rabbit anti bk  (Alomone Labs)


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    Alomone Labs rabbit anti bk
    Rabbit Anti Bk, 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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    anti bk ca  (Alomone Labs)


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    Alomone Labs anti bk ca
    Anti Bk Ca, 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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    rabbit anti bk  (Alomone Labs)


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    Alomone Labs rabbit anti bk
    Rabbit Anti Bk, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bk ca  (Alomone Labs)


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    Alomone Labs bk ca
    Bk Ca, 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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    polyclonal bk antibodies  (Alomone Labs)


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    Alomone Labs polyclonal bk antibodies
    Polyclonal Bk Antibodies, 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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    calcium modulated potassium channel bk  (Alomone Labs)


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    Alomone Labs calcium modulated potassium channel bk
    Calcium Modulated Potassium Channel Bk, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    antibody against bk ca β1 apc 036  (Alomone Labs)


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    Alomone Labs antibody against bk ca β1 apc 036
    <t>BK</t> <t>Ca</t> <t>-β1</t> expression is reduced in the carotid arteries of rat balloon-injured model. Representative images of H&E (A) and immunohistochemical staining of BK Ca −α and BK ca −β1 (B) in injured and sham-operated carotid arteries of rat balloon-injured model at 14 days post injury. Scale bar = 100 μm. (C) Quantified mRNA levels of BK ca −α and BK ca −β1 analyzed by qRT-PCR. Western blot images (D) and quantification (E) for indicated proteins. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 4∼6 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. sham).
    Antibody Against Bk Ca β1 Apc 036, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells"

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    Journal: Frontiers in Cardiovascular Medicine

    doi: 10.3389/fcvm.2022.1062695

    BK Ca -β1 expression is reduced in the carotid arteries of rat balloon-injured model. Representative images of H&E (A) and immunohistochemical staining of BK Ca −α and BK ca −β1 (B) in injured and sham-operated carotid arteries of rat balloon-injured model at 14 days post injury. Scale bar = 100 μm. (C) Quantified mRNA levels of BK ca −α and BK ca −β1 analyzed by qRT-PCR. Western blot images (D) and quantification (E) for indicated proteins. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 4∼6 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. sham).
    Figure Legend Snippet: BK Ca -β1 expression is reduced in the carotid arteries of rat balloon-injured model. Representative images of H&E (A) and immunohistochemical staining of BK Ca −α and BK ca −β1 (B) in injured and sham-operated carotid arteries of rat balloon-injured model at 14 days post injury. Scale bar = 100 μm. (C) Quantified mRNA levels of BK ca −α and BK ca −β1 analyzed by qRT-PCR. Western blot images (D) and quantification (E) for indicated proteins. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 4∼6 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. sham).

    Techniques Used: Expressing, Immunohistochemical staining, Staining, Quantitative RT-PCR, Western Blot

    BK Ca -β1 expression is positively associated with VSMC differentiation markers in vitro . Western blot images (A) and quantification (B) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs of passage 1 and passage 6. Western blot images (C) and quantification (D) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (E) and quantification (F) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3-5 of VSMCs were used in (C) through (F) . Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 5 for each group, ns, not significant, * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control).
    Figure Legend Snippet: BK Ca -β1 expression is positively associated with VSMC differentiation markers in vitro . Western blot images (A) and quantification (B) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs of passage 1 and passage 6. Western blot images (C) and quantification (D) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (E) and quantification (F) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3-5 of VSMCs were used in (C) through (F) . Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 5 for each group, ns, not significant, * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control).

    Techniques Used: Expressing, In Vitro, Western Blot

    Decreased BK ca −β1 expression is mediated by elevated PDGF-BB in vivo . (A) Quantified mRNA levels of PDGF-B and TGF-β analyzed by qRT-PCR in injured and sham-operated carotid arteries. Western blot images (B) and quantification (C) of BK ca −α and BK ca −β1 in the carotid arteries of mice injected with saline or PDGF-BB via tail vein. Data are presented as means ± SEM ( n = 6 for each group, ns, not significant, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. control).
    Figure Legend Snippet: Decreased BK ca −β1 expression is mediated by elevated PDGF-BB in vivo . (A) Quantified mRNA levels of PDGF-B and TGF-β analyzed by qRT-PCR in injured and sham-operated carotid arteries. Western blot images (B) and quantification (C) of BK ca −α and BK ca −β1 in the carotid arteries of mice injected with saline or PDGF-BB via tail vein. Data are presented as means ± SEM ( n = 6 for each group, ns, not significant, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. control).

    Techniques Used: Expressing, In Vivo, Quantitative RT-PCR, Western Blot, Injection

    BK Ca -β1 is essential for VSMCs to maintain a differentiated phenotype. (A) Representative micrographs of VSMCs treated with BK ca −β1 siRNA or scramble siRNA transfection. (B) Representative immunofluorescent images of F-actin of VSMCs stained with phalloidin (red). Nuclei were stained with DAPI (blue). Scale bar = 25 μm. (C) The percentage of spindle-like or polygonal-like cells in each group. Western blot images (D) and quantification (E) of BK ca −β1, α-SMA, and SM22α. Representative images (F) and quantification (G) of the areas of collagen gel in each group. The size of the collagen gel in each well was calculated compared to the total area of the well. Data are presented as means ± SEM ( n = 5∼6 for each group, *** P < 0.001 vs. scramble).
    Figure Legend Snippet: BK Ca -β1 is essential for VSMCs to maintain a differentiated phenotype. (A) Representative micrographs of VSMCs treated with BK ca −β1 siRNA or scramble siRNA transfection. (B) Representative immunofluorescent images of F-actin of VSMCs stained with phalloidin (red). Nuclei were stained with DAPI (blue). Scale bar = 25 μm. (C) The percentage of spindle-like or polygonal-like cells in each group. Western blot images (D) and quantification (E) of BK ca −β1, α-SMA, and SM22α. Representative images (F) and quantification (G) of the areas of collagen gel in each group. The size of the collagen gel in each well was calculated compared to the total area of the well. Data are presented as means ± SEM ( n = 5∼6 for each group, *** P < 0.001 vs. scramble).

    Techniques Used: Transfection, Staining, Western Blot

    BK Ca -β1 knockdown induces proliferative, migratory, and synthetic phenotype of VSMCs. (A) Proliferation curves of VSMCs transfected with BK ca −β1 or scrambled siRNA. Representative images (B) and quantification (C) of migration assay. (D) Quantified mRNA levels of inflammatory factors analyzed by qRT-PCR. Representative images (E) and quantification (F) of activities of MMP-9 and MMP-2 tested using gelatin zymography. Data are presented as means ± SEM ( n = 5∼6 for each group, * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. scramble).
    Figure Legend Snippet: BK Ca -β1 knockdown induces proliferative, migratory, and synthetic phenotype of VSMCs. (A) Proliferation curves of VSMCs transfected with BK ca −β1 or scrambled siRNA. Representative images (B) and quantification (C) of migration assay. (D) Quantified mRNA levels of inflammatory factors analyzed by qRT-PCR. Representative images (E) and quantification (F) of activities of MMP-9 and MMP-2 tested using gelatin zymography. Data are presented as means ± SEM ( n = 5∼6 for each group, * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. scramble).

    Techniques Used: Transfection, Migration, Quantitative RT-PCR, Zymography

    Decreased BK ca −β1 expression is correlated with VSMC dedifferentiation and atherosclerosis in human. Western blot images (A) and quantification (B) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (C) and quantification (D) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3–5 of VSMCs were used. (E) Representative western blot images of the protein levels of BK ca −α and BK ca −β1 in lysates of human carotid endarterectomy artery (CEA) and control internal mammary arteries (IMA). (F) Quantification was performed by calculating the ratio between the levels of BK ca −β1 and BK ca −α. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM (n = 3∼5 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. control).
    Figure Legend Snippet: Decreased BK ca −β1 expression is correlated with VSMC dedifferentiation and atherosclerosis in human. Western blot images (A) and quantification (B) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (C) and quantification (D) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3–5 of VSMCs were used. (E) Representative western blot images of the protein levels of BK ca −α and BK ca −β1 in lysates of human carotid endarterectomy artery (CEA) and control internal mammary arteries (IMA). (F) Quantification was performed by calculating the ratio between the levels of BK ca −β1 and BK ca −α. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM (n = 3∼5 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. control).

    Techniques Used: Expressing, 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
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    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

    anti bk α antibody  (Alomone Labs)


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    Alomone Labs anti bk α antibody
    A . Representative Western Blots of <t>BK</t> <t>α</t> 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.
    Anti Bk α Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti bk α antibody - by Bioz Stars, 2023-01
    80/100 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 channel β subunit 4  (Alomone Labs)


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    Alomone Labs bk ca channel β subunit 4
    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The <t>BK</t> <t>Ca</t> subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .
    Bk Ca Channel β Subunit 4, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bk ca channel β subunit 4 - by Bioz Stars, 2023-01
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    Images

    1) Product Images from "Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain"

    Article Title: Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0068125

    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .
    Figure Legend Snippet: A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .

    Techniques Used: Positive Control, Negative Control, Western Blot, Labeling, Marker, Electron Microscopy, Cell Culture, Immunolabeling, Transfection, Binding Assay, Staining

    Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.
    Figure Legend Snippet: Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.

    Techniques Used: Staining, Isolation, Blue Native PAGE, Western Blot

    rabbit polyclonal anti bk ca channel β subunit 4 antibody  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti bk ca channel β subunit 4 antibody
    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The <t>BK</t> <t>Ca</t> subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .
    Rabbit Polyclonal Anti Bk Ca Channel β Subunit 4 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 "Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain"

    Article Title: Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0068125

    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .
    Figure Legend Snippet: A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .

    Techniques Used: Positive Control, Negative Control, Western Blot, Labeling, Marker, Electron Microscopy, Cell Culture, Immunolabeling, Transfection, Binding Assay, Staining

    Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.
    Figure Legend Snippet: Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.

    Techniques Used: Staining, Isolation, Blue Native PAGE, Western Blot

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    Alomone Labs rabbit anti bk
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    <t>BK</t> <t>Ca</t> <t>-β1</t> expression is reduced in the carotid arteries of rat balloon-injured model. Representative images of H&E (A) and immunohistochemical staining of BK Ca −α and BK ca −β1 (B) in injured and sham-operated carotid arteries of rat balloon-injured model at 14 days post injury. Scale bar = 100 μm. (C) Quantified mRNA levels of BK ca −α and BK ca −β1 analyzed by qRT-PCR. Western blot images (D) and quantification (E) for indicated proteins. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 4∼6 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. sham).
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    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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    A . Representative Western Blots of <t>BK</t> <t>α</t> 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.
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    Alomone Labs bk ca channel β subunit 4
    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The <t>BK</t> <t>Ca</t> subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .
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    Alomone Labs rabbit polyclonal anti bk ca channel β subunit 4 antibody
    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The <t>BK</t> <t>Ca</t> subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .
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    Image Search Results


    BK Ca -β1 expression is reduced in the carotid arteries of rat balloon-injured model. Representative images of H&E (A) and immunohistochemical staining of BK Ca −α and BK ca −β1 (B) in injured and sham-operated carotid arteries of rat balloon-injured model at 14 days post injury. Scale bar = 100 μm. (C) Quantified mRNA levels of BK ca −α and BK ca −β1 analyzed by qRT-PCR. Western blot images (D) and quantification (E) for indicated proteins. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 4∼6 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. sham).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    doi: 10.3389/fcvm.2022.1062695

    Figure Lengend Snippet: BK Ca -β1 expression is reduced in the carotid arteries of rat balloon-injured model. Representative images of H&E (A) and immunohistochemical staining of BK Ca −α and BK ca −β1 (B) in injured and sham-operated carotid arteries of rat balloon-injured model at 14 days post injury. Scale bar = 100 μm. (C) Quantified mRNA levels of BK ca −α and BK ca −β1 analyzed by qRT-PCR. Western blot images (D) and quantification (E) for indicated proteins. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 4∼6 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. sham).

    Article Snippet: An antibody against BK Ca -β1 (APC-036) used for immunohistochemical staining and western blot was purchased from Alomone labs (Jerusalem, Israel).

    Techniques: Expressing, Immunohistochemical staining, Staining, Quantitative RT-PCR, Western Blot

    BK Ca -β1 expression is positively associated with VSMC differentiation markers in vitro . Western blot images (A) and quantification (B) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs of passage 1 and passage 6. Western blot images (C) and quantification (D) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (E) and quantification (F) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3-5 of VSMCs were used in (C) through (F) . Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 5 for each group, ns, not significant, * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    doi: 10.3389/fcvm.2022.1062695

    Figure Lengend Snippet: BK Ca -β1 expression is positively associated with VSMC differentiation markers in vitro . Western blot images (A) and quantification (B) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs of passage 1 and passage 6. Western blot images (C) and quantification (D) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (E) and quantification (F) of BK ca −α, BK ca −β1, and VSMC differentiation markers expression in VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3-5 of VSMCs were used in (C) through (F) . Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM ( n = 5 for each group, ns, not significant, * P < 0.05, ** P < 0.01, and *** P < 0.001 vs. control).

    Article Snippet: An antibody against BK Ca -β1 (APC-036) used for immunohistochemical staining and western blot was purchased from Alomone labs (Jerusalem, Israel).

    Techniques: Expressing, In Vitro, Western Blot

    Decreased BK ca −β1 expression is mediated by elevated PDGF-BB in vivo . (A) Quantified mRNA levels of PDGF-B and TGF-β analyzed by qRT-PCR in injured and sham-operated carotid arteries. Western blot images (B) and quantification (C) of BK ca −α and BK ca −β1 in the carotid arteries of mice injected with saline or PDGF-BB via tail vein. Data are presented as means ± SEM ( n = 6 for each group, ns, not significant, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. control).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    doi: 10.3389/fcvm.2022.1062695

    Figure Lengend Snippet: Decreased BK ca −β1 expression is mediated by elevated PDGF-BB in vivo . (A) Quantified mRNA levels of PDGF-B and TGF-β analyzed by qRT-PCR in injured and sham-operated carotid arteries. Western blot images (B) and quantification (C) of BK ca −α and BK ca −β1 in the carotid arteries of mice injected with saline or PDGF-BB via tail vein. Data are presented as means ± SEM ( n = 6 for each group, ns, not significant, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. control).

    Article Snippet: An antibody against BK Ca -β1 (APC-036) used for immunohistochemical staining and western blot was purchased from Alomone labs (Jerusalem, Israel).

    Techniques: Expressing, In Vivo, Quantitative RT-PCR, Western Blot, Injection

    BK Ca -β1 is essential for VSMCs to maintain a differentiated phenotype. (A) Representative micrographs of VSMCs treated with BK ca −β1 siRNA or scramble siRNA transfection. (B) Representative immunofluorescent images of F-actin of VSMCs stained with phalloidin (red). Nuclei were stained with DAPI (blue). Scale bar = 25 μm. (C) The percentage of spindle-like or polygonal-like cells in each group. Western blot images (D) and quantification (E) of BK ca −β1, α-SMA, and SM22α. Representative images (F) and quantification (G) of the areas of collagen gel in each group. The size of the collagen gel in each well was calculated compared to the total area of the well. Data are presented as means ± SEM ( n = 5∼6 for each group, *** P < 0.001 vs. scramble).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    doi: 10.3389/fcvm.2022.1062695

    Figure Lengend Snippet: BK Ca -β1 is essential for VSMCs to maintain a differentiated phenotype. (A) Representative micrographs of VSMCs treated with BK ca −β1 siRNA or scramble siRNA transfection. (B) Representative immunofluorescent images of F-actin of VSMCs stained with phalloidin (red). Nuclei were stained with DAPI (blue). Scale bar = 25 μm. (C) The percentage of spindle-like or polygonal-like cells in each group. Western blot images (D) and quantification (E) of BK ca −β1, α-SMA, and SM22α. Representative images (F) and quantification (G) of the areas of collagen gel in each group. The size of the collagen gel in each well was calculated compared to the total area of the well. Data are presented as means ± SEM ( n = 5∼6 for each group, *** P < 0.001 vs. scramble).

    Article Snippet: An antibody against BK Ca -β1 (APC-036) used for immunohistochemical staining and western blot was purchased from Alomone labs (Jerusalem, Israel).

    Techniques: Transfection, Staining, Western Blot

    BK Ca -β1 knockdown induces proliferative, migratory, and synthetic phenotype of VSMCs. (A) Proliferation curves of VSMCs transfected with BK ca −β1 or scrambled siRNA. Representative images (B) and quantification (C) of migration assay. (D) Quantified mRNA levels of inflammatory factors analyzed by qRT-PCR. Representative images (E) and quantification (F) of activities of MMP-9 and MMP-2 tested using gelatin zymography. Data are presented as means ± SEM ( n = 5∼6 for each group, * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. scramble).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    doi: 10.3389/fcvm.2022.1062695

    Figure Lengend Snippet: BK Ca -β1 knockdown induces proliferative, migratory, and synthetic phenotype of VSMCs. (A) Proliferation curves of VSMCs transfected with BK ca −β1 or scrambled siRNA. Representative images (B) and quantification (C) of migration assay. (D) Quantified mRNA levels of inflammatory factors analyzed by qRT-PCR. Representative images (E) and quantification (F) of activities of MMP-9 and MMP-2 tested using gelatin zymography. Data are presented as means ± SEM ( n = 5∼6 for each group, * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001 vs. scramble).

    Article Snippet: An antibody against BK Ca -β1 (APC-036) used for immunohistochemical staining and western blot was purchased from Alomone labs (Jerusalem, Israel).

    Techniques: Transfection, Migration, Quantitative RT-PCR, Zymography

    Decreased BK ca −β1 expression is correlated with VSMC dedifferentiation and atherosclerosis in human. Western blot images (A) and quantification (B) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (C) and quantification (D) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3–5 of VSMCs were used. (E) Representative western blot images of the protein levels of BK ca −α and BK ca −β1 in lysates of human carotid endarterectomy artery (CEA) and control internal mammary arteries (IMA). (F) Quantification was performed by calculating the ratio between the levels of BK ca −β1 and BK ca −α. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM (n = 3∼5 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. control).

    Journal: Frontiers in Cardiovascular Medicine

    Article Title: Large-conductance Ca 2 + -activated K + channel β1-subunit maintains the contractile phenotype of vascular smooth muscle cells

    doi: 10.3389/fcvm.2022.1062695

    Figure Lengend Snippet: Decreased BK ca −β1 expression is correlated with VSMC dedifferentiation and atherosclerosis in human. Western blot images (A) and quantification (B) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs after PDGF-BB treatment (25 μg/L). Western blot images (C) and quantification (D) of BK ca −α and BK ca −β1 expression in human primary aortic VSMCs treated with TGF-β (2.5 μg/L). VSMCs were subjected to serum-starvation for 24 h and then treated with the indicated stimulation for 48 h. Passages 3–5 of VSMCs were used. (E) Representative western blot images of the protein levels of BK ca −α and BK ca −β1 in lysates of human carotid endarterectomy artery (CEA) and control internal mammary arteries (IMA). (F) Quantification was performed by calculating the ratio between the levels of BK ca −β1 and BK ca −α. Eukaryotic initiation factor 5 (eIF5) was used as an internal control. Data are presented as means ± SEM (n = 3∼5 for each group, ns, not significant, * P < 0.05, ** P < 0.01 vs. control).

    Article Snippet: An antibody against BK Ca -β1 (APC-036) used for immunohistochemical staining and western blot was purchased from Alomone labs (Jerusalem, Israel).

    Techniques: Expressing, Western Blot

    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

    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

    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .

    Journal: PLoS ONE

    Article Title: Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain

    doi: 10.1371/journal.pone.0068125

    Figure Lengend Snippet: A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .

    Article Snippet: The membranes were exposed to polyclonal antibodies that recognize BK Ca channel β subunit 4 (anti-β4, 1∶200, Alomone Labs) and cytochrome c oxidase subunit IV (COX IV, 1∶1000, Cell Signaling).

    Techniques: Positive Control, Negative Control, Western Blot, Labeling, Marker, Electron Microscopy, Cell Culture, Immunolabeling, Transfection, Binding Assay, Staining

    Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.

    Journal: PLoS ONE

    Article Title: Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain

    doi: 10.1371/journal.pone.0068125

    Figure Lengend Snippet: Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.

    Article Snippet: The membranes were exposed to polyclonal antibodies that recognize BK Ca channel β subunit 4 (anti-β4, 1∶200, Alomone Labs) and cytochrome c oxidase subunit IV (COX IV, 1∶1000, Cell Signaling).

    Techniques: Staining, Isolation, Blue Native PAGE, Western Blot

    A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .

    Journal: PLoS ONE

    Article Title: Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain

    doi: 10.1371/journal.pone.0068125

    Figure Lengend Snippet: A. Detection of mitoBK Ca channel regulatory β4 subunit mRNA in astrocytoma cells. The BK Ca subunit β4 mRNA was detected at a size of 405 bp. No products were obtained for the BK Ca subunits β1, β2 and β3. GAPDH served as a positive control and was detected at a size of 496 bp. The negative control without reverse transcriptase (−RT) and samples without cDNA (−A) had no signals. The results presented are representative of seven independent experiments. B. Immunoblot of astrocytoma mitochondria, astrocytoma cell homogenate and brain homogenate fractions labeled with the anti-BK Ca channel β4 subunit antibody. A control antigen (BK Ca β4+ peptide) was used as a positive control for the specificity of the antibody. An anti-cytochrome c oxidase subunit IV antibody (COX IV) was used as a mitochondrial marker (n = 3). C. Immuno-gold electron microscopy localization of the BK Ca channel β4 regulatory subunit in mitochondria of cultured human astrocytoma cells. The β4 subunit molecules were labeled using 10 nm colloidal-gold particles (arrows). D. High-power confocal image of cultured astrocytoma cells immunolabeled to detect OxPhos (red) and β4-GFP-transfected cells (green). The superimposition of the two signals revealed the mitochondrial localization of BK Ca β4 in human astrocytoma cells (yellow). The DNA-binding dye DAPI was used to stain the cell nuclei (blue). For details concerning the astrocytoma cells, see the .

    Article Snippet: The immunoreactions consisted of sequential incubations with a rabbit polyclonal anti-BK Ca channel β subunit 4 antibody (anti-β4, 1∶20, Alomone Labs) followed by species-specific donkey secondary antibodies coupled to 10 nm gold particles (Electron Microscopy Sciences).

    Techniques: Positive Control, Negative Control, Western Blot, Labeling, Marker, Electron Microscopy, Cell Culture, Immunolabeling, Transfection, Binding Assay, Staining

    Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.

    Journal: PLoS ONE

    Article Title: Putative Structural and Functional Coupling of the Mitochondrial BK Ca Channel to the Respiratory Chain

    doi: 10.1371/journal.pone.0068125

    Figure Lengend Snippet: Two-dimensional separation was performed as described in the , and the PVDF membrane was first immunoblotted for the BK Ca channel β4 subunit (below, Coomassie staining panel). Next, the PVDF membrane was immunoblotted for the subunits of individual respiratory chain complexes (below the BK Ca β4 panel). The BN-PAGE was calibrated based on the location of mitochondrial respiratory chain complexes that were isolated from rat heart mitochondria (above the panel for the blue native PAGE of mitochondria from astrocytoma cells). In the native astrocytoma lysate, mitochondria BK Ca β4 co-localized with subunit I of cytochrome c oxidase. M, the monomeric form of cytochrome c oxidase; D, the dimeric form of cytochrome c oxidase; Sc 1 and Sc 2 , complexes with higher molecular weights containing cytochrome c oxidase. A typical immunoblot from three separate experiments is shown.

    Article Snippet: The immunoreactions consisted of sequential incubations with a rabbit polyclonal anti-BK Ca channel β subunit 4 antibody (anti-β4, 1∶20, Alomone Labs) followed by species-specific donkey secondary antibodies coupled to 10 nm gold particles (Electron Microscopy Sciences).

    Techniques: Staining, Isolation, Blue Native PAGE, Western Blot