bk β1 subunit  (Alomone Labs)


Bioz Verified Symbol Alomone Labs is a verified supplier
Bioz Manufacturer Symbol Alomone Labs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Alomone Labs bk β1 subunit
    Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of <t>β1-subunit</t> A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p
    Bk β1 Subunit, 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/bk β1 subunit/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bk β1 subunit - by Bioz Stars, 2022-05
    94/100 stars

    Images

    1) Product Images from "MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria"

    Article Title: MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria

    Journal: The Journal of physiology

    doi: 10.1113/JP277769

    Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p
    Figure Legend Snippet: Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p

    Techniques Used:

    MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.
    Figure Legend Snippet: MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.

    Techniques Used: Immunoprecipitation, Activity Assay

    Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p
    Figure Legend Snippet: Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p

    Techniques Used: Cell Culture, Transfection, Labeling

    2) Product Images from "MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria"

    Article Title: MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria

    Journal: The Journal of physiology

    doi: 10.1113/JP277769

    Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p
    Figure Legend Snippet: Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p

    Techniques Used:

    MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.
    Figure Legend Snippet: MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.

    Techniques Used: Immunoprecipitation, Activity Assay

    Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p
    Figure Legend Snippet: Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p

    Techniques Used: Cell Culture, Transfection, Labeling

    3) Product Images from "Abnormal Ca2+ Spark/STOC Coupling in Cerebral Artery Smooth Muscle Cells of Obese Type 2 Diabetic Mice"

    Article Title: Abnormal Ca2+ Spark/STOC Coupling in Cerebral Artery Smooth Muscle Cells of Obese Type 2 Diabetic Mice

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0053321

    Decreased BK β1/α -subunit ratio in vascular tissues of db/db mice. A . Representative Western Blots of BK α and β1 subunits obtained from control and db/db vascular tissues. Samples containing 30 µg of protein from aorta whole homogenates were run on 15% acrylamide gels and probed with anti-BK α subunit antibody (1∶1000), anti-BK β1 subunit antibody (1∶500) and anti-actin (1∶8000). B . Bar graph represents normalized BKβ1/α densitometric ratios (n = 7 for each group). * P
    Figure Legend Snippet: Decreased BK β1/α -subunit ratio in vascular tissues of db/db mice. A . Representative Western Blots of BK α and β1 subunits obtained from control and db/db vascular tissues. Samples containing 30 µg of protein from aorta whole homogenates were run on 15% acrylamide gels and probed with anti-BK α subunit antibody (1∶1000), anti-BK β1 subunit antibody (1∶500) and anti-actin (1∶8000). B . Bar graph represents normalized BKβ1/α densitometric ratios (n = 7 for each group). * P

    Techniques Used: Mouse Assay, Western Blot

    4) Product Images from "Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase"

    Article Title: Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/jcmm.13103

    Effect of genistein on BK channel current in BK ‐ HEK 293 cells. (A) Voltage‐dependent BK current recorded in a typical BK ‐ HEK 293 cell stably expressing both α‐ and β1‐subunit with the voltage protocol as shown in the inset in the absence and presence of 10 μM genistein, and upon washout. (B) Original BK current traces in a representative BK ‐ HEK 293 cell during control, in the presence of 10 μM genistein, and genistein plus 1 mM orthovanadate ( OV ). (C) Mean percentage values of BK current measured at +70 mV during control, 10 μM genistein, washout, 10 μM genistein and genistein plus 1 mM OV ( n = 6, ** P
    Figure Legend Snippet: Effect of genistein on BK channel current in BK ‐ HEK 293 cells. (A) Voltage‐dependent BK current recorded in a typical BK ‐ HEK 293 cell stably expressing both α‐ and β1‐subunit with the voltage protocol as shown in the inset in the absence and presence of 10 μM genistein, and upon washout. (B) Original BK current traces in a representative BK ‐ HEK 293 cell during control, in the presence of 10 μM genistein, and genistein plus 1 mM orthovanadate ( OV ). (C) Mean percentage values of BK current measured at +70 mV during control, 10 μM genistein, washout, 10 μM genistein and genistein plus 1 mM OV ( n = 6, ** P

    Techniques Used: Stable Transfection, Expressing

    Membrane current in HEK 293 cells stably expressing human BK channel α‐ and β1‐subunits. (A) Voltage‐dependent BK current traces recorded in a representative cell with the voltage protocol as shown in the inset before and after application of 1 μM paxilline (a selective BK channel blocker), and washout of paxilline. (B) I‐V relationships of BK current in the absence and presence of 1 μM paxilline, and upon washout ( n = 5, * P
    Figure Legend Snippet: Membrane current in HEK 293 cells stably expressing human BK channel α‐ and β1‐subunits. (A) Voltage‐dependent BK current traces recorded in a representative cell with the voltage protocol as shown in the inset before and after application of 1 μM paxilline (a selective BK channel blocker), and washout of paxilline. (B) I‐V relationships of BK current in the absence and presence of 1 μM paxilline, and upon washout ( n = 5, * P

    Techniques Used: Stable Transfection, Expressing

    Tyrosine phosphorylation level of β1 subunits in BK ‐ HEK 293 cells. (A) Images of immunoprecipitation and Western blotting in BK ‐ HEK 293 cells treated with vehicle (control), 100 ng/ml EGF , 1 mM orthovanadate ( OV ), 10 μM genistein, genistein plus OV , 10 μM tyrphostin AG 556 ( AG 556), and AG 556 plus OV . (B) Mean percentage values of relative tyrosine‐phosphorylated β1 protein. The amount of protein from the immunoprecipitation (as shown in A) was normalized with those from the Western blotting. Relative phosphorylated protein level is expressed as a percentage of vehicle control ( n = 5, * P
    Figure Legend Snippet: Tyrosine phosphorylation level of β1 subunits in BK ‐ HEK 293 cells. (A) Images of immunoprecipitation and Western blotting in BK ‐ HEK 293 cells treated with vehicle (control), 100 ng/ml EGF , 1 mM orthovanadate ( OV ), 10 μM genistein, genistein plus OV , 10 μM tyrphostin AG 556 ( AG 556), and AG 556 plus OV . (B) Mean percentage values of relative tyrosine‐phosphorylated β1 protein. The amount of protein from the immunoprecipitation (as shown in A) was normalized with those from the Western blotting. Relative phosphorylated protein level is expressed as a percentage of vehicle control ( n = 5, * P

    Techniques Used: Immunoprecipitation, Western Blot

    5) Product Images from "Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase"

    Article Title: Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/jcmm.13103

    Effect of genistein on BK channel current in BK ‐ HEK 293 cells. (A) Voltage‐dependent BK current recorded in a typical BK ‐ HEK 293 cell stably expressing both α‐ and β1‐subunit with the voltage protocol as shown in the inset in the absence and presence of 10 μM genistein, and upon washout. (B) Original BK current traces in a representative BK ‐ HEK 293 cell during control, in the presence of 10 μM genistein, and genistein plus 1 mM orthovanadate ( OV ). (C) Mean percentage values of BK current measured at +70 mV during control, 10 μM genistein, washout, 10 μM genistein and genistein plus 1 mM OV ( n = 6, ** P
    Figure Legend Snippet: Effect of genistein on BK channel current in BK ‐ HEK 293 cells. (A) Voltage‐dependent BK current recorded in a typical BK ‐ HEK 293 cell stably expressing both α‐ and β1‐subunit with the voltage protocol as shown in the inset in the absence and presence of 10 μM genistein, and upon washout. (B) Original BK current traces in a representative BK ‐ HEK 293 cell during control, in the presence of 10 μM genistein, and genistein plus 1 mM orthovanadate ( OV ). (C) Mean percentage values of BK current measured at +70 mV during control, 10 μM genistein, washout, 10 μM genistein and genistein plus 1 mM OV ( n = 6, ** P

    Techniques Used: Stable Transfection, Expressing

    Membrane current in HEK 293 cells stably expressing human BK channel α‐ and β1‐subunits. (A) Voltage‐dependent BK current traces recorded in a representative cell with the voltage protocol as shown in the inset before and after application of 1 μM paxilline (a selective BK channel blocker), and washout of paxilline. (B) I‐V relationships of BK current in the absence and presence of 1 μM paxilline, and upon washout ( n = 5, * P
    Figure Legend Snippet: Membrane current in HEK 293 cells stably expressing human BK channel α‐ and β1‐subunits. (A) Voltage‐dependent BK current traces recorded in a representative cell with the voltage protocol as shown in the inset before and after application of 1 μM paxilline (a selective BK channel blocker), and washout of paxilline. (B) I‐V relationships of BK current in the absence and presence of 1 μM paxilline, and upon washout ( n = 5, * P

    Techniques Used: Stable Transfection, Expressing

    Tyrosine phosphorylation level of β1 subunits in BK ‐ HEK 293 cells. (A) Images of immunoprecipitation and Western blotting in BK ‐ HEK 293 cells treated with vehicle (control), 100 ng/ml EGF , 1 mM orthovanadate ( OV ), 10 μM genistein, genistein plus OV , 10 μM tyrphostin AG 556 ( AG 556), and AG 556 plus OV . (B) Mean percentage values of relative tyrosine‐phosphorylated β1 protein. The amount of protein from the immunoprecipitation (as shown in A) was normalized with those from the Western blotting. Relative phosphorylated protein level is expressed as a percentage of vehicle control ( n = 5, * P
    Figure Legend Snippet: Tyrosine phosphorylation level of β1 subunits in BK ‐ HEK 293 cells. (A) Images of immunoprecipitation and Western blotting in BK ‐ HEK 293 cells treated with vehicle (control), 100 ng/ml EGF , 1 mM orthovanadate ( OV ), 10 μM genistein, genistein plus OV , 10 μM tyrphostin AG 556 ( AG 556), and AG 556 plus OV . (B) Mean percentage values of relative tyrosine‐phosphorylated β1 protein. The amount of protein from the immunoprecipitation (as shown in A) was normalized with those from the Western blotting. Relative phosphorylated protein level is expressed as a percentage of vehicle control ( n = 5, * P

    Techniques Used: Immunoprecipitation, Western Blot

    6) Product Images from "Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca2+-activated K+ channels in bronchial smooth muscle cells"

    Article Title: Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca2+-activated K+ channels in bronchial smooth muscle cells

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00331.2019

    Large-conductance Ca 2+ -activated K + channel γ1-subunit (BKγ1) expression is selectively high in mouse bronchial smooth muscle (BSM). A : real-time PCR analyses of BKγ subunits (BKγ1–4) in mouse bronchial smooth muscles (BSMs; N = 3). B : real-time PCR analyses of BKα, BKβ1, and BKγ1 in several types of mouse SM tissues ( N = 4–5). C : real-time PCR analysis was performed to compare BKγ1 mRNA expression between mouse trachea and bronchus (trachea, N = 3; bronchus, N = 5). * P
    Figure Legend Snippet: Large-conductance Ca 2+ -activated K + channel γ1-subunit (BKγ1) expression is selectively high in mouse bronchial smooth muscle (BSM). A : real-time PCR analyses of BKγ subunits (BKγ1–4) in mouse bronchial smooth muscles (BSMs; N = 3). B : real-time PCR analyses of BKα, BKβ1, and BKγ1 in several types of mouse SM tissues ( N = 4–5). C : real-time PCR analysis was performed to compare BKγ1 mRNA expression between mouse trachea and bronchus (trachea, N = 3; bronchus, N = 5). * P

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    7) Product Images from "Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca2+-activated K+ channels in bronchial smooth muscle cells"

    Article Title: Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca2+-activated K+ channels in bronchial smooth muscle cells

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00331.2019

    Large-conductance Ca 2+ -activated K + channel γ1-subunit (BKγ1) expression is selectively high in mouse bronchial smooth muscle (BSM). A : real-time PCR analyses of BKγ subunits (BKγ1–4) in mouse bronchial smooth muscles (BSMs; N = 3). B : real-time PCR analyses of BKα, BKβ1, and BKγ1 in several types of mouse SM tissues ( N = 4–5). C : real-time PCR analysis was performed to compare BKγ1 mRNA expression between mouse trachea and bronchus (trachea, N = 3; bronchus, N = 5). * P
    Figure Legend Snippet: Large-conductance Ca 2+ -activated K + channel γ1-subunit (BKγ1) expression is selectively high in mouse bronchial smooth muscle (BSM). A : real-time PCR analyses of BKγ subunits (BKγ1–4) in mouse bronchial smooth muscles (BSMs; N = 3). B : real-time PCR analyses of BKα, BKβ1, and BKγ1 in several types of mouse SM tissues ( N = 4–5). C : real-time PCR analysis was performed to compare BKγ1 mRNA expression between mouse trachea and bronchus (trachea, N = 3; bronchus, N = 5). * P

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    8) Product Images from "MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria"

    Article Title: MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria

    Journal: The Journal of physiology

    doi: 10.1113/JP277769

    Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p
    Figure Legend Snippet: Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p

    Techniques Used:

    MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.
    Figure Legend Snippet: MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.

    Techniques Used: Immunoprecipitation, Activity Assay

    Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p
    Figure Legend Snippet: Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p

    Techniques Used: Cell Culture, Transfection, Labeling

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Alomone Labs bk β1 subunit
    Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of <t>β1-subunit</t> A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p
    Bk β1 Subunit, 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/bk β1 subunit/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bk β1 subunit - by Bioz Stars, 2022-05
    94/100 stars
      Buy from Supplier

    Image Search Results


    Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p

    Journal: The Journal of physiology

    Article Title: MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria

    doi: 10.1113/JP277769

    Figure Lengend Snippet: Mitochondrial calcium uptake is impaired by Paxilline and by genetic ablation of β1-subunit A) Paxilline reduces the amount of mitochondrial Ca 2+ necessary to induce formation and opening of mPTP. B) Mitochondria from the β1 KO required less Ca 2+ than mitochondria from the Wt to trigger the opening of mPTP. C) Calcium retention capacity values obtained in A for paxilline and in B for the β1-KO mitochondria. Bars SEM, (* p

    Article Snippet: Polyclonal antibody against BKCa (Rabbit Anti-KCNMA1 Cat. APC-021 and APC-151), and polyclonal antibody for BK-β1 subunit (Rabbit Anti-KCNMB1, Cat. APC-036) were from Alomone labs.

    Techniques:

    MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.

    Journal: The Journal of physiology

    Article Title: MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria

    doi: 10.1113/JP277769

    Figure Lengend Snippet: MitoBK Ca alpha and auxiliary β1 subunit association in cardiac mitochondria. A) Immunoprecipitation (IP) of BK Ca alpha and BK-β1 subunit with an antibody against BK Ca ). Taken together, these results indicates an association between mitoBK Ca and its auxiliary β1 subunit. Having demonstrated this, we characterized the biophysical properties of mitoBK Ca in Wt and β1-KO cardiac mitoplasts. B) Single-channel currents of mitoBK Ca recorded from Wt mitoplasts. The P o of the channel was 0.9 ± 0.08, n=4, in average at +80 mV and the indicated matrix Ca 2+ . C) Representative traces of a mitoplast from the β1 KO, were no single-channel current was detected at the indicated voltages and matrix Ca 2+ (upper traces). Few mitoplasts (5 out of 28, mitoplasts, n=5 hearts) showed mitoBK Ca channel activity with a P o of 0.4 ± 0.004, n=3 at +40 mV in the indicated matrix Ca 2+ . D) Plots of I vs. V at 12 µM matrix Ca 2+ from Wt and β1 KO mitoplasts (data from 6 and 3 patches, respectively). A slope conductance of 302±26 (n=4) and 335 ±15 pS (n=3) was calculated for Wt and β1 KO, respectively. E) Plots of P o vs. V for mitoBK Ca channels, data points represent the average of 4 and 3 mitoplasts for Wt and BK-β1 KO, respectively. Bars SEM.

    Article Snippet: Polyclonal antibody against BKCa (Rabbit Anti-KCNMA1 Cat. APC-021 and APC-151), and polyclonal antibody for BK-β1 subunit (Rabbit Anti-KCNMB1, Cat. APC-036) were from Alomone labs.

    Techniques: Immunoprecipitation, Activity Assay

    Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p

    Journal: The Journal of physiology

    Article Title: MitoBKCa channel is functionally associated with its regulatory β1 subunit in cardiac mitochondria

    doi: 10.1113/JP277769

    Figure Lengend Snippet: Localization of BKDEC and β1 subunit in HeLa cells. A) Cultured cells co-transfected with BKDEC alpha+β1subunit, loaded with mitotracker red, and DAPI B) β1-flag labeled with an anti-flag C) BKDEC labeled with anti-HA. D) Merge of mitotracker red, BKDEC and β1. E) Cross-correlation index (CCi), relative to mitotracker red signal, calculated from cells overexpressing BKDEC alone (Cci=0.53±0.05) and co-expressed with β1 subunit (Cci=0.77±0.01, n=11 cells from 3 different preparations).*p

    Article Snippet: Polyclonal antibody against BKCa (Rabbit Anti-KCNMA1 Cat. APC-021 and APC-151), and polyclonal antibody for BK-β1 subunit (Rabbit Anti-KCNMB1, Cat. APC-036) were from Alomone labs.

    Techniques: Cell Culture, Transfection, Labeling

    Decreased BK β1/α -subunit ratio in vascular tissues of db/db mice. A . Representative Western Blots of BK α and β1 subunits obtained from control and db/db vascular tissues. Samples containing 30 µg of protein from aorta whole homogenates were run on 15% acrylamide gels and probed with anti-BK α subunit antibody (1∶1000), anti-BK β1 subunit antibody (1∶500) and anti-actin (1∶8000). B . Bar graph represents normalized BKβ1/α densitometric ratios (n = 7 for each group). * P

    Journal: PLoS ONE

    Article Title: Abnormal Ca2+ Spark/STOC Coupling in Cerebral Artery Smooth Muscle Cells of Obese Type 2 Diabetic Mice

    doi: 10.1371/journal.pone.0053321

    Figure Lengend Snippet: Decreased BK β1/α -subunit ratio in vascular tissues of db/db mice. A . Representative Western Blots of BK α and β1 subunits obtained from control and db/db vascular tissues. Samples containing 30 µg of protein from aorta whole homogenates were run on 15% acrylamide gels and probed with anti-BK α subunit antibody (1∶1000), anti-BK β1 subunit antibody (1∶500) and anti-actin (1∶8000). B . Bar graph represents normalized BKβ1/α densitometric ratios (n = 7 for each group). * P

    Article Snippet: Supernatants were fractionated on 15% SDS-PAGE gels, transferred onto nitrocellulose membranes (1 h at 100 V, Hybond-ECL, GE Healthcare Bio-Sciences Corp, NJ, USA) and probed with anti-BK α antibody (1∶1000; Alomone Labs, Jerusalem Israel), anti BK β1 antibody (1∶500; Alomone Labs, Jerusalem Israel), anti RyR (1∶5000; Thermo Scientific) and anti-actin antibody (1∶8000, Sigma-Aldrich) in phosphate-buffered saline solution containing Tween-20 (PBS-T; in mmol/L: 3 KH2 PO4 , 10 Na2 HPO4 , 150 NaCl, 0.1% Tween-20, pH 7.2–7.4).

    Techniques: Mouse Assay, Western Blot

    Effect of genistein on BK channel current in BK ‐ HEK 293 cells. (A) Voltage‐dependent BK current recorded in a typical BK ‐ HEK 293 cell stably expressing both α‐ and β1‐subunit with the voltage protocol as shown in the inset in the absence and presence of 10 μM genistein, and upon washout. (B) Original BK current traces in a representative BK ‐ HEK 293 cell during control, in the presence of 10 μM genistein, and genistein plus 1 mM orthovanadate ( OV ). (C) Mean percentage values of BK current measured at +70 mV during control, 10 μM genistein, washout, 10 μM genistein and genistein plus 1 mM OV ( n = 6, ** P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase

    doi: 10.1111/jcmm.13103

    Figure Lengend Snippet: Effect of genistein on BK channel current in BK ‐ HEK 293 cells. (A) Voltage‐dependent BK current recorded in a typical BK ‐ HEK 293 cell stably expressing both α‐ and β1‐subunit with the voltage protocol as shown in the inset in the absence and presence of 10 μM genistein, and upon washout. (B) Original BK current traces in a representative BK ‐ HEK 293 cell during control, in the presence of 10 μM genistein, and genistein plus 1 mM orthovanadate ( OV ). (C) Mean percentage values of BK current measured at +70 mV during control, 10 μM genistein, washout, 10 μM genistein and genistein plus 1 mM OV ( n = 6, ** P

    Article Snippet: Proteins were immunoprecipitated overnight at 4°C using 1 μg of mouse anti‐BK channel α (APC‐021; Alomone Labs, Jerusalem, Israel) antibody or 1 μg of mouse anti‐β1 (APC‐036; Alomone Labs, Jerusalem, Israel) antibody and 20 μl of Protein A/G beads (sc‐2003; Santa Cruz Biotechnology, Inc. CA, USA).

    Techniques: Stable Transfection, Expressing

    Membrane current in HEK 293 cells stably expressing human BK channel α‐ and β1‐subunits. (A) Voltage‐dependent BK current traces recorded in a representative cell with the voltage protocol as shown in the inset before and after application of 1 μM paxilline (a selective BK channel blocker), and washout of paxilline. (B) I‐V relationships of BK current in the absence and presence of 1 μM paxilline, and upon washout ( n = 5, * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase

    doi: 10.1111/jcmm.13103

    Figure Lengend Snippet: Membrane current in HEK 293 cells stably expressing human BK channel α‐ and β1‐subunits. (A) Voltage‐dependent BK current traces recorded in a representative cell with the voltage protocol as shown in the inset before and after application of 1 μM paxilline (a selective BK channel blocker), and washout of paxilline. (B) I‐V relationships of BK current in the absence and presence of 1 μM paxilline, and upon washout ( n = 5, * P

    Article Snippet: Proteins were immunoprecipitated overnight at 4°C using 1 μg of mouse anti‐BK channel α (APC‐021; Alomone Labs, Jerusalem, Israel) antibody or 1 μg of mouse anti‐β1 (APC‐036; Alomone Labs, Jerusalem, Israel) antibody and 20 μl of Protein A/G beads (sc‐2003; Santa Cruz Biotechnology, Inc. CA, USA).

    Techniques: Stable Transfection, Expressing

    Tyrosine phosphorylation level of β1 subunits in BK ‐ HEK 293 cells. (A) Images of immunoprecipitation and Western blotting in BK ‐ HEK 293 cells treated with vehicle (control), 100 ng/ml EGF , 1 mM orthovanadate ( OV ), 10 μM genistein, genistein plus OV , 10 μM tyrphostin AG 556 ( AG 556), and AG 556 plus OV . (B) Mean percentage values of relative tyrosine‐phosphorylated β1 protein. The amount of protein from the immunoprecipitation (as shown in A) was normalized with those from the Western blotting. Relative phosphorylated protein level is expressed as a percentage of vehicle control ( n = 5, * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Tyrphostin AG556 increases the activity of large conductance Ca2+‐activated K+ channels by inhibiting epidermal growth factor receptor tyrosine kinase

    doi: 10.1111/jcmm.13103

    Figure Lengend Snippet: Tyrosine phosphorylation level of β1 subunits in BK ‐ HEK 293 cells. (A) Images of immunoprecipitation and Western blotting in BK ‐ HEK 293 cells treated with vehicle (control), 100 ng/ml EGF , 1 mM orthovanadate ( OV ), 10 μM genistein, genistein plus OV , 10 μM tyrphostin AG 556 ( AG 556), and AG 556 plus OV . (B) Mean percentage values of relative tyrosine‐phosphorylated β1 protein. The amount of protein from the immunoprecipitation (as shown in A) was normalized with those from the Western blotting. Relative phosphorylated protein level is expressed as a percentage of vehicle control ( n = 5, * P

    Article Snippet: Proteins were immunoprecipitated overnight at 4°C using 1 μg of mouse anti‐BK channel α (APC‐021; Alomone Labs, Jerusalem, Israel) antibody or 1 μg of mouse anti‐β1 (APC‐036; Alomone Labs, Jerusalem, Israel) antibody and 20 μl of Protein A/G beads (sc‐2003; Santa Cruz Biotechnology, Inc. CA, USA).

    Techniques: Immunoprecipitation, Western Blot