bkα  (Alomone Labs)


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    Structured Review

    Alomone Labs bkα
    Depolymerization of microtubules decreases the number of <t>BKα</t> and RyR2 colocalization sites. ( A ) Wide-field image of a freshly isolated arterial myocyte immunolabeled for BKα ( n = 12 cells, n = 3 animals). Red box indicates the area where superresolution images were obtained. Scale bar, 10 μm. ( B ) Superresolution localization map obtained after immunolabeling with anti-BKμ (green) and anti-RyR2 (red) antibodies ( n = 12 cells, n = 3 animals). Scale bar, 3 μm. ROIs (yellow boxes) are shown in magnified view (I) and (II) below. Scale bars, 0.2 μm. ( C ) Cluster size distribution histograms of RyR2 and BKα ( n = 11,005 or n = 11,940 particles for RyR2 and BKα, respectively; 12 cells, n = 3 animals). ( D ) Summary of object-based analysis to determine the number of BKα protein cluster centroids per cell that overlay with RyR2 protein clusters in control cells, cells in which a random BKα distribution has been simulated, and cells treated with nocodazole (10 μM). * P ≤ 0.05 compared to control ( n =12 cells per group, 3 animals). Coloc., colocalization.
    Bkα, 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
    https://www.bioz.com/result/bkα/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bkα - by Bioz Stars, 2022-07
    95/100 stars

    Images

    1) Product Images from "Microtubule structures underlying the sarcoplasmic reticulum support peripheral coupling sites to regulate smooth muscle contractility"

    Article Title: Microtubule structures underlying the sarcoplasmic reticulum support peripheral coupling sites to regulate smooth muscle contractility

    Journal: Science signaling

    doi: 10.1126/scisignal.aan2694

    Depolymerization of microtubules decreases the number of BKα and RyR2 colocalization sites. ( A ) Wide-field image of a freshly isolated arterial myocyte immunolabeled for BKα ( n = 12 cells, n = 3 animals). Red box indicates the area where superresolution images were obtained. Scale bar, 10 μm. ( B ) Superresolution localization map obtained after immunolabeling with anti-BKμ (green) and anti-RyR2 (red) antibodies ( n = 12 cells, n = 3 animals). Scale bar, 3 μm. ROIs (yellow boxes) are shown in magnified view (I) and (II) below. Scale bars, 0.2 μm. ( C ) Cluster size distribution histograms of RyR2 and BKα ( n = 11,005 or n = 11,940 particles for RyR2 and BKα, respectively; 12 cells, n = 3 animals). ( D ) Summary of object-based analysis to determine the number of BKα protein cluster centroids per cell that overlay with RyR2 protein clusters in control cells, cells in which a random BKα distribution has been simulated, and cells treated with nocodazole (10 μM). * P ≤ 0.05 compared to control ( n =12 cells per group, 3 animals). Coloc., colocalization.
    Figure Legend Snippet: Depolymerization of microtubules decreases the number of BKα and RyR2 colocalization sites. ( A ) Wide-field image of a freshly isolated arterial myocyte immunolabeled for BKα ( n = 12 cells, n = 3 animals). Red box indicates the area where superresolution images were obtained. Scale bar, 10 μm. ( B ) Superresolution localization map obtained after immunolabeling with anti-BKμ (green) and anti-RyR2 (red) antibodies ( n = 12 cells, n = 3 animals). Scale bar, 3 μm. ROIs (yellow boxes) are shown in magnified view (I) and (II) below. Scale bars, 0.2 μm. ( C ) Cluster size distribution histograms of RyR2 and BKα ( n = 11,005 or n = 11,940 particles for RyR2 and BKα, respectively; 12 cells, n = 3 animals). ( D ) Summary of object-based analysis to determine the number of BKα protein cluster centroids per cell that overlay with RyR2 protein clusters in control cells, cells in which a random BKα distribution has been simulated, and cells treated with nocodazole (10 μM). * P ≤ 0.05 compared to control ( n =12 cells per group, 3 animals). Coloc., colocalization.

    Techniques Used: Isolation, Immunolabeling

    2) Product Images from "G9a Is Essential for Epigenetic Silencing of K+ Channel Genes in Acute-to-Chronic Pain Transition"

    Article Title: G9a Is Essential for Epigenetic Silencing of K+ Channel Genes in Acute-to-Chronic Pain Transition

    Journal: Nature neuroscience

    doi: 10.1038/nn.4165

    Inhibition of G9a activity normalizes K + channel gene expression in the DRG diminished by nerve injury ( a-d) Effects of intrathecal treatments with vehicle (n = 10), SAHA (50 μg, n = 9), UNC0638 (10 μg, n = 8), GSK503 (5 μg, n = 10), SAHA plus GSK503 (n = 8), SAHA plus UNC0638 (n = 9) or UNC0638 plus GSK503 (n = 8) on the mRNA levels of Kcna4 ( a ), Kcnd2 ( b ), Kcnq2 ( c ), and Kcnma1 ( d ) in the DRG obtained from SNL rats 28 days after surgery. Data from sham control rats were plotted as the control (n = 6 rats). ( e,f ) Effects of nerve injury and UNC0638 on the protein levels of Kv1.4, Kv4.2, Kv7.2 and BKα1 in the L5 and L6 DRG (n = 6 rats in each group). ( g,h ) Effect of G9a-specific siRNA on the G9a and H3K9me2 protein levels in the DRG obtained from SNL rats 24 h after the last injection (n = 5 in each group). ( i,j ) Effects of G9a-specific siRNA on the mRNA levels of G9a, Ezh2, Kcna4, Kcnd2, Kcnq2 and Kcnma1 in the DRG obtained from SNL ( i ) and sham control ( j ) rats 24 h after the last injection (n = 10 in each group). Data are presented as mean ± s.e.m. Statistical analysis was performed using two-way ANOVA followed by Bonferroni’s post hoc tests ( a-d ), one-way ANOVA ( f,h,i ), or Mann-Whitney test ( j ). * P
    Figure Legend Snippet: Inhibition of G9a activity normalizes K + channel gene expression in the DRG diminished by nerve injury ( a-d) Effects of intrathecal treatments with vehicle (n = 10), SAHA (50 μg, n = 9), UNC0638 (10 μg, n = 8), GSK503 (5 μg, n = 10), SAHA plus GSK503 (n = 8), SAHA plus UNC0638 (n = 9) or UNC0638 plus GSK503 (n = 8) on the mRNA levels of Kcna4 ( a ), Kcnd2 ( b ), Kcnq2 ( c ), and Kcnma1 ( d ) in the DRG obtained from SNL rats 28 days after surgery. Data from sham control rats were plotted as the control (n = 6 rats). ( e,f ) Effects of nerve injury and UNC0638 on the protein levels of Kv1.4, Kv4.2, Kv7.2 and BKα1 in the L5 and L6 DRG (n = 6 rats in each group). ( g,h ) Effect of G9a-specific siRNA on the G9a and H3K9me2 protein levels in the DRG obtained from SNL rats 24 h after the last injection (n = 5 in each group). ( i,j ) Effects of G9a-specific siRNA on the mRNA levels of G9a, Ezh2, Kcna4, Kcnd2, Kcnq2 and Kcnma1 in the DRG obtained from SNL ( i ) and sham control ( j ) rats 24 h after the last injection (n = 10 in each group). Data are presented as mean ± s.e.m. Statistical analysis was performed using two-way ANOVA followed by Bonferroni’s post hoc tests ( a-d ), one-way ANOVA ( f,h,i ), or Mann-Whitney test ( j ). * P

    Techniques Used: Inhibition, Activity Assay, Expressing, Injection, MANN-WHITNEY

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    Alomone Labs mouse anti bk channel α
    Membrane current in  HEK  293 cells stably expressing human  BK  channel α‐ and β1‐subunits.  (A)  Voltage‐dependent  BK  current traces recorded in a representative cell with the voltage protocol as shown in the  inset  before and after application of 1 μM paxilline (a selective  BK  channel blocker), and washout of paxilline.  (B)  I‐V  relationships of  BK  current in the absence and presence of 1 μM paxilline, and upon washout ( n  = 5, * P 
    Mouse Anti Bk Channel α, 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
    https://www.bioz.com/result/mouse anti bk channel α/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti bk channel α - by Bioz Stars, 2022-07
    95/100 stars
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    Membrane current in  HEK  293 cells stably expressing human  BK  channel α‐ and β1‐subunits.  (A)  Voltage‐dependent  BK  current traces recorded in a representative cell with the voltage protocol as shown in the  inset  before and after application of 1 μM paxilline (a selective  BK  channel blocker), and washout of paxilline.  (B)  I‐V  relationships of  BK  current in the absence and presence of 1 μM paxilline, and upon washout ( n  = 5, * P 

    Journal: Journal of Cellular and Molecular Medicine

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

    doi: 10.1111/jcmm.13103

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

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

    Techniques: Stable Transfection, Expressing

    Depolymerization of microtubules decreases the number of BKα and RyR2 colocalization sites. ( A ) Wide-field image of a freshly isolated arterial myocyte immunolabeled for BKα ( n = 12 cells, n = 3 animals). Red box indicates the area where superresolution images were obtained. Scale bar, 10 μm. ( B ) Superresolution localization map obtained after immunolabeling with anti-BKμ (green) and anti-RyR2 (red) antibodies ( n = 12 cells, n = 3 animals). Scale bar, 3 μm. ROIs (yellow boxes) are shown in magnified view (I) and (II) below. Scale bars, 0.2 μm. ( C ) Cluster size distribution histograms of RyR2 and BKα ( n = 11,005 or n = 11,940 particles for RyR2 and BKα, respectively; 12 cells, n = 3 animals). ( D ) Summary of object-based analysis to determine the number of BKα protein cluster centroids per cell that overlay with RyR2 protein clusters in control cells, cells in which a random BKα distribution has been simulated, and cells treated with nocodazole (10 μM). * P ≤ 0.05 compared to control ( n =12 cells per group, 3 animals). Coloc., colocalization.

    Journal: Science signaling

    Article Title: Microtubule structures underlying the sarcoplasmic reticulum support peripheral coupling sites to regulate smooth muscle contractility

    doi: 10.1126/scisignal.aan2694

    Figure Lengend Snippet: Depolymerization of microtubules decreases the number of BKα and RyR2 colocalization sites. ( A ) Wide-field image of a freshly isolated arterial myocyte immunolabeled for BKα ( n = 12 cells, n = 3 animals). Red box indicates the area where superresolution images were obtained. Scale bar, 10 μm. ( B ) Superresolution localization map obtained after immunolabeling with anti-BKμ (green) and anti-RyR2 (red) antibodies ( n = 12 cells, n = 3 animals). Scale bar, 3 μm. ROIs (yellow boxes) are shown in magnified view (I) and (II) below. Scale bars, 0.2 μm. ( C ) Cluster size distribution histograms of RyR2 and BKα ( n = 11,005 or n = 11,940 particles for RyR2 and BKα, respectively; 12 cells, n = 3 animals). ( D ) Summary of object-based analysis to determine the number of BKα protein cluster centroids per cell that overlay with RyR2 protein clusters in control cells, cells in which a random BKα distribution has been simulated, and cells treated with nocodazole (10 μM). * P ≤ 0.05 compared to control ( n =12 cells per group, 3 animals). Coloc., colocalization.

    Article Snippet: Cells were fixed with 3.2% formaldehyde/0.1% glutaraldehyde–phosphate-buffered saline (PBS), permeabilized and blocked with 0.2% saponin/5% horse serum–PBS, and incubated with primary antibodies against α-tubulin (1:100; MA1-80017, Life Technologies), BKα (1:100; APC-021, Alomone Labs), and RyR2 (1:100; ab2868, Abcam).

    Techniques: Isolation, Immunolabeling

    Changes in the mGluR5 protein levels in the DRG and dorsal spinal cord in control and diabetic rats. A, representative gel images show the density of mGluR5 protein band in the dorsal spinal cord and DRG. Note that β-actin was used as a loading control. B, summary data show the difference in the mGluR5 protein level in the dorsal spinal cord and DRG. Data are presented as means ± SEM. *P

    Journal: Journal of neurochemistry

    Article Title: Regulation of Increased Glutamatergic Input to Spinal Dorsal Horn Neurons by mGluR5 in Diabetic Neuropathic Pain

    doi: 10.1111/j.1471-4159.2009.06437.x

    Figure Lengend Snippet: Changes in the mGluR5 protein levels in the DRG and dorsal spinal cord in control and diabetic rats. A, representative gel images show the density of mGluR5 protein band in the dorsal spinal cord and DRG. Note that β-actin was used as a loading control. B, summary data show the difference in the mGluR5 protein level in the dorsal spinal cord and DRG. Data are presented as means ± SEM. *P

    Article Snippet: The membrane was blocked for 2 h in 5% nonfat milk in phosphate-buffered saline and then incubated with rabbit anti-mGluR5 primary antibody (APC-021, Alomone Labs, Jerusalem, Israel; dilution: 1:1000) overnight at 4°C.

    Techniques:

    Inhibition of G9a activity normalizes K + channel gene expression in the DRG diminished by nerve injury ( a-d) Effects of intrathecal treatments with vehicle (n = 10), SAHA (50 μg, n = 9), UNC0638 (10 μg, n = 8), GSK503 (5 μg, n = 10), SAHA plus GSK503 (n = 8), SAHA plus UNC0638 (n = 9) or UNC0638 plus GSK503 (n = 8) on the mRNA levels of Kcna4 ( a ), Kcnd2 ( b ), Kcnq2 ( c ), and Kcnma1 ( d ) in the DRG obtained from SNL rats 28 days after surgery. Data from sham control rats were plotted as the control (n = 6 rats). ( e,f ) Effects of nerve injury and UNC0638 on the protein levels of Kv1.4, Kv4.2, Kv7.2 and BKα1 in the L5 and L6 DRG (n = 6 rats in each group). ( g,h ) Effect of G9a-specific siRNA on the G9a and H3K9me2 protein levels in the DRG obtained from SNL rats 24 h after the last injection (n = 5 in each group). ( i,j ) Effects of G9a-specific siRNA on the mRNA levels of G9a, Ezh2, Kcna4, Kcnd2, Kcnq2 and Kcnma1 in the DRG obtained from SNL ( i ) and sham control ( j ) rats 24 h after the last injection (n = 10 in each group). Data are presented as mean ± s.e.m. Statistical analysis was performed using two-way ANOVA followed by Bonferroni’s post hoc tests ( a-d ), one-way ANOVA ( f,h,i ), or Mann-Whitney test ( j ). * P

    Journal: Nature neuroscience

    Article Title: G9a Is Essential for Epigenetic Silencing of K+ Channel Genes in Acute-to-Chronic Pain Transition

    doi: 10.1038/nn.4165

    Figure Lengend Snippet: Inhibition of G9a activity normalizes K + channel gene expression in the DRG diminished by nerve injury ( a-d) Effects of intrathecal treatments with vehicle (n = 10), SAHA (50 μg, n = 9), UNC0638 (10 μg, n = 8), GSK503 (5 μg, n = 10), SAHA plus GSK503 (n = 8), SAHA plus UNC0638 (n = 9) or UNC0638 plus GSK503 (n = 8) on the mRNA levels of Kcna4 ( a ), Kcnd2 ( b ), Kcnq2 ( c ), and Kcnma1 ( d ) in the DRG obtained from SNL rats 28 days after surgery. Data from sham control rats were plotted as the control (n = 6 rats). ( e,f ) Effects of nerve injury and UNC0638 on the protein levels of Kv1.4, Kv4.2, Kv7.2 and BKα1 in the L5 and L6 DRG (n = 6 rats in each group). ( g,h ) Effect of G9a-specific siRNA on the G9a and H3K9me2 protein levels in the DRG obtained from SNL rats 24 h after the last injection (n = 5 in each group). ( i,j ) Effects of G9a-specific siRNA on the mRNA levels of G9a, Ezh2, Kcna4, Kcnd2, Kcnq2 and Kcnma1 in the DRG obtained from SNL ( i ) and sham control ( j ) rats 24 h after the last injection (n = 10 in each group). Data are presented as mean ± s.e.m. Statistical analysis was performed using two-way ANOVA followed by Bonferroni’s post hoc tests ( a-d ), one-way ANOVA ( f,h,i ), or Mann-Whitney test ( j ). * P

    Article Snippet: The membranes were treated with 5% bovine serum albumin in Tris buffer containing Tween 20 (TNT) for 2 h and then incubated with one of the following primary antibodies overnight at 4°C: Kv1.4 (catalog #05-409, Upstate Biotechnology), Kv4.2 (catalog #APC-023, Alomone Labs), Kv7.2 (catalog #APC-050, Alomone Labs), BKα1 (catalog #APC-021, Alomone Labs), acetyl-H3 (catalog #06-599, Millipore), H3K9ac (catalog #39917, Active Motif), H3K27me3 (catalog #9733, Cell Signaling Technology), histone H3 (catalog #9715, Cell Signaling Technology), H3K9me2 (catalog #ab1220, Abcam), G9a (catalog #09-071, Millipore), HDAC1 (catalog #IMG-337, Imgenex), and HDAC2, HDAC4, HDAC5 and EZH2 (catalog #2540, #2072, #2082 and #5246, respectively; Cell Signaling Technology).

    Techniques: Inhibition, Activity Assay, Expressing, Injection, MANN-WHITNEY