bk β1 antibody  (Alomone Labs)


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    Alomone Labs bk β1 antibody
    A . Representative Western Blots of BK α and <t>β1</t> 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 <0.05.
    Bk β1 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/bk β1 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bk β1 antibody - by Bioz Stars, 2023-01
    94/100 stars

    Images

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

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

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0053321

    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 <0.05.
    Figure Legend Snippet: 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 <0.05.

    Techniques Used: Western Blot

    bk β1 antibody  (Alomone Labs)


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    Alomone Labs bk β1 antibody
    A . Representative Western Blots of BK α and <t>β1</t> 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 <0.05.
    Bk β1 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/bk β1 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bk β1 antibody - by Bioz Stars, 2023-01
    94/100 stars

    Images

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

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

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0053321

    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 <0.05.
    Figure Legend Snippet: 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 <0.05.

    Techniques Used: Western Blot

    bk ca β1 subunit  (Alomone Labs)


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    Alomone Labs bk ca β1 subunit
    Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of <t>BK</t> <t>Ca</t> channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and <t>β1</t> subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.
    Bk Ca 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
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    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bk ca β1 subunit - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Aldosterone-Induced Sarco/Endoplasmic Reticulum Ca 2+ Pump Upregulation Counterbalances Ca v 1.2-Mediated Ca 2+ Influx in Mesenteric Arteries"

    Article Title: Aldosterone-Induced Sarco/Endoplasmic Reticulum Ca 2+ Pump Upregulation Counterbalances Ca v 1.2-Mediated Ca 2+ Influx in Mesenteric Arteries

    Journal: Frontiers in Physiology

    doi: 10.3389/fphys.2022.834220

    Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of BK Ca channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and β1 subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.
    Figure Legend Snippet: Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of BK Ca channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and β1 subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.

    Techniques Used: Expressing, Western Blot

    Proposed model for ALDO-mediated upregulation of the functional unit that controls Ca 2+ dynamics at the SR-PM nanodomain of MASMCs. In normal conditions (CONTROL, left ) K + -mediated membrane depolarization induces a Ca 2+ influx via Ca v 1.2 (LTCCs). This Ca 2+ entry is buffered by the SERCA pump toward the luminal SR Ca 2+ reservoirs activating RyRs (Ca 2+ sparks) and BK Ca channels (STOCs). Ca v 1.2, SERCA pump, RyRs and BK Ca channels work as a functional unit in the PM-SR nanodomain regulating [Ca 2+ ] cyt , luminal SR Ca 2+ levels, and opposing vasoconstriction. The treatment of MAs with aldosterone (ALDO, right ) increases Ca v 1.2 protein expression and induces higher Ca 2+ entry in MASMCs. However, the depolarization-induced vascular contraction was not enhanced because of the upregulation of this functional unit, which involves increased expression and activity of SERCA pump controlling abnormal Ca 2+ influx at the PM-SR nanodomain, increasing SR Ca 2+ content, Ca 2+ spark and STOC frequencies, opposing to depolarization-induced vasoconstriction and enhancing ACh-mediated vasorelaxation.
    Figure Legend Snippet: Proposed model for ALDO-mediated upregulation of the functional unit that controls Ca 2+ dynamics at the SR-PM nanodomain of MASMCs. In normal conditions (CONTROL, left ) K + -mediated membrane depolarization induces a Ca 2+ influx via Ca v 1.2 (LTCCs). This Ca 2+ entry is buffered by the SERCA pump toward the luminal SR Ca 2+ reservoirs activating RyRs (Ca 2+ sparks) and BK Ca channels (STOCs). Ca v 1.2, SERCA pump, RyRs and BK Ca channels work as a functional unit in the PM-SR nanodomain regulating [Ca 2+ ] cyt , luminal SR Ca 2+ levels, and opposing vasoconstriction. The treatment of MAs with aldosterone (ALDO, right ) increases Ca v 1.2 protein expression and induces higher Ca 2+ entry in MASMCs. However, the depolarization-induced vascular contraction was not enhanced because of the upregulation of this functional unit, which involves increased expression and activity of SERCA pump controlling abnormal Ca 2+ influx at the PM-SR nanodomain, increasing SR Ca 2+ content, Ca 2+ spark and STOC frequencies, opposing to depolarization-induced vasoconstriction and enhancing ACh-mediated vasorelaxation.

    Techniques Used: Functional Assay, Expressing, Activity Assay

    apc 036  (Alomone Labs)


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    Alomone Labs apc 036
    Apc 036, 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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    Average 94 stars, based on 1 article reviews
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    apc 036 - by Bioz Stars, 2023-01
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    bk beta1  (Alomone Labs)


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    Alomone Labs bk beta1
    Antibody list.
    Bk Beta1, 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 beta1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    bk beta1 - by Bioz Stars, 2023-01
    94/100 stars

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    1) Product Images from "Low Salt Delivery Triggers Autocrine Release of Prostaglandin E2 From the Aldosterone-Sensitive Distal Nephron in Familial Hyperkalemic Hypertension Mice"

    Article Title: Low Salt Delivery Triggers Autocrine Release of Prostaglandin E2 From the Aldosterone-Sensitive Distal Nephron in Familial Hyperkalemic Hypertension Mice

    Journal: Frontiers in Physiology

    doi: 10.3389/fphys.2021.787323

    Antibody list.
    Figure Legend Snippet: Antibody list.

    Techniques Used: Immunofluorescence, Western Blot

    Inhibition of the EP1 receptor rescues renal outer medullary potassium (ROMK) protein abundance. (A) plasma K+, (B) Total K+ excretion: total K+ intake ratio per individual mouse, (C) transtubular K+ gradient of an individual mouse, and (D) western blot and analysis of ROMK and (E) BK-beta1. * p < 0.05; statistical significance evaluated by two-tailed t -test.
    Figure Legend Snippet: Inhibition of the EP1 receptor rescues renal outer medullary potassium (ROMK) protein abundance. (A) plasma K+, (B) Total K+ excretion: total K+ intake ratio per individual mouse, (C) transtubular K+ gradient of an individual mouse, and (D) western blot and analysis of ROMK and (E) BK-beta1. * p < 0.05; statistical significance evaluated by two-tailed t -test.

    Techniques Used: Inhibition, Western Blot, Two Tailed Test

    bkβ1  (Alomone Labs)


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    Alomone Labs bkβ1
    (A) 12 weeks after active immunization with AT1R-ECII, the OD value of serum AT1-AA in rats was detected. Detection of (B) caudal vein blood pressure and (C) vascular wall thickness of thoracic aorta in AT1-AA-positive rats, n=5. (D) The light and heavy chains of AT1-AA isolated by SDS-PAGE gel. (E) Effect of AT1-AA on the beating of neonatal rat cardiomyocytes. (F) The effect of AT1-AA on vasomotion was detected by vascular ring. Detection of <t>BKβ1</t> protein level in (G) thoracic aorta of AT1-AA-positive rats and (I) VSMCs treated with AT1-AA, n=5. (H) Detection of BKβ1 protein level in thoracic aorta of AT1-AA-positive rats by immunofluorescence method, n=4.
    Bkβ1, 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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    bkβ1 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "MiR-339-3p aggravates rat vascular inflammation induced by AT1R autoantibodies by down-regulating BKα protein expression"

    Article Title: MiR-339-3p aggravates rat vascular inflammation induced by AT1R autoantibodies by down-regulating BKα protein expression

    Journal: bioRxiv

    doi: 10.1101/2021.10.17.464722

    (A) 12 weeks after active immunization with AT1R-ECII, the OD value of serum AT1-AA in rats was detected. Detection of (B) caudal vein blood pressure and (C) vascular wall thickness of thoracic aorta in AT1-AA-positive rats, n=5. (D) The light and heavy chains of AT1-AA isolated by SDS-PAGE gel. (E) Effect of AT1-AA on the beating of neonatal rat cardiomyocytes. (F) The effect of AT1-AA on vasomotion was detected by vascular ring. Detection of BKβ1 protein level in (G) thoracic aorta of AT1-AA-positive rats and (I) VSMCs treated with AT1-AA, n=5. (H) Detection of BKβ1 protein level in thoracic aorta of AT1-AA-positive rats by immunofluorescence method, n=4.
    Figure Legend Snippet: (A) 12 weeks after active immunization with AT1R-ECII, the OD value of serum AT1-AA in rats was detected. Detection of (B) caudal vein blood pressure and (C) vascular wall thickness of thoracic aorta in AT1-AA-positive rats, n=5. (D) The light and heavy chains of AT1-AA isolated by SDS-PAGE gel. (E) Effect of AT1-AA on the beating of neonatal rat cardiomyocytes. (F) The effect of AT1-AA on vasomotion was detected by vascular ring. Detection of BKβ1 protein level in (G) thoracic aorta of AT1-AA-positive rats and (I) VSMCs treated with AT1-AA, n=5. (H) Detection of BKβ1 protein level in thoracic aorta of AT1-AA-positive rats by immunofluorescence method, n=4.

    Techniques Used: Isolation, SDS Page, Immunofluorescence

    anti bkβ1 antibody  (Alomone Labs)


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    Alomone Labs anti bkβ1 antibody
    Large-conductance Ca2+-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, <t>BKβ1,</t> 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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
    Anti Bkβ1 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
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    Images

    1) Product Images from "Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca 2+ -activated K + channels in bronchial smooth muscle cells"

    Article Title: Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca 2+ -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 Ca2+-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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
    Figure Legend Snippet: Large-conductance Ca2+-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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Microscopy

    Voltage-dependence of the large-conductance Ca2+-activated K+ (BK) channels in mouse bronchial smooth muscle cells (mBSMCs), mouse aortic SMCs (mASMCs), and a HEK293-based heterologous system. A: BK currents were recorded at pCa 8.0 using whole cell patch-clamp recordings in HEK293 cells expressing BKα-mCherry (BKα), BKα-mCherry + BKβ1-GFP (BKα+β1), BKα+γ1, and BKα + BKβ1-mCherry + BKγ1-GFP (BKα+β1+γ1). K+ currents were recorded in response to pulse protocols shown in insets. Representative traces of whole cell currents and tail currents from each cell are shown. B: BK activation curves in mBSMCs (n = 5), mASMCs (n = 5), BKα (n = 5), BKα+β1 (n = 5), BKα+γ1 (n = 5), and BKα+β1+γ1 (n = 4) in A and Fig. 4. Relationships between selected test potential by the maximum current amplitude (G/Gmax) and voltage were fitted with the Boltzmann equation. C: voltage values required for half-maximum activation (V1/2) were calculated by the activation curve of B. *P < 0.05 vs. mBSMCs, by Tukey’s test.
    Figure Legend Snippet: Voltage-dependence of the large-conductance Ca2+-activated K+ (BK) channels in mouse bronchial smooth muscle cells (mBSMCs), mouse aortic SMCs (mASMCs), and a HEK293-based heterologous system. A: BK currents were recorded at pCa 8.0 using whole cell patch-clamp recordings in HEK293 cells expressing BKα-mCherry (BKα), BKα-mCherry + BKβ1-GFP (BKα+β1), BKα+γ1, and BKα + BKβ1-mCherry + BKγ1-GFP (BKα+β1+γ1). K+ currents were recorded in response to pulse protocols shown in insets. Representative traces of whole cell currents and tail currents from each cell are shown. B: BK activation curves in mBSMCs (n = 5), mASMCs (n = 5), BKα (n = 5), BKα+β1 (n = 5), BKα+γ1 (n = 5), and BKα+β1+γ1 (n = 4) in A and Fig. 4. Relationships between selected test potential by the maximum current amplitude (G/Gmax) and voltage were fitted with the Boltzmann equation. C: voltage values required for half-maximum activation (V1/2) were calculated by the activation curve of B. *P < 0.05 vs. mBSMCs, by Tukey’s test.

    Techniques Used: Patch Clamp, Expressing, Activation Assay

    anti bkβ1 antibody  (Alomone Labs)


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    Alomone Labs anti bkβ1 antibody
    Large-conductance Ca2+-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, <t>BKβ1,</t> 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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
    Anti Bkβ1 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/anti bkβ1 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti bkβ1 antibody - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca 2+ -activated K + channels in bronchial smooth muscle cells"

    Article Title: Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca 2+ -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 Ca2+-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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
    Figure Legend Snippet: Large-conductance Ca2+-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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Microscopy

    Voltage-dependence of the large-conductance Ca2+-activated K+ (BK) channels in mouse bronchial smooth muscle cells (mBSMCs), mouse aortic SMCs (mASMCs), and a HEK293-based heterologous system. A: BK currents were recorded at pCa 8.0 using whole cell patch-clamp recordings in HEK293 cells expressing BKα-mCherry (BKα), BKα-mCherry + BKβ1-GFP (BKα+β1), BKα+γ1, and BKα + BKβ1-mCherry + BKγ1-GFP (BKα+β1+γ1). K+ currents were recorded in response to pulse protocols shown in insets. Representative traces of whole cell currents and tail currents from each cell are shown. B: BK activation curves in mBSMCs (n = 5), mASMCs (n = 5), BKα (n = 5), BKα+β1 (n = 5), BKα+γ1 (n = 5), and BKα+β1+γ1 (n = 4) in A and Fig. 4. Relationships between selected test potential by the maximum current amplitude (G/Gmax) and voltage were fitted with the Boltzmann equation. C: voltage values required for half-maximum activation (V1/2) were calculated by the activation curve of B. *P < 0.05 vs. mBSMCs, by Tukey’s test.
    Figure Legend Snippet: Voltage-dependence of the large-conductance Ca2+-activated K+ (BK) channels in mouse bronchial smooth muscle cells (mBSMCs), mouse aortic SMCs (mASMCs), and a HEK293-based heterologous system. A: BK currents were recorded at pCa 8.0 using whole cell patch-clamp recordings in HEK293 cells expressing BKα-mCherry (BKα), BKα-mCherry + BKβ1-GFP (BKα+β1), BKα+γ1, and BKα + BKβ1-mCherry + BKγ1-GFP (BKα+β1+γ1). K+ currents were recorded in response to pulse protocols shown in insets. Representative traces of whole cell currents and tail currents from each cell are shown. B: BK activation curves in mBSMCs (n = 5), mASMCs (n = 5), BKα (n = 5), BKα+β1 (n = 5), BKα+γ1 (n = 5), and BKα+β1+γ1 (n = 4) in A and Fig. 4. Relationships between selected test potential by the maximum current amplitude (G/Gmax) and voltage were fitted with the Boltzmann equation. C: voltage values required for half-maximum activation (V1/2) were calculated by the activation curve of B. *P < 0.05 vs. mBSMCs, by Tukey’s test.

    Techniques Used: Patch Clamp, Expressing, Activation Assay

    anti sloβ1  (Alomone Labs)


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    kcnmb1  (Alomone Labs)


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    170 bkca β1 antibody  (Alomone Labs)


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    Alomone Labs bk β1 antibody
    A . Representative Western Blots of BK α and <t>β1</t> 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 <0.05.
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    Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of <t>BK</t> <t>Ca</t> channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and <t>β1</t> subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.
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    Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of <t>BK</t> <t>Ca</t> channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and <t>β1</t> subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.
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    (A) 12 weeks after active immunization with AT1R-ECII, the OD value of serum AT1-AA in rats was detected. Detection of (B) caudal vein blood pressure and (C) vascular wall thickness of thoracic aorta in AT1-AA-positive rats, n=5. (D) The light and heavy chains of AT1-AA isolated by SDS-PAGE gel. (E) Effect of AT1-AA on the beating of neonatal rat cardiomyocytes. (F) The effect of AT1-AA on vasomotion was detected by vascular ring. Detection of <t>BKβ1</t> protein level in (G) thoracic aorta of AT1-AA-positive rats and (I) VSMCs treated with AT1-AA, n=5. (H) Detection of BKβ1 protein level in thoracic aorta of AT1-AA-positive rats by immunofluorescence method, n=4.
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    Alomone Labs anti bkβ1 antibody
    Large-conductance Ca2+-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, <t>BKβ1,</t> 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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
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    Large-conductance Ca2+-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, <t>BKβ1,</t> 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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
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    Alomone Labs kcnmb1
    Large-conductance Ca2+-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, <t>BKβ1,</t> 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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
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    Alomone Labs 170 bkca β1 antibody
    Large-conductance Ca2+-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, <t>BKβ1,</t> 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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.
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    Image Search Results


    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 <0.05.

    Journal: PLoS ONE

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

    doi: 10.1371/journal.pone.0053321

    Figure Lengend Snippet: 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 <0.05.

    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 KH 2 PO 4 , 10 Na 2 HPO 4 , 150 NaCl, 0.1% Tween-20, pH 7.2–7.4).

    Techniques: Western Blot

    Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of BK Ca channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and β1 subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.

    Journal: Frontiers in Physiology

    Article Title: Aldosterone-Induced Sarco/Endoplasmic Reticulum Ca 2+ Pump Upregulation Counterbalances Ca v 1.2-Mediated Ca 2+ Influx in Mesenteric Arteries

    doi: 10.3389/fphys.2022.834220

    Figure Lengend Snippet: Aldosterone treatment increases the frequency and the amplitude of STOCs in MASMCs without modifying BK channel subunit expression. (A) Representative traces of STOCs recorded at a holding potential of –40 mV from MASMCs in the absence (CONTROL, black trace ) or after 24 h-treatment with aldosterone 10 nM (ALDO, red trace ). Scatterplots with mean ± SEM illustrate STOC frequency ( B , normalized with respect to cell capacitance, in events/s/pF), STOC amplitude ( C , normalized with respect to cell capacitance, in pA/pF), and STOC area-under-the-curve ( D , in pA.s) in control MASMCs ( n = 119 events/ n = 12 cells/ N = 4 animals, empty circles ) and ALDO-treated cells ( n = 333 events/ n = 12 cells/ N = 5 animals, red circles ). * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control group. (E) Histogram distribution of normalized STOC amplitudes in control ( n = 119 events/ n = 12 cells/ N = 4 rats, white bars ) and ALDO-treated MASMCs ( n = 333 events/ n = 12 cells/ N = 5 rats, red bars ) indicates the increase in the amplitude of STOCs above 3.6 pA/pF in ALDO-treated cells. (F,G) Representative immunoblot images and scatterplot with mean ± SEM of BK Ca channel α subunit expression ( n = 4 control samples, empty circles ; n = 4 ALDO-treated samples, red circles ), and β1 subunit expression ( n = 5 control samples, empty triangles ; n = 5 ALDO-treated samples, red triangles ). Each sample was prepared with a pool of 3–4 MA segments from three rats. Values were normalized with respect to GAPDH expression.

    Article Snippet: Separated proteins were transferred onto nitrocellulose or PVDF membrane for 2 h, 100 V at 4°C and blocked from non-specific binding with 5% non-fat dried milk in phosphate buffered saline-Tween 20 (0.1%) (PBS-T) for 1 h, before the incubation with commercial primary antibodies previously used at indicated publications, against Ca v 1.2 (1:200, Cat# AB10515, Millipore, Merck KGaA, Darmstadt, Germany) ( ); SERCA2 pump (1:4,000, Cat# ab2861, Abcam, Cambridge, MA, United States) ( ); Ryanodine receptor (RyR, 1:5000, Cat# ab2868, Abcam, Cambridge, MA, United States) ( ); calsequestrin (CSQ2, 1:4,000, Cat# ab108289, Abcam, Cambridge, MA, United States) ( ); sorcin (1:1,000, a kind gift from Héctor H. Valdivia laboratory, University of Wisconsin, Madison, WI, United States) ( ); FKBP12.6 (1:2,000, Cat# sc-376135, Santa Cruz Biotechnology, Inc., Dallas, TX, United States) ( ); MR (1:200; Cat# MRN2 2B7, DSHB, University of Iowa, Iowa City, IA, United States) ( ); BK Ca α subunit (1:200, Cat# APC-009, Alomone Labs, Jerusalem, Israel) , BK Ca β1 subunit (1:5000, Cat# APC-036, Alomone Labs, Jerusalem, Israel) , Orai1 (1:200, Cat# O8264, Sigma–Aldrich Química, S.L.

    Techniques: Expressing, Western Blot

    Proposed model for ALDO-mediated upregulation of the functional unit that controls Ca 2+ dynamics at the SR-PM nanodomain of MASMCs. In normal conditions (CONTROL, left ) K + -mediated membrane depolarization induces a Ca 2+ influx via Ca v 1.2 (LTCCs). This Ca 2+ entry is buffered by the SERCA pump toward the luminal SR Ca 2+ reservoirs activating RyRs (Ca 2+ sparks) and BK Ca channels (STOCs). Ca v 1.2, SERCA pump, RyRs and BK Ca channels work as a functional unit in the PM-SR nanodomain regulating [Ca 2+ ] cyt , luminal SR Ca 2+ levels, and opposing vasoconstriction. The treatment of MAs with aldosterone (ALDO, right ) increases Ca v 1.2 protein expression and induces higher Ca 2+ entry in MASMCs. However, the depolarization-induced vascular contraction was not enhanced because of the upregulation of this functional unit, which involves increased expression and activity of SERCA pump controlling abnormal Ca 2+ influx at the PM-SR nanodomain, increasing SR Ca 2+ content, Ca 2+ spark and STOC frequencies, opposing to depolarization-induced vasoconstriction and enhancing ACh-mediated vasorelaxation.

    Journal: Frontiers in Physiology

    Article Title: Aldosterone-Induced Sarco/Endoplasmic Reticulum Ca 2+ Pump Upregulation Counterbalances Ca v 1.2-Mediated Ca 2+ Influx in Mesenteric Arteries

    doi: 10.3389/fphys.2022.834220

    Figure Lengend Snippet: Proposed model for ALDO-mediated upregulation of the functional unit that controls Ca 2+ dynamics at the SR-PM nanodomain of MASMCs. In normal conditions (CONTROL, left ) K + -mediated membrane depolarization induces a Ca 2+ influx via Ca v 1.2 (LTCCs). This Ca 2+ entry is buffered by the SERCA pump toward the luminal SR Ca 2+ reservoirs activating RyRs (Ca 2+ sparks) and BK Ca channels (STOCs). Ca v 1.2, SERCA pump, RyRs and BK Ca channels work as a functional unit in the PM-SR nanodomain regulating [Ca 2+ ] cyt , luminal SR Ca 2+ levels, and opposing vasoconstriction. The treatment of MAs with aldosterone (ALDO, right ) increases Ca v 1.2 protein expression and induces higher Ca 2+ entry in MASMCs. However, the depolarization-induced vascular contraction was not enhanced because of the upregulation of this functional unit, which involves increased expression and activity of SERCA pump controlling abnormal Ca 2+ influx at the PM-SR nanodomain, increasing SR Ca 2+ content, Ca 2+ spark and STOC frequencies, opposing to depolarization-induced vasoconstriction and enhancing ACh-mediated vasorelaxation.

    Article Snippet: Separated proteins were transferred onto nitrocellulose or PVDF membrane for 2 h, 100 V at 4°C and blocked from non-specific binding with 5% non-fat dried milk in phosphate buffered saline-Tween 20 (0.1%) (PBS-T) for 1 h, before the incubation with commercial primary antibodies previously used at indicated publications, against Ca v 1.2 (1:200, Cat# AB10515, Millipore, Merck KGaA, Darmstadt, Germany) ( ); SERCA2 pump (1:4,000, Cat# ab2861, Abcam, Cambridge, MA, United States) ( ); Ryanodine receptor (RyR, 1:5000, Cat# ab2868, Abcam, Cambridge, MA, United States) ( ); calsequestrin (CSQ2, 1:4,000, Cat# ab108289, Abcam, Cambridge, MA, United States) ( ); sorcin (1:1,000, a kind gift from Héctor H. Valdivia laboratory, University of Wisconsin, Madison, WI, United States) ( ); FKBP12.6 (1:2,000, Cat# sc-376135, Santa Cruz Biotechnology, Inc., Dallas, TX, United States) ( ); MR (1:200; Cat# MRN2 2B7, DSHB, University of Iowa, Iowa City, IA, United States) ( ); BK Ca α subunit (1:200, Cat# APC-009, Alomone Labs, Jerusalem, Israel) , BK Ca β1 subunit (1:5000, Cat# APC-036, Alomone Labs, Jerusalem, Israel) , Orai1 (1:200, Cat# O8264, Sigma–Aldrich Química, S.L.

    Techniques: Functional Assay, Expressing, Activity Assay

    Antibody list.

    Journal: Frontiers in Physiology

    Article Title: Low Salt Delivery Triggers Autocrine Release of Prostaglandin E2 From the Aldosterone-Sensitive Distal Nephron in Familial Hyperkalemic Hypertension Mice

    doi: 10.3389/fphys.2021.787323

    Figure Lengend Snippet: Antibody list.

    Article Snippet: Bk-beta1 , Alomone APC-036 , Rabbit , WB 1:6,000.

    Techniques: Immunofluorescence, Western Blot

    Inhibition of the EP1 receptor rescues renal outer medullary potassium (ROMK) protein abundance. (A) plasma K+, (B) Total K+ excretion: total K+ intake ratio per individual mouse, (C) transtubular K+ gradient of an individual mouse, and (D) western blot and analysis of ROMK and (E) BK-beta1. * p < 0.05; statistical significance evaluated by two-tailed t -test.

    Journal: Frontiers in Physiology

    Article Title: Low Salt Delivery Triggers Autocrine Release of Prostaglandin E2 From the Aldosterone-Sensitive Distal Nephron in Familial Hyperkalemic Hypertension Mice

    doi: 10.3389/fphys.2021.787323

    Figure Lengend Snippet: Inhibition of the EP1 receptor rescues renal outer medullary potassium (ROMK) protein abundance. (A) plasma K+, (B) Total K+ excretion: total K+ intake ratio per individual mouse, (C) transtubular K+ gradient of an individual mouse, and (D) western blot and analysis of ROMK and (E) BK-beta1. * p < 0.05; statistical significance evaluated by two-tailed t -test.

    Article Snippet: Bk-beta1 , Alomone APC-036 , Rabbit , WB 1:6,000.

    Techniques: Inhibition, Western Blot, Two Tailed Test

    (A) 12 weeks after active immunization with AT1R-ECII, the OD value of serum AT1-AA in rats was detected. Detection of (B) caudal vein blood pressure and (C) vascular wall thickness of thoracic aorta in AT1-AA-positive rats, n=5. (D) The light and heavy chains of AT1-AA isolated by SDS-PAGE gel. (E) Effect of AT1-AA on the beating of neonatal rat cardiomyocytes. (F) The effect of AT1-AA on vasomotion was detected by vascular ring. Detection of BKβ1 protein level in (G) thoracic aorta of AT1-AA-positive rats and (I) VSMCs treated with AT1-AA, n=5. (H) Detection of BKβ1 protein level in thoracic aorta of AT1-AA-positive rats by immunofluorescence method, n=4.

    Journal: bioRxiv

    Article Title: MiR-339-3p aggravates rat vascular inflammation induced by AT1R autoantibodies by down-regulating BKα protein expression

    doi: 10.1101/2021.10.17.464722

    Figure Lengend Snippet: (A) 12 weeks after active immunization with AT1R-ECII, the OD value of serum AT1-AA in rats was detected. Detection of (B) caudal vein blood pressure and (C) vascular wall thickness of thoracic aorta in AT1-AA-positive rats, n=5. (D) The light and heavy chains of AT1-AA isolated by SDS-PAGE gel. (E) Effect of AT1-AA on the beating of neonatal rat cardiomyocytes. (F) The effect of AT1-AA on vasomotion was detected by vascular ring. Detection of BKβ1 protein level in (G) thoracic aorta of AT1-AA-positive rats and (I) VSMCs treated with AT1-AA, n=5. (H) Detection of BKβ1 protein level in thoracic aorta of AT1-AA-positive rats by immunofluorescence method, n=4.

    Article Snippet: After the sections were deparaffinized and hydrated, the antigen was repaired by the high-pressure method, blocked with 10% goat serum, and then incubated with primary antibodies against BKα (Alomone Labs, APC-107, Israel), BKβ1 (Alomone Labs, APC-036, Israel), CD3 (Abcam, ab5690, UK), CD19 (Bioss, bs-0079R, China), CD68 (Affinity Biosciences., DF7518, USA) and α-SMA (Abcam, ab7817, UK) at 4°C overnight.

    Techniques: Isolation, SDS Page, Immunofluorescence

    Large-conductance Ca2+-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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.

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

    Article Title: Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca 2+ -activated K + channels in bronchial smooth muscle cells

    doi: 10.1152/ajplung.00331.2019

    Figure Lengend Snippet: Large-conductance Ca2+-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 < 0.05 vs. trachea by Student’s t test. D: Western blotting analyses of BKα, BKβ1, BKγ1, and β-actin, using specific antibodies, respectively, in mouse aortic and bronchial SMs (mASMs and mBSMs, respectively) on the same membrane. Similar results were obtained from 3 independent experiments. To obtain enough protein, 3 mice were used for each experiment. E: immunocytostaining was performed to reveal cellular localization of BKα and BKγ1. Images were acquired using a confocal microscope. Merged fluorescent images were overlapped with a cell image (right). Aortic SMC was used as a control, in which BKγ1 expression is low.

    Article Snippet: The blots were incubated with anti-LRRC26 antibody (1:100 dilution, sc-132325; Santa Cruz Biotechnology, Houston, TX), anti-BKα antibody (1:200 dilution, APC-107, Alomone Laboratories), or anti-BKβ1 antibody (1:100 dilution, APC-036, Alomone Laboratories) and then incubated with horseradish peroxidase-conjugated IgG antibody (Chemicon International, Temecula, CA).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Microscopy

    Voltage-dependence of the large-conductance Ca2+-activated K+ (BK) channels in mouse bronchial smooth muscle cells (mBSMCs), mouse aortic SMCs (mASMCs), and a HEK293-based heterologous system. A: BK currents were recorded at pCa 8.0 using whole cell patch-clamp recordings in HEK293 cells expressing BKα-mCherry (BKα), BKα-mCherry + BKβ1-GFP (BKα+β1), BKα+γ1, and BKα + BKβ1-mCherry + BKγ1-GFP (BKα+β1+γ1). K+ currents were recorded in response to pulse protocols shown in insets. Representative traces of whole cell currents and tail currents from each cell are shown. B: BK activation curves in mBSMCs (n = 5), mASMCs (n = 5), BKα (n = 5), BKα+β1 (n = 5), BKα+γ1 (n = 5), and BKα+β1+γ1 (n = 4) in A and Fig. 4. Relationships between selected test potential by the maximum current amplitude (G/Gmax) and voltage were fitted with the Boltzmann equation. C: voltage values required for half-maximum activation (V1/2) were calculated by the activation curve of B. *P < 0.05 vs. mBSMCs, by Tukey’s test.

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

    Article Title: Roles of LRRC26 as an auxiliary γ1-subunit of large-conductance Ca 2+ -activated K + channels in bronchial smooth muscle cells

    doi: 10.1152/ajplung.00331.2019

    Figure Lengend Snippet: Voltage-dependence of the large-conductance Ca2+-activated K+ (BK) channels in mouse bronchial smooth muscle cells (mBSMCs), mouse aortic SMCs (mASMCs), and a HEK293-based heterologous system. A: BK currents were recorded at pCa 8.0 using whole cell patch-clamp recordings in HEK293 cells expressing BKα-mCherry (BKα), BKα-mCherry + BKβ1-GFP (BKα+β1), BKα+γ1, and BKα + BKβ1-mCherry + BKγ1-GFP (BKα+β1+γ1). K+ currents were recorded in response to pulse protocols shown in insets. Representative traces of whole cell currents and tail currents from each cell are shown. B: BK activation curves in mBSMCs (n = 5), mASMCs (n = 5), BKα (n = 5), BKα+β1 (n = 5), BKα+γ1 (n = 5), and BKα+β1+γ1 (n = 4) in A and Fig. 4. Relationships between selected test potential by the maximum current amplitude (G/Gmax) and voltage were fitted with the Boltzmann equation. C: voltage values required for half-maximum activation (V1/2) were calculated by the activation curve of B. *P < 0.05 vs. mBSMCs, by Tukey’s test.

    Article Snippet: The blots were incubated with anti-LRRC26 antibody (1:100 dilution, sc-132325; Santa Cruz Biotechnology, Houston, TX), anti-BKα antibody (1:200 dilution, APC-107, Alomone Laboratories), or anti-BKβ1 antibody (1:100 dilution, APC-036, Alomone Laboratories) and then incubated with horseradish peroxidase-conjugated IgG antibody (Chemicon International, Temecula, CA).

    Techniques: Patch Clamp, Expressing, Activation Assay