kcnq3  (Alomone Labs)


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    Structured Review

    Alomone Labs kcnq3
    Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and <t>KCNQ2/KCNQ3</t> potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P
    Kcnq3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G"

    Article Title: Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200805169

    Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P
    Figure Legend Snippet: Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P

    Techniques Used: Construct, Cell Culture, Expressing, Mutagenesis, Transfection, Staining, Fluorescence, MANN-WHITNEY

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    Alomone Labs anti kv7 3
    Kv7.2 and 7.3 protein and mRNA expression levels were decreased in the CeA in SHRs. ( A – D ) Original gel images and quantification of band density show the total protein levels of Kv7.2 and <t>Kv7.3</t> in the CeA ( A ), PVN ( B ), HP ( C ), and PFC ( D ) from WKY rats and SHRs ( n =6 samples in each group). In these protein assays, each sample consisting of respective tissues from one rat. ( E – G ) Summary of quantitative RT–PCR data show mRNA levels of Kv7.2 and Kv7.3 in the CeA ( E ), PVN ( F ), and HP ( G ) from WKY rats and SHRs ( n =5 samples in each group). Data are presented as the mean ± SEM. * P
    Anti Kv7 3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Alomone Labs mouse anti kca3 1
    Role of TRPV4 and <t>KCa3.1</t> in alteration of membrane potential and Ca 2+ entry in astrocytes following OGD. a–f Changes in membrane potential in response to activation of KCa3.1 channels and TRPV4 channels in astrocytes exposed to OGD 1 h. a , b 1-EBIO was added to WT astrocytes and membrane potential measured with or without OGD or HC 067047. Data are presented as means ± SEM. n = 10–20. *** p
    Mouse Anti Kca3 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Kv7.2 and 7.3 protein and mRNA expression levels were decreased in the CeA in SHRs. ( A – D ) Original gel images and quantification of band density show the total protein levels of Kv7.2 and Kv7.3 in the CeA ( A ), PVN ( B ), HP ( C ), and PFC ( D ) from WKY rats and SHRs ( n =6 samples in each group). In these protein assays, each sample consisting of respective tissues from one rat. ( E – G ) Summary of quantitative RT–PCR data show mRNA levels of Kv7.2 and Kv7.3 in the CeA ( E ), PVN ( F ), and HP ( G ) from WKY rats and SHRs ( n =5 samples in each group). Data are presented as the mean ± SEM. * P

    Journal: Cardiovascular Research

    Article Title: Impaired Kv7 channel activity in the central amygdala contributes to elevated sympathetic outflow in hypertension

    doi: 10.1093/cvr/cvab031

    Figure Lengend Snippet: Kv7.2 and 7.3 protein and mRNA expression levels were decreased in the CeA in SHRs. ( A – D ) Original gel images and quantification of band density show the total protein levels of Kv7.2 and Kv7.3 in the CeA ( A ), PVN ( B ), HP ( C ), and PFC ( D ) from WKY rats and SHRs ( n =6 samples in each group). In these protein assays, each sample consisting of respective tissues from one rat. ( E – G ) Summary of quantitative RT–PCR data show mRNA levels of Kv7.2 and Kv7.3 in the CeA ( E ), PVN ( F ), and HP ( G ) from WKY rats and SHRs ( n =5 samples in each group). Data are presented as the mean ± SEM. * P

    Article Snippet: Immunohistochemical staining was performed to determine the spatial distribution of Kv7 channels in the CeA–RVLM neurons by using anti-Kv7.3 (Alomone Labs) antibody.

    Techniques: Expressing, Quantitative RT-PCR

    Reduced expression of Kv7.2/Kv7.3 in the CeA was independent of high blood pressure in SHRs. ( A and B ) Western blot images and quantification of band density show the total protein levels of Kv7.2 ( A ) and Kv7.3 ( B ) (normalized to β-actin) in the CeA in 4, 7, and 13 weeks old WKY rats and SHRs ( n =4 rats in each group). ( C ) Summary data show mean ABP measured by telemetry approach in SHRs subjected to the CGx and sham surgery ( n =6 rats in each group). (D–F) Western blot images and quantification of band density show the total protein levels of Kv7.2 and Kv7.3 (normalized to β-actin) in the CeA ( D ), the PVN ( E ), and HP ( F ) in SHRs subjected to CGx or sham surgery ( n =6 rats in each group). Data are presented as the mean±SEM. * P

    Journal: Cardiovascular Research

    Article Title: Impaired Kv7 channel activity in the central amygdala contributes to elevated sympathetic outflow in hypertension

    doi: 10.1093/cvr/cvab031

    Figure Lengend Snippet: Reduced expression of Kv7.2/Kv7.3 in the CeA was independent of high blood pressure in SHRs. ( A and B ) Western blot images and quantification of band density show the total protein levels of Kv7.2 ( A ) and Kv7.3 ( B ) (normalized to β-actin) in the CeA in 4, 7, and 13 weeks old WKY rats and SHRs ( n =4 rats in each group). ( C ) Summary data show mean ABP measured by telemetry approach in SHRs subjected to the CGx and sham surgery ( n =6 rats in each group). (D–F) Western blot images and quantification of band density show the total protein levels of Kv7.2 and Kv7.3 (normalized to β-actin) in the CeA ( D ), the PVN ( E ), and HP ( F ) in SHRs subjected to CGx or sham surgery ( n =6 rats in each group). Data are presented as the mean±SEM. * P

    Article Snippet: Immunohistochemical staining was performed to determine the spatial distribution of Kv7 channels in the CeA–RVLM neurons by using anti-Kv7.3 (Alomone Labs) antibody.

    Techniques: Expressing, Western Blot

    M-currents were decreased in CeA–RVLM neurons in SHRs. ( A ) Images show retrograde tracer injection sites in the RVLM viewed by light (a) and fluorescent (b) microscope and Fluosphere labelled neurons in the CeA viewed by light (c and e) and fluorescent (d and f) microscope. ( B ) Immunostaining images show that Kv7.3 immunoreactivities were expressed on DiI-labelled CeA neurons. ( C and D ) Original recordings ( C ) and summary data ( D ) show the basal and QO-58-induced M-currents, which were defined as XE-991-sensitive tail currents in basal and the presence of QO-58, were significantly diminished in retrogradely labelled CeA–RVLM neurons in SHRs ( n =10 neurons in 4 rats) compared with WKY rats ( n =9 neurons in 4 rats).*** P

    Journal: Cardiovascular Research

    Article Title: Impaired Kv7 channel activity in the central amygdala contributes to elevated sympathetic outflow in hypertension

    doi: 10.1093/cvr/cvab031

    Figure Lengend Snippet: M-currents were decreased in CeA–RVLM neurons in SHRs. ( A ) Images show retrograde tracer injection sites in the RVLM viewed by light (a) and fluorescent (b) microscope and Fluosphere labelled neurons in the CeA viewed by light (c and e) and fluorescent (d and f) microscope. ( B ) Immunostaining images show that Kv7.3 immunoreactivities were expressed on DiI-labelled CeA neurons. ( C and D ) Original recordings ( C ) and summary data ( D ) show the basal and QO-58-induced M-currents, which were defined as XE-991-sensitive tail currents in basal and the presence of QO-58, were significantly diminished in retrogradely labelled CeA–RVLM neurons in SHRs ( n =10 neurons in 4 rats) compared with WKY rats ( n =9 neurons in 4 rats).*** P

    Article Snippet: Immunohistochemical staining was performed to determine the spatial distribution of Kv7 channels in the CeA–RVLM neurons by using anti-Kv7.3 (Alomone Labs) antibody.

    Techniques: Injection, Microscopy, Immunostaining

    Role of TRPV4 and KCa3.1 in alteration of membrane potential and Ca 2+ entry in astrocytes following OGD. a–f Changes in membrane potential in response to activation of KCa3.1 channels and TRPV4 channels in astrocytes exposed to OGD 1 h. a , b 1-EBIO was added to WT astrocytes and membrane potential measured with or without OGD or HC 067047. Data are presented as means ± SEM. n = 10–20. *** p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: Role of TRPV4 and KCa3.1 in alteration of membrane potential and Ca 2+ entry in astrocytes following OGD. a–f Changes in membrane potential in response to activation of KCa3.1 channels and TRPV4 channels in astrocytes exposed to OGD 1 h. a , b 1-EBIO was added to WT astrocytes and membrane potential measured with or without OGD or HC 067047. Data are presented as means ± SEM. n = 10–20. *** p

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Activation Assay

    KCa3.1 and TRPV4 co-localized in primary cultured astrocytes and mouse brain cortex. Double immunofluorescence images of KCa3.1 (green) and TRPV4 (red) in normal mouse brains ( a , b ), and primary cultured astrocytes ( c , d ). Note the strong co-localization indicated by merge yellow fluorescence, quantification of the co-localization observed in experiments as shown in g. ( e ) The histograms represent the ratio of the mean Pearson correlation coefficient calculated from the co-labeling in a number of samples, as indicated above the bar. Scale bar: 25 μm

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: KCa3.1 and TRPV4 co-localized in primary cultured astrocytes and mouse brain cortex. Double immunofluorescence images of KCa3.1 (green) and TRPV4 (red) in normal mouse brains ( a , b ), and primary cultured astrocytes ( c , d ). Note the strong co-localization indicated by merge yellow fluorescence, quantification of the co-localization observed in experiments as shown in g. ( e ) The histograms represent the ratio of the mean Pearson correlation coefficient calculated from the co-labeling in a number of samples, as indicated above the bar. Scale bar: 25 μm

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Cell Culture, Immunofluorescence, Fluorescence, Labeling

    Involvement of KCa3.1 in OGD-induced reactive astrogliosis. a , b Representative western blot showing GFAP expression in cultured astrocytes treated with OGD for 4 h in the presence of 1 μM TRAM-34 and 10 μM HC 067047. Quantification of western blot for GFAP expression ( n = 3). Data are presented as means ± SEM. # p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: Involvement of KCa3.1 in OGD-induced reactive astrogliosis. a , b Representative western blot showing GFAP expression in cultured astrocytes treated with OGD for 4 h in the presence of 1 μM TRAM-34 and 10 μM HC 067047. Quantification of western blot for GFAP expression ( n = 3). Data are presented as means ± SEM. # p

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Western Blot, Expressing, Cell Culture

    Upregulation of KCa3.1 channels and GFAP in mouse brains following pMCAO. a , b Western blot analysis of lysates from 10-week-old male WT mice following 1, 3, 6, or 12 h of pMCAO analyzed by antibodies to KCa3.1 ( a ) and GFAP ( b ). Data represent the means ± SEM of KCa3.1 and GFAP density normalized to β-actin values for n = 3. * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: Upregulation of KCa3.1 channels and GFAP in mouse brains following pMCAO. a , b Western blot analysis of lysates from 10-week-old male WT mice following 1, 3, 6, or 12 h of pMCAO analyzed by antibodies to KCa3.1 ( a ) and GFAP ( b ). Data represent the means ± SEM of KCa3.1 and GFAP density normalized to β-actin values for n = 3. * p

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Western Blot, Mouse Assay

    KCa3.1 deficiency reduces infarction volume and improves of neurological conditions. Focal cerebral ischemia was induced by pMCAO. a , c , and e Representative TTC staining of five corresponding coronal brain sections of a 10-week-old male WT mouse and a 10 week-old male KCa3.1 −/− mouse after 3 h ( a ), 6 h ( c ), and 24 h ( e ) of pMCAO. b , d , and f . Quantitative analysis of infarction volume in a, c, and e, respectively. Data are presented as means ± SEM. n = 6. * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: KCa3.1 deficiency reduces infarction volume and improves of neurological conditions. Focal cerebral ischemia was induced by pMCAO. a , c , and e Representative TTC staining of five corresponding coronal brain sections of a 10-week-old male WT mouse and a 10 week-old male KCa3.1 −/− mouse after 3 h ( a ), 6 h ( c ), and 24 h ( e ) of pMCAO. b , d , and f . Quantitative analysis of infarction volume in a, c, and e, respectively. Data are presented as means ± SEM. n = 6. * p

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Staining

    Upregulation of KCa3.1, GFAP, and TRPV4 channels following OGD in cultured astrocytes. Western blot analysis of ( a ) KCa3.1, ( b ) GFAP, and ( c ) TRPV4 expression after OGD-treatment for 0, 1, 3, 4, 6, 12 h. Data represent the means ± SEM of KCa3.1, GFAP, and TRPV4 density normalized to β-actin values for n = 3 cultures. * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: Upregulation of KCa3.1, GFAP, and TRPV4 channels following OGD in cultured astrocytes. Western blot analysis of ( a ) KCa3.1, ( b ) GFAP, and ( c ) TRPV4 expression after OGD-treatment for 0, 1, 3, 4, 6, 12 h. Data represent the means ± SEM of KCa3.1, GFAP, and TRPV4 density normalized to β-actin values for n = 3 cultures. * p

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Cell Culture, Western Blot, Expressing

    Decreased glial activation and neuronal loss in brains of KCa3.1 deletion mice following pMCAO. Reactive astrocytes ( a ), activated microglia ( b ), and neurons ( c ) from the hippocampal CA1 regions of WT or KCa3.1 −/− mice at 6 h after pMCAO were visualized by GFAP, Iba1, and NeuN immunostaining, respectively. At least four coronal slices from each mouse brain and at least three brains of each genotype were used for immunostaining and counting. n = 4 per group. Scale bar: 75 μm. Data represent means ± SEM. * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke

    doi: 10.1186/s12974-017-0973-8

    Figure Lengend Snippet: Decreased glial activation and neuronal loss in brains of KCa3.1 deletion mice following pMCAO. Reactive astrocytes ( a ), activated microglia ( b ), and neurons ( c ) from the hippocampal CA1 regions of WT or KCa3.1 −/− mice at 6 h after pMCAO were visualized by GFAP, Iba1, and NeuN immunostaining, respectively. At least four coronal slices from each mouse brain and at least three brains of each genotype were used for immunostaining and counting. n = 4 per group. Scale bar: 75 μm. Data represent means ± SEM. * p

    Article Snippet: Sections and cells were incubated at 4 °C overnight with primary antibodies: mouse anti-KCa3.1 (1:100; Alomone Labs), rabbit anti-GFAP (1:500; Dako); rabbit anti-Iba1 (1:500; Abcam); rabbit anti-NeuN antibody (1:500; Millipore), rabbit anti-TRPV4 (1:200; Alomone Labs).

    Techniques: Activation Assay, Mouse Assay, Immunostaining

    AKT modulation is crucial for KCa3.1-mediated ER stress in microglia. a , b Representative blots of p-AKT and total AKT in SNpc from a WT, WT+MPTP, KCa3.1 −/− , KCa3.1 −/− +MPTP group mice and from b control, MPTP, MPTP+Se, Se group mice. Data are presented as the mean ± SEM ( n = 3–5). Western blot was repeated three times and showed similar results. The OD value of p-AKT was normalized to that of AKT. * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 represents a valid pharmacological target for microgliosis-induced neuronal impairment in a mouse model of Parkinson’s disease

    doi: 10.1186/s12974-019-1682-2

    Figure Lengend Snippet: AKT modulation is crucial for KCa3.1-mediated ER stress in microglia. a , b Representative blots of p-AKT and total AKT in SNpc from a WT, WT+MPTP, KCa3.1 −/− , KCa3.1 −/− +MPTP group mice and from b control, MPTP, MPTP+Se, Se group mice. Data are presented as the mean ± SEM ( n = 3–5). Western blot was repeated three times and showed similar results. The OD value of p-AKT was normalized to that of AKT. * p

    Article Snippet: The blots were then incubated overnight at 4 °C with the following primary antibodies: β-actin (1:3000; Sigma-Aldrich), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-GRP78, mouse anti-CHOP, rabbit anti-phospho-Akt (Ser473), rabbit anti-phospho-Akt (Thr308), rabbit anti-Akt, rabbit anti-phospho-4E-BP1, rabbit anti-phospho-p70 S6 (1:1000; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-KCa3.1 (1:100; Alomone Labs, Ltd., Jerusalem, Israel).

    Techniques: Mouse Assay, Western Blot

    KCa3.1 involved in microglia SOCE and ER stress. a , b Representative images of GRP78, p-PERK, and p-eIF2α in KCa3.1 −/− microglia, responses to 500 μM MPP + ( a ) or 1 μM Tg ( b ) vs. WT cells. Mean values of GRP78, p-PERK, and p-eIF2α relative to β-actin. Data are presented as the mean ± SEM ( n = 3). Western blot was repeated three times and showed similar results. * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 represents a valid pharmacological target for microgliosis-induced neuronal impairment in a mouse model of Parkinson’s disease

    doi: 10.1186/s12974-019-1682-2

    Figure Lengend Snippet: KCa3.1 involved in microglia SOCE and ER stress. a , b Representative images of GRP78, p-PERK, and p-eIF2α in KCa3.1 −/− microglia, responses to 500 μM MPP + ( a ) or 1 μM Tg ( b ) vs. WT cells. Mean values of GRP78, p-PERK, and p-eIF2α relative to β-actin. Data are presented as the mean ± SEM ( n = 3). Western blot was repeated three times and showed similar results. * p

    Article Snippet: The blots were then incubated overnight at 4 °C with the following primary antibodies: β-actin (1:3000; Sigma-Aldrich), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-GRP78, mouse anti-CHOP, rabbit anti-phospho-Akt (Ser473), rabbit anti-phospho-Akt (Thr308), rabbit anti-Akt, rabbit anti-phospho-4E-BP1, rabbit anti-phospho-p70 S6 (1:1000; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-KCa3.1 (1:100; Alomone Labs, Ltd., Jerusalem, Israel).

    Techniques: Western Blot

    Upregulation of KCa3.1 channels and Iba1 in the brains of PD mouse model. a Western blot analysis of SNpc lysates from control and MPTP-induced PD mouse model analyzed by antibodies to TH, GFAP, Iba1, and KCa3.1. Data represent the mean ± SEM ( n = 3). Western blot was repeated three times and showed similar results; * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 represents a valid pharmacological target for microgliosis-induced neuronal impairment in a mouse model of Parkinson’s disease

    doi: 10.1186/s12974-019-1682-2

    Figure Lengend Snippet: Upregulation of KCa3.1 channels and Iba1 in the brains of PD mouse model. a Western blot analysis of SNpc lysates from control and MPTP-induced PD mouse model analyzed by antibodies to TH, GFAP, Iba1, and KCa3.1. Data represent the mean ± SEM ( n = 3). Western blot was repeated three times and showed similar results; * p

    Article Snippet: The blots were then incubated overnight at 4 °C with the following primary antibodies: β-actin (1:3000; Sigma-Aldrich), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-GRP78, mouse anti-CHOP, rabbit anti-phospho-Akt (Ser473), rabbit anti-phospho-Akt (Thr308), rabbit anti-Akt, rabbit anti-phospho-4E-BP1, rabbit anti-phospho-p70 S6 (1:1000; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-KCa3.1 (1:100; Alomone Labs, Ltd., Jerusalem, Israel).

    Techniques: Western Blot

    Genetic KCa3.1 deletion and pharmacological blockade with senicapoc attenuate MPTP-induced loss of DA neurons. a – g WT or KCa3.1 −/− mice received sequential intraperitoneal injections of MPTP (20 mg/kg) with or without senicapoc (100 mg/kg, once daily, p.o.) treatment for 5 days as described in the “ Material and methods ” section. Open field test ( b – e ) and the rotarod test ( f , g ) for bradykinesia were performed. Behavioral tests for MPTP-induced bradykinesia were conducted on the indicated days. Data are presented as mean ± SEM ( n = 10–15). b – e ** p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 represents a valid pharmacological target for microgliosis-induced neuronal impairment in a mouse model of Parkinson’s disease

    doi: 10.1186/s12974-019-1682-2

    Figure Lengend Snippet: Genetic KCa3.1 deletion and pharmacological blockade with senicapoc attenuate MPTP-induced loss of DA neurons. a – g WT or KCa3.1 −/− mice received sequential intraperitoneal injections of MPTP (20 mg/kg) with or without senicapoc (100 mg/kg, once daily, p.o.) treatment for 5 days as described in the “ Material and methods ” section. Open field test ( b – e ) and the rotarod test ( f , g ) for bradykinesia were performed. Behavioral tests for MPTP-induced bradykinesia were conducted on the indicated days. Data are presented as mean ± SEM ( n = 10–15). b – e ** p

    Article Snippet: The blots were then incubated overnight at 4 °C with the following primary antibodies: β-actin (1:3000; Sigma-Aldrich), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-GRP78, mouse anti-CHOP, rabbit anti-phospho-Akt (Ser473), rabbit anti-phospho-Akt (Thr308), rabbit anti-Akt, rabbit anti-phospho-4E-BP1, rabbit anti-phospho-p70 S6 (1:1000; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-KCa3.1 (1:100; Alomone Labs, Ltd., Jerusalem, Israel).

    Techniques: Mouse Assay

    Genetic KCa3.1 deletion and pharmacological blockade with senicapoc attenuated MPTP-induced ER stress. a , d Western blot analysis of GRP78 and CHOP protein levels in SNpc. b , c , e , f Data are presented as the mean ± SEM ( n = 5–6). Western blot was repeated three times and showed similar results. # p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 represents a valid pharmacological target for microgliosis-induced neuronal impairment in a mouse model of Parkinson’s disease

    doi: 10.1186/s12974-019-1682-2

    Figure Lengend Snippet: Genetic KCa3.1 deletion and pharmacological blockade with senicapoc attenuated MPTP-induced ER stress. a , d Western blot analysis of GRP78 and CHOP protein levels in SNpc. b , c , e , f Data are presented as the mean ± SEM ( n = 5–6). Western blot was repeated three times and showed similar results. # p

    Article Snippet: The blots were then incubated overnight at 4 °C with the following primary antibodies: β-actin (1:3000; Sigma-Aldrich), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-GRP78, mouse anti-CHOP, rabbit anti-phospho-Akt (Ser473), rabbit anti-phospho-Akt (Thr308), rabbit anti-Akt, rabbit anti-phospho-4E-BP1, rabbit anti-phospho-p70 S6 (1:1000; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-KCa3.1 (1:100; Alomone Labs, Ltd., Jerusalem, Israel).

    Techniques: Western Blot

    Genetic KCa3.1 deletion and pharmacological blockade with senicapoc attenuate MPTP-induced microgliosis. a , c Immunostaining for Iba1 in SNpc. Bar 50 μM. Quantitative analysis of Iba1 + cells in SNpc. Data are presented as mean ± SEM ( n = 5–8). * p

    Journal: Journal of Neuroinflammation

    Article Title: The potassium channel KCa3.1 represents a valid pharmacological target for microgliosis-induced neuronal impairment in a mouse model of Parkinson’s disease

    doi: 10.1186/s12974-019-1682-2

    Figure Lengend Snippet: Genetic KCa3.1 deletion and pharmacological blockade with senicapoc attenuate MPTP-induced microgliosis. a , c Immunostaining for Iba1 in SNpc. Bar 50 μM. Quantitative analysis of Iba1 + cells in SNpc. Data are presented as mean ± SEM ( n = 5–8). * p

    Article Snippet: The blots were then incubated overnight at 4 °C with the following primary antibodies: β-actin (1:3000; Sigma-Aldrich), rabbit anti-mTOR, rabbit anti-phospho-mTOR (Ser2448), rabbit anti-GRP78, mouse anti-CHOP, rabbit anti-phospho-Akt (Ser473), rabbit anti-phospho-Akt (Thr308), rabbit anti-Akt, rabbit anti-phospho-4E-BP1, rabbit anti-phospho-p70 S6 (1:1000; Cell Signaling Technology, Danvers, MA, USA), and mouse anti-KCa3.1 (1:100; Alomone Labs, Ltd., Jerusalem, Israel).

    Techniques: Immunostaining

    Involvement of KCa3.1 in OGD-induced phenotypic modulation of astrocytes through the ERK1/2 and JNK signaling pathways. (A,C,E) Representative images of total JNK, ERK1/2, P38 and phosphorylated JNK (p-JNK), ERK1/2 (p-ERK1/2), P38 (p-P38) in WT and KO astrocytes with or without OGD (1 h). (B,D,F) Mean values of p-JNK, p-ERK1/2 and p-P38 relative to total JNK, ERK1/2 and P38 protein ( n = 3). Data are presented as means ± SEM. * p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: Involvement of KCa3.1 in OGD-induced phenotypic modulation of astrocytes through the ERK1/2 and JNK signaling pathways. (A,C,E) Representative images of total JNK, ERK1/2, P38 and phosphorylated JNK (p-JNK), ERK1/2 (p-ERK1/2), P38 (p-P38) in WT and KO astrocytes with or without OGD (1 h). (B,D,F) Mean values of p-JNK, p-ERK1/2 and p-P38 relative to total JNK, ERK1/2 and P38 protein ( n = 3). Data are presented as means ± SEM. * p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques:

    Involvement of KCa3.1 in pMCAO mouse model through ERK1/2 and JNK signaling pathways. Focal cerebral ischemia was induced by pMCAO in WT and KO mice. (A–D) Western blot analysis of lysates from 10-week-old male WT and KO mice 1, 3, 6 and 24 h after pMCAO, analyzed by antibodies to phosphorylated ERK1/2 (p-ERK1/2), JNK (p-JNK), P38 (p-P38). Data represent means ± SEM of p-ERK1/2, p-JNK, p-P38 density, normalized to β-actin values ( n = 3). * p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: Involvement of KCa3.1 in pMCAO mouse model through ERK1/2 and JNK signaling pathways. Focal cerebral ischemia was induced by pMCAO in WT and KO mice. (A–D) Western blot analysis of lysates from 10-week-old male WT and KO mice 1, 3, 6 and 24 h after pMCAO, analyzed by antibodies to phosphorylated ERK1/2 (p-ERK1/2), JNK (p-JNK), P38 (p-P38). Data represent means ± SEM of p-ERK1/2, p-JNK, p-P38 density, normalized to β-actin values ( n = 3). * p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: Mouse Assay, Western Blot

    KCa3.1 is involved in ER stress in vivo . Focal cerebral ischemia was induced by pMCAO in WT and KO mice. (A–C) Western blot analysis of lysates from 10-week-old male WT and KO mice 1, 3, 6 and 24 h after pMCAO, analyzed by antibodies to GFAP and GRP78. Data represent means ± SEM of GFAP and GRP78 density, normalized to β-actin values ( n = 3). * p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: KCa3.1 is involved in ER stress in vivo . Focal cerebral ischemia was induced by pMCAO in WT and KO mice. (A–C) Western blot analysis of lysates from 10-week-old male WT and KO mice 1, 3, 6 and 24 h after pMCAO, analyzed by antibodies to GFAP and GRP78. Data represent means ± SEM of GFAP and GRP78 density, normalized to β-actin values ( n = 3). * p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: In Vivo, Mouse Assay, Western Blot

    Blockade of KCa3.1 attenuated OGD-induced astrogliosis and endoplasmic reticulum (ER) stress in primary astrocytes. (A) Whole-cell lysates were collected to evaluate the expression of GFAP and 78 kDa glucose-regulated protein (GRP78) in primary astrocytes by western blotting after 4 h OGD. β-Actin was used as a loading control. (B) The bar graphs represent the ratio of GFAP/β-actin and GRP78/β-actin, normalized to the control ( n = 3–4). β-Actin was used as a loading control. The data are expressed as means ± SEM. # p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: Blockade of KCa3.1 attenuated OGD-induced astrogliosis and endoplasmic reticulum (ER) stress in primary astrocytes. (A) Whole-cell lysates were collected to evaluate the expression of GFAP and 78 kDa glucose-regulated protein (GRP78) in primary astrocytes by western blotting after 4 h OGD. β-Actin was used as a loading control. (B) The bar graphs represent the ratio of GFAP/β-actin and GRP78/β-actin, normalized to the control ( n = 3–4). β-Actin was used as a loading control. The data are expressed as means ± SEM. # p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: Expressing, Western Blot

    Genetic deletion of KCa3.1 attenuated OGD-induced ER stress in primary astrocytes. (A,B) Whole-cell lysates were collected to evaluate the expression of GFAP in wildtype (WT) and KCa3.1 KO astrocytes by western blotting after 4 h OGD. β-Actin was used as a loading control. The bar graphs represent the ratio of GFAP/β-actin, normalized to the control ( n = 3–4). (C,D) Whole-cell lysates were collected to evaluate the expression of GRP78 in WT and KCa3.1 KO astrocytes by western blotting after 1 h OGD. β-Actin was used as a loading control. The bar graphs represent the ratio of GRP78/β-actin, normalized to the control ( n = 3–4). (E,F) Whole-cell lysates were collected to evaluate the expression of p-eIF-2α in WT and KCa3.1 KO astrocytes by western blotting after 4 h OGD. β-Actin was used as a loading control. The bar graphs represent the ratio of p-eIF-2α/β-actin, normalized to the control ( n = 3–4). The data are expressed as means ± SEM. ** p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: Genetic deletion of KCa3.1 attenuated OGD-induced ER stress in primary astrocytes. (A,B) Whole-cell lysates were collected to evaluate the expression of GFAP in wildtype (WT) and KCa3.1 KO astrocytes by western blotting after 4 h OGD. β-Actin was used as a loading control. The bar graphs represent the ratio of GFAP/β-actin, normalized to the control ( n = 3–4). (C,D) Whole-cell lysates were collected to evaluate the expression of GRP78 in WT and KCa3.1 KO astrocytes by western blotting after 1 h OGD. β-Actin was used as a loading control. The bar graphs represent the ratio of GRP78/β-actin, normalized to the control ( n = 3–4). (E,F) Whole-cell lysates were collected to evaluate the expression of p-eIF-2α in WT and KCa3.1 KO astrocytes by western blotting after 4 h OGD. β-Actin was used as a loading control. The bar graphs represent the ratio of p-eIF-2α/β-actin, normalized to the control ( n = 3–4). The data are expressed as means ± SEM. ** p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: Expressing, Western Blot

    KCa3.1 channel is involved in OGD-induced reduction in viability of astrocytes. Cell viability was determined using the CCK-8 assay. The values represent the fold changes of cell viability induced by OGD. Genetic deletion of the KCa3.1 channel attenuated the decrease in viability of astrocytes after 4 h OGD, compared with WT cells ( n = 5). The data are expressed as means ± SEM. ** p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: KCa3.1 channel is involved in OGD-induced reduction in viability of astrocytes. Cell viability was determined using the CCK-8 assay. The values represent the fold changes of cell viability induced by OGD. Genetic deletion of the KCa3.1 channel attenuated the decrease in viability of astrocytes after 4 h OGD, compared with WT cells ( n = 5). The data are expressed as means ± SEM. ** p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: CCK-8 Assay

    KCa3.1 deficiency reduces infarction volume. Focal cerebral ischemia was induced by permanent middle cerebral artery occlusion (pMCAO). (A–C) Representative TTC staining of five corresponding coronal brain sections of WT and KO mouse after 3 h (A) , 6 h (B) and 24 h (C) of pMCAO. (D) Quantitative analysis of infarction volume in 3, 6 and 24 h, respectively. Data are presented as means ± SEM. n = 5. * p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: KCa3.1 deficiency reduces infarction volume. Focal cerebral ischemia was induced by permanent middle cerebral artery occlusion (pMCAO). (A–C) Representative TTC staining of five corresponding coronal brain sections of WT and KO mouse after 3 h (A) , 6 h (B) and 24 h (C) of pMCAO. (D) Quantitative analysis of infarction volume in 3, 6 and 24 h, respectively. Data are presented as means ± SEM. n = 5. * p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: Staining

    Up-regulation of KCa3.1 in OGD-induced reactive astrogliosis. Primary cultured astrocytes were subjected to OGD in vitro for different time periods, as shown. (A) Western blot analysis of astrocytic lysates following 1, 3, 4, 6 or 12 h of OGD, analyzed by antibodies to KCa3.1 and glial fibrillary acidic protein (GFAP). β-Actin was used as a loading control. (B) The bar graphs represent the fold changes of KCa3.1 and GFAP, normalized to control cells ( n = 3). The data are expressed as means ± SEM. * p

    Journal: Frontiers in Cellular Neuroscience

    Article Title: KCa3.1 Inhibition Switches the Astrocyte Phenotype during Astrogliosis Associated with Ischemic Stroke Via Endoplasmic Reticulum Stress and MAPK Signaling Pathways

    doi: 10.3389/fncel.2017.00319

    Figure Lengend Snippet: Up-regulation of KCa3.1 in OGD-induced reactive astrogliosis. Primary cultured astrocytes were subjected to OGD in vitro for different time periods, as shown. (A) Western blot analysis of astrocytic lysates following 1, 3, 4, 6 or 12 h of OGD, analyzed by antibodies to KCa3.1 and glial fibrillary acidic protein (GFAP). β-Actin was used as a loading control. (B) The bar graphs represent the fold changes of KCa3.1 and GFAP, normalized to control cells ( n = 3). The data are expressed as means ± SEM. * p

    Article Snippet: The membranes were first incubated (overnight, 4°C) with the following primary antibodies: anti-total p38/JNK/ERK/c-Jun/eIF-2α, anti-phospho-p38/JNK/ERK/c-Jun/eIF-2α antibodies (1:1000, Cell Signaling Technology, Danvers, MA, USA), anti-GRP78 antibody (1:1000, Abcam), anti-GFAP antibody (1:5000, Dako, Glostrup, Denmark), anti-KCa3.1 antibody (1:500, Alomone Labs, Jerusalem, Israel) and anti-β-actin (1:1000, Sigma).

    Techniques: Cell Culture, In Vitro, Western Blot