ) and neuron-specific BKα KO (Nestin-Cre + /KCNMA1 fl/fl ) mice ( C ). Nuclei are shown in blue (DAPI). (Scale bars: 40 or 10 μm.)

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Glutamate-activated BK channel complexes formed with NMDA receptors

    doi: 10.1073/pnas.1802567115

    Figure Lengend Snippet: In situ PLA of BKα and GluN1 colocalization in HEK-293 cells and mouse brains. ( A ) PLA signals (red dots) probed with anti-V5 and -FLAG antibodies under a nonpermeabilized condition were detected in HEK-293 cells coexpressing V5-BKα and FLAG-GluN1. ( B and C ) In situ PLA of BKα–GluN1 complexes in the hippocampal dentate gyrus of control (Nestin-Cre − /KCNMA1 fl/fl ) mice ( B ) and neuron-specific BKα KO (Nestin-Cre + /KCNMA1 fl/fl ) mice ( C ). Nuclei are shown in blue (DAPI). (Scale bars: 40 or 10 μm.)

    Article Snippet: Rabbit polyclonal anti-GluN1 (catalog no. G8913; Sigma-Aldrich), anti-BKα (catalog no. APC-107; Alomone Labs), anti-GluN2A (catalog no. AB1555; EMD Millipore), anti-GluN2B (catalog no. SAB2104208; Sigma-Aldrich), and anti-FLAG (catalog no. F7425; Sigma-Aldrich) and mouse monoclonal anti-BKα (catalog no. L6/60; NeuroMabs) antibodies were used for immunopurification.

    Techniques: In Situ, Proximity Ligation Assay, Mouse Assay

    Postsynaptic BK channels regulate synaptic transmission in mature dentate granule cells via NMDAR-mediated channel activation. ( A ) Effects of paxilline (Pax) alone and combined with AP5 on the amplitudes of evoked EPSPs ( n = 13). ( B ) Effects of AP5 alone and combined with paxilline on the amplitudes of evoked EPSPs ( n = 13). For comparison, the effects of AP5 alone on evoked EPSPs over a similar extended time course ( n = 6) were included in the averaged plot. ( C ) Effects of paxilline alone and combined with AP5 on the amplitudes of evoked EPSPs in mature granule cells in BKα-KO (Nestin-Cre + /KCNMA1 fl/fl ) mice ( n = 9). ( D ) The effect of paxilline alone (bath) and combined with AP5 (bath) on evoked EPSPs in the presence of intracellularly applied MK-801 ( n = 9). ( E ) Effects of paxilline on evoked EPSPs in the presence of intracellularly applied paxilline ( n = 8). ( F ) Effects of paxilline on evoked EPSPs in the presence of intracellularly applied 0.5 mg/mL BKα46–93 ( n = 8) or scrambled ( n = 7) peptide. Pep., peptide. ( G ) Effects of extracellularly and intracellularly applied paxilline ( n = 9 and 7, respectively) and KO of BK channels (Nestin-Cre + /KCNMA1 fl/fl ) ( n = 5) on paired-pulse ratios. All experiments were done with regular C57BL/C6 mice except as specified. Control, data obtained without or before drug application. Paxilline and AP5 were perfused in the bath solution at a concentration of 10 and 200 µM, respectively, and they were applied either individually or combined together at a later stage of the experiment. Statistical differences were evaluated by using a t test. N.S., not significant. * P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Glutamate-activated BK channel complexes formed with NMDA receptors

    doi: 10.1073/pnas.1802567115

    Figure Lengend Snippet: Postsynaptic BK channels regulate synaptic transmission in mature dentate granule cells via NMDAR-mediated channel activation. ( A ) Effects of paxilline (Pax) alone and combined with AP5 on the amplitudes of evoked EPSPs ( n = 13). ( B ) Effects of AP5 alone and combined with paxilline on the amplitudes of evoked EPSPs ( n = 13). For comparison, the effects of AP5 alone on evoked EPSPs over a similar extended time course ( n = 6) were included in the averaged plot. ( C ) Effects of paxilline alone and combined with AP5 on the amplitudes of evoked EPSPs in mature granule cells in BKα-KO (Nestin-Cre + /KCNMA1 fl/fl ) mice ( n = 9). ( D ) The effect of paxilline alone (bath) and combined with AP5 (bath) on evoked EPSPs in the presence of intracellularly applied MK-801 ( n = 9). ( E ) Effects of paxilline on evoked EPSPs in the presence of intracellularly applied paxilline ( n = 8). ( F ) Effects of paxilline on evoked EPSPs in the presence of intracellularly applied 0.5 mg/mL BKα46–93 ( n = 8) or scrambled ( n = 7) peptide. Pep., peptide. ( G ) Effects of extracellularly and intracellularly applied paxilline ( n = 9 and 7, respectively) and KO of BK channels (Nestin-Cre + /KCNMA1 fl/fl ) ( n = 5) on paired-pulse ratios. All experiments were done with regular C57BL/C6 mice except as specified. Control, data obtained without or before drug application. Paxilline and AP5 were perfused in the bath solution at a concentration of 10 and 200 µM, respectively, and they were applied either individually or combined together at a later stage of the experiment. Statistical differences were evaluated by using a t test. N.S., not significant. * P

    Article Snippet: Rabbit polyclonal anti-GluN1 (catalog no. G8913; Sigma-Aldrich), anti-BKα (catalog no. APC-107; Alomone Labs), anti-GluN2A (catalog no. AB1555; EMD Millipore), anti-GluN2B (catalog no. SAB2104208; Sigma-Aldrich), and anti-FLAG (catalog no. F7425; Sigma-Aldrich) and mouse monoclonal anti-BKα (catalog no. L6/60; NeuroMabs) antibodies were used for immunopurification.

    Techniques: Transmission Assay, Activation Assay, Mouse Assay, Concentration Assay

    Functional expression of BK channels in rat MV. A, co-expression of BK channel α- and β1-subunits in rat MV. Myocytes labeled with an anti-BK channel α-subunits (anti- slo ) antibody (green) and anti-BKCa 2+ β1 (red). B , Western

    Journal: Journal of cardiovascular pharmacology

    Article Title: Requirement for functional BK channels in maintaining oscillation in venomotor tone revealed by species differences in expression of the ?1 accessory subunits

    doi: 10.1097/FJC.0b013e318233614c

    Figure Lengend Snippet: Functional expression of BK channels in rat MV. A, co-expression of BK channel α- and β1-subunits in rat MV. Myocytes labeled with an anti-BK channel α-subunits (anti- slo ) antibody (green) and anti-BKCa 2+ β1 (red). B , Western

    Article Snippet: For Western blot analysis, we used a primary antibody targeted to BK channel α-subunits (anti-BKca2+ 1.1, 1:500; Alomone Labs.

    Techniques: Functional Assay, Expressing, Labeling, Western Blot

    (A) Representative amplification plots and agarose gel separation of real‐time RT‐PCR analysis of BK β 1‐subunit and GAPDH in MA, colons, and kidneys from WT and BK β 1‐KO mice. The expression threshold was set at 0.22, a level above background fluorescence but within the linear phase of the amplification plot. The intersection between the threshold level and the amplification plot is the Ct value, which correlates with the amount of template in the sample. Ct values over 35 are excluded, as these values approach the sensitivity limits of the Taqman assay. Amplification of real‐time RT‐PCR products was seen at 75 bp in tissues from WT animals only. Con, nontemplate control. (B) Representative western blot obtained using anti‐BK α ‐subunit antibody in colonic and kidney tissues from WT and BK β 1‐KO mice. Antibody detected a protein band at ~100 kDa in all tissues from WT and BK β 1‐KO mice. The signals are blocked by preincubation with the antibody competing peptide (CP). Arrows indicate the manufacturer's recommended molecular weight of BK α ‐subunit protein.

    Journal: Physiological Reports

    Article Title: Western blot analysis of BK channel β1‐subunit expression should be interpreted cautiously when using commercially available antibodies

    doi: 10.14814/phy2.12189

    Figure Lengend Snippet: (A) Representative amplification plots and agarose gel separation of real‐time RT‐PCR analysis of BK β 1‐subunit and GAPDH in MA, colons, and kidneys from WT and BK β 1‐KO mice. The expression threshold was set at 0.22, a level above background fluorescence but within the linear phase of the amplification plot. The intersection between the threshold level and the amplification plot is the Ct value, which correlates with the amount of template in the sample. Ct values over 35 are excluded, as these values approach the sensitivity limits of the Taqman assay. Amplification of real‐time RT‐PCR products was seen at 75 bp in tissues from WT animals only. Con, nontemplate control. (B) Representative western blot obtained using anti‐BK α ‐subunit antibody in colonic and kidney tissues from WT and BK β 1‐KO mice. Antibody detected a protein band at ~100 kDa in all tissues from WT and BK β 1‐KO mice. The signals are blocked by preincubation with the antibody competing peptide (CP). Arrows indicate the manufacturer's recommended molecular weight of BK α ‐subunit protein.

    Article Snippet: We also tested an anti‐BK α ‐subunit antibody (APC‐107, anti‐KCa1.1 , 1:500; Alomone Labs, Jerusalem, Israel) in protein extracts from colons and kidneys, to confirm BK channel expression in these tissues.

    Techniques: Amplification, Agarose Gel Electrophoresis, Quantitative RT-PCR, Mouse Assay, Expressing, Fluorescence, TaqMan Assay, Western Blot, Molecular Weight

    NKβ1 down-regulation reduces the cell surface expression of Slo1 channels in HEK293T cells. A, Cell-surface biotinylation assay showing cell surface and total expression of Myc-Slo1 in HEK293T cell transiently cotransfected with si-NKβ1

    Journal: FEBS letters

    Article Title: The ?1-subunit of Na+/K+-ATPase interacts with BKCa channels and affects their steady-state expression on the cell surface

    doi: 10.1016/j.febslet.2009.08.039

    Figure Lengend Snippet: NKβ1 down-regulation reduces the cell surface expression of Slo1 channels in HEK293T cells. A, Cell-surface biotinylation assay showing cell surface and total expression of Myc-Slo1 in HEK293T cell transiently cotransfected with si-NKβ1

    Article Snippet: Signals from anti-Slo1 and anti-NKβ1 show extensive overlap, especially in intracellular compartments of somatic areas.

    Techniques: Expressing, Cell Surface Biotinylation Assay

    NKβ1 interacts with neuronal Slo1 channels. A, B Schematic representations of Slo1 and NKβ1 respectively. The bait fragment used in the yeast two-hybrid screen is highlighted in blue. C, Co-immunoprecipitation of NKβ1 and Slo1

    Journal: FEBS letters

    Article Title: The ?1-subunit of Na+/K+-ATPase interacts with BKCa channels and affects their steady-state expression on the cell surface

    doi: 10.1016/j.febslet.2009.08.039

    Figure Lengend Snippet: NKβ1 interacts with neuronal Slo1 channels. A, B Schematic representations of Slo1 and NKβ1 respectively. The bait fragment used in the yeast two-hybrid screen is highlighted in blue. C, Co-immunoprecipitation of NKβ1 and Slo1

    Article Snippet: Signals from anti-Slo1 and anti-NKβ1 show extensive overlap, especially in intracellular compartments of somatic areas.

    Techniques: Two Hybrid Screening, Immunoprecipitation

    Interaction between NKβ1 and Slo1 occurs at multiple regions. A, GST pull-down assay carried out on chick CG lysates showing that a fusion protein containing the bait, GST-Slo1(G785-A985) binds to NKβ1. Additional fusion proteins from

    Journal: FEBS letters

    Article Title: The ?1-subunit of Na+/K+-ATPase interacts with BKCa channels and affects their steady-state expression on the cell surface

    doi: 10.1016/j.febslet.2009.08.039

    Figure Lengend Snippet: Interaction between NKβ1 and Slo1 occurs at multiple regions. A, GST pull-down assay carried out on chick CG lysates showing that a fusion protein containing the bait, GST-Slo1(G785-A985) binds to NKβ1. Additional fusion proteins from

    Article Snippet: Signals from anti-Slo1 and anti-NKβ1 show extensive overlap, especially in intracellular compartments of somatic areas.

    Techniques: Pull Down Assay

    Co-localization pattern of NKβ1 and Slo1. Top panel shows co-localization of NKβ1 (red) and Slo1 (green) in E9 chick CG neurons. The regions enclosed by white squares are magnified in the bottom panels to show neurites and cell bodies.

    Journal: FEBS letters

    Article Title: The ?1-subunit of Na+/K+-ATPase interacts with BKCa channels and affects their steady-state expression on the cell surface

    doi: 10.1016/j.febslet.2009.08.039

    Figure Lengend Snippet: Co-localization pattern of NKβ1 and Slo1. Top panel shows co-localization of NKβ1 (red) and Slo1 (green) in E9 chick CG neurons. The regions enclosed by white squares are magnified in the bottom panels to show neurites and cell bodies.

    Article Snippet: Signals from anti-Slo1 and anti-NKβ1 show extensive overlap, especially in intracellular compartments of somatic areas.

    Techniques:

    Inside-out patch recordings made from HEK293T cells expressing Slo1. A, Typical families of currents evoked by voltage steps (-80 mV to +80 mV) in inside-out patches from transfected HEK293T cells. The bath solution contained 20 μM Ca 2+ . No currents

    Journal: FEBS letters

    Article Title: The ?1-subunit of Na+/K+-ATPase interacts with BKCa channels and affects their steady-state expression on the cell surface

    doi: 10.1016/j.febslet.2009.08.039

    Figure Lengend Snippet: Inside-out patch recordings made from HEK293T cells expressing Slo1. A, Typical families of currents evoked by voltage steps (-80 mV to +80 mV) in inside-out patches from transfected HEK293T cells. The bath solution contained 20 μM Ca 2+ . No currents

    Article Snippet: Signals from anti-Slo1 and anti-NKβ1 show extensive overlap, especially in intracellular compartments of somatic areas.

    Techniques: Expressing, Transfection