rabbit anti cacna1b  (Alomone Labs)


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    Alomone Labs rabbit anti cacna1b
    Primary antibodies used in the present study.
    Rabbit Anti Cacna1b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti cacna1b/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti cacna1b - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK"

    Article Title: Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    doi: 10.12659/MSM.912862

    Primary antibodies used in the present study.
    Figure Legend Snippet: Primary antibodies used in the present study.

    Techniques Used:

    Effects of knockdown ACAT1 on CACNAs, PKC, and ERK phosphorylation and in Aβ-induced SH-SY5Y cells. ( A ) Western blot results showed that the relative expression of CACNA1b and CACNA2d1 was increased significantly, while the total PKC and the ratio of phospho-ERK (p-ERK)/ERK were decreased significantly after Aβ 25-35 treatment. ( B ) Knockdown of ACAT1 rescued the reduction of PKC and phosphorylation level of ERK, and also retarded the upregulation of CACNA1b and CACNA2d1 induced by Aβ. (** P <0.01 and * P <0.05).
    Figure Legend Snippet: Effects of knockdown ACAT1 on CACNAs, PKC, and ERK phosphorylation and in Aβ-induced SH-SY5Y cells. ( A ) Western blot results showed that the relative expression of CACNA1b and CACNA2d1 was increased significantly, while the total PKC and the ratio of phospho-ERK (p-ERK)/ERK were decreased significantly after Aβ 25-35 treatment. ( B ) Knockdown of ACAT1 rescued the reduction of PKC and phosphorylation level of ERK, and also retarded the upregulation of CACNA1b and CACNA2d1 induced by Aβ. (** P <0.01 and * P <0.05).

    Techniques Used: Western Blot, Expressing

    rabbit anti cacna1b  (Alomone Labs)


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  • 94

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    Alomone Labs rabbit anti cacna1b
    Primary antibodies used in the present study.
    Rabbit Anti Cacna1b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti cacna1b/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti cacna1b - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK"

    Article Title: Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    doi: 10.12659/MSM.912862

    Primary antibodies used in the present study.
    Figure Legend Snippet: Primary antibodies used in the present study.

    Techniques Used:

    Effects of knockdown ACAT1 on CACNAs, PKC, and ERK phosphorylation and in Aβ-induced SH-SY5Y cells. ( A ) Western blot results showed that the relative expression of CACNA1b and CACNA2d1 was increased significantly, while the total PKC and the ratio of phospho-ERK (p-ERK)/ERK were decreased significantly after Aβ 25-35 treatment. ( B ) Knockdown of ACAT1 rescued the reduction of PKC and phosphorylation level of ERK, and also retarded the upregulation of CACNA1b and CACNA2d1 induced by Aβ. (** P <0.01 and * P <0.05).
    Figure Legend Snippet: Effects of knockdown ACAT1 on CACNAs, PKC, and ERK phosphorylation and in Aβ-induced SH-SY5Y cells. ( A ) Western blot results showed that the relative expression of CACNA1b and CACNA2d1 was increased significantly, while the total PKC and the ratio of phospho-ERK (p-ERK)/ERK were decreased significantly after Aβ 25-35 treatment. ( B ) Knockdown of ACAT1 rescued the reduction of PKC and phosphorylation level of ERK, and also retarded the upregulation of CACNA1b and CACNA2d1 induced by Aβ. (** P <0.01 and * P <0.05).

    Techniques Used: Western Blot, Expressing

    cav2 2  (Alomone Labs)


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    Alomone Labs cav2 2
    Primer sequences.
    Cav2 2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    cav2 2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Upregulation of N-Type Voltage-Gated Calcium Channels Induces Neuropathic Pain in Experimental Autoimmune Neuritis"

    Article Title: Upregulation of N-Type Voltage-Gated Calcium Channels Induces Neuropathic Pain in Experimental Autoimmune Neuritis

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2022/8547095

    Primer sequences.
    Figure Legend Snippet: Primer sequences.

    Techniques Used: Sequencing

    Effect of Cav2.2 on clinical score and sciatic nerve tissue of rats. (a) Clinical score record of rats during 18 days of immunization; (b) changes in body weight of rats during 18 days of immunization; (c) luxol fast blue (LFB) staining-based observation of the degree of cell infiltration and demyelination in sciatic nerve tissue of rats on the 18 th day of immunization. ∗∗ P < 0.01 vs. control group, ## P < 0.01 vs. EAN-shRNA group.
    Figure Legend Snippet: Effect of Cav2.2 on clinical score and sciatic nerve tissue of rats. (a) Clinical score record of rats during 18 days of immunization; (b) changes in body weight of rats during 18 days of immunization; (c) luxol fast blue (LFB) staining-based observation of the degree of cell infiltration and demyelination in sciatic nerve tissue of rats on the 18 th day of immunization. ∗∗ P < 0.01 vs. control group, ## P < 0.01 vs. EAN-shRNA group.

    Techniques Used: Staining, shRNA

    Effect of Cav2.2 on allodynia in rats. (a–d) Measurement of withdrawal threshold to mechanical (a), thermal (b), and cold (c) stimulation, and mechanical hyperalgesia threshold (d) during 18 days of immunization. ∗∗ P < 0.01 vs. Control group, ## P < 0.01 vs. EAN-shRNA group.
    Figure Legend Snippet: Effect of Cav2.2 on allodynia in rats. (a–d) Measurement of withdrawal threshold to mechanical (a), thermal (b), and cold (c) stimulation, and mechanical hyperalgesia threshold (d) during 18 days of immunization. ∗∗ P < 0.01 vs. Control group, ## P < 0.01 vs. EAN-shRNA group.

    Techniques Used: shRNA

    Effect of Cav2.2 on rat inflammatory response. (a) ELISA-based measurement of IL-6 and TNF- α expression in rat serum; (b) qRT-PCR-based measurement of mRNA expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve; (c) western blot-based measurement of protein expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve. ∗ P < 0.05 and ∗∗ P < 0.01 vs. control group, # P < 0.05 and ## P < 0.01 vs. EAN-shRNA group.
    Figure Legend Snippet: Effect of Cav2.2 on rat inflammatory response. (a) ELISA-based measurement of IL-6 and TNF- α expression in rat serum; (b) qRT-PCR-based measurement of mRNA expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve; (c) western blot-based measurement of protein expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve. ∗ P < 0.05 and ∗∗ P < 0.01 vs. control group, # P < 0.05 and ## P < 0.01 vs. EAN-shRNA group.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Expressing, Quantitative RT-PCR, Western Blot, shRNA

    α1b  (Alomone Labs)


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    Alomone Labs α1b
    Ca channel α 1 subunits co-express with the ganglion cell antibody RBPMS in vertical sections showing the inner plexiform layer (IPL), the ganglion cell layer (GCL) and the nerve fiber layer (NFL). ( Top row ) Double immunostaining with α1C subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). RGC axons (arrowhead) as well as putative Müller and neuronal cell processes in the IPL showed immunostaining. Control preadsorption of α1C antibody with the immunization peptide showed no staining. ( Second row ) Double immunostaining with α1D subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Numerous processes in the IPL as well as the RGC axons throughout the NFL (arrowhead) were also labelled. Control preadsorption of α1D antibody with the immunization peptide showed no staining. ( Third row ) Double immunostaining with <t>α1B</t> subunit and RBPMS antibodies shows colocalization in RGC somata (filled arrow). Processes in the IPL, putative displaced amacrine cells in the GCL (open arrows) and RGC axons throughout the NFL (arrowheads) showed immunostaining. Control preadsorption of α1B antibody with the immunization peptide showed no staining. ( Bottom row ) Double immunostaining with α1A subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Labelling in the IPL and in putative displaced amacrine cells in the GCL (open arrows) was also seen. Control preadsorption of α1A antibody with the immunization peptide showed no staining. Scale bar is 20 µm.
    α1b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α1b/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α1b - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Differential Calcium Signaling Mediated by Voltage-Gated Calcium Channels in Rat Retinal Ganglion Cells and Their Unmyelinated Axons"

    Article Title: Differential Calcium Signaling Mediated by Voltage-Gated Calcium Channels in Rat Retinal Ganglion Cells and Their Unmyelinated Axons

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0084507

    Ca channel α 1 subunits co-express with the ganglion cell antibody RBPMS in vertical sections showing the inner plexiform layer (IPL), the ganglion cell layer (GCL) and the nerve fiber layer (NFL). ( Top row ) Double immunostaining with α1C subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). RGC axons (arrowhead) as well as putative Müller and neuronal cell processes in the IPL showed immunostaining. Control preadsorption of α1C antibody with the immunization peptide showed no staining. ( Second row ) Double immunostaining with α1D subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Numerous processes in the IPL as well as the RGC axons throughout the NFL (arrowhead) were also labelled. Control preadsorption of α1D antibody with the immunization peptide showed no staining. ( Third row ) Double immunostaining with α1B subunit and RBPMS antibodies shows colocalization in RGC somata (filled arrow). Processes in the IPL, putative displaced amacrine cells in the GCL (open arrows) and RGC axons throughout the NFL (arrowheads) showed immunostaining. Control preadsorption of α1B antibody with the immunization peptide showed no staining. ( Bottom row ) Double immunostaining with α1A subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Labelling in the IPL and in putative displaced amacrine cells in the GCL (open arrows) was also seen. Control preadsorption of α1A antibody with the immunization peptide showed no staining. Scale bar is 20 µm.
    Figure Legend Snippet: Ca channel α 1 subunits co-express with the ganglion cell antibody RBPMS in vertical sections showing the inner plexiform layer (IPL), the ganglion cell layer (GCL) and the nerve fiber layer (NFL). ( Top row ) Double immunostaining with α1C subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). RGC axons (arrowhead) as well as putative Müller and neuronal cell processes in the IPL showed immunostaining. Control preadsorption of α1C antibody with the immunization peptide showed no staining. ( Second row ) Double immunostaining with α1D subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Numerous processes in the IPL as well as the RGC axons throughout the NFL (arrowhead) were also labelled. Control preadsorption of α1D antibody with the immunization peptide showed no staining. ( Third row ) Double immunostaining with α1B subunit and RBPMS antibodies shows colocalization in RGC somata (filled arrow). Processes in the IPL, putative displaced amacrine cells in the GCL (open arrows) and RGC axons throughout the NFL (arrowheads) showed immunostaining. Control preadsorption of α1B antibody with the immunization peptide showed no staining. ( Bottom row ) Double immunostaining with α1A subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Labelling in the IPL and in putative displaced amacrine cells in the GCL (open arrows) was also seen. Control preadsorption of α1A antibody with the immunization peptide showed no staining. Scale bar is 20 µm.

    Techniques Used: Double Immunostaining, Immunostaining, Staining

    R at wholemount retina labelled with RBPMS (red), α1B VGCC subunit (green), and NF-M (white) antibodies. α1B colocalized with RBPMS in RGC somata (filled arrow), NF-M in RGC axons (arrowhead) and putative displaced amacrine cells (open arrow). Stack of six optical sections each of 0.3 µm thickness. Scale bar is 20 µm.
    Figure Legend Snippet: R at wholemount retina labelled with RBPMS (red), α1B VGCC subunit (green), and NF-M (white) antibodies. α1B colocalized with RBPMS in RGC somata (filled arrow), NF-M in RGC axons (arrowhead) and putative displaced amacrine cells (open arrow). Stack of six optical sections each of 0.3 µm thickness. Scale bar is 20 µm.

    Techniques Used:

    anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b  (Alomone Labs)


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    Alomone Labs anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b
    Anti Ca V 2 2 Cacna1b Antibody Voltage Dependent N Type Calcium Channel Subunit α 1b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b - by Bioz Stars, 2023-02
    94/100 stars

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    rabbit anti n type calcium channel  (Alomone Labs)


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    Alomone Labs rabbit anti n type calcium channel
    Rabbit Anti N Type Calcium Channel, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    anti cacna1b cav2 2 antibody  (Alomone Labs)


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    Alomone Labs anti cacna1b cav2 2 antibody
    Anti Cacna1b Cav2 2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti cacna1b cav2 2 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    anti cacna1b cav2 2 antibody - by Bioz Stars, 2023-02
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    anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b  (Alomone Labs)


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    Alomone Labs anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b
    Anti Ca V 2 2 Cacna1b Antibody Voltage Dependent N Type Calcium Channel Subunit α 1b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    anti ca v 2 2 cacna1b antibody voltage dependent n type calcium channel subunit α 1b - by Bioz Stars, 2023-02
    94/100 stars

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    rabbit anti cacna1b  (Alomone Labs)


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    Alomone Labs rabbit anti cacna1b
    Rabbit Anti Cacna1b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti cacna1b/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    rabbit anti cacna1b - by Bioz Stars, 2023-02
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    rabbit anti ca v 2 2 antibody  (Alomone Labs)


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    Alomone Labs rabbit anti ca v 2 2 antibody
    Rabbit Anti Ca V 2 2 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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    anti cav2 2  (Alomone Labs)


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    Alomone Labs anti cav2 2
    Schematic representation of <t>Cav2.2</t> channels and mMORs. a The Cav2.2 proximal C-terminus is in part encoded by the mutually exclusive exons 37a and 37b. The illustration shows the amino acids encoded by each exon. Shown in red is the tyrosine that was mutated for the experiments in Fig. . b MOR full-length distal C-terminal variants are produced by alternative splicing and amino acid sequences encoded by exon 4, 7 and 7–8-9 are depicted
    Anti Cav2 2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti cav2 2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti cav2 2 - by Bioz Stars, 2023-02
    94/100 stars

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    1) Product Images from "Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors"

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    Journal: Molecular Brain

    doi: 10.1186/s13041-019-0524-6

    Schematic representation of Cav2.2 channels and mMORs. a The Cav2.2 proximal C-terminus is in part encoded by the mutually exclusive exons 37a and 37b. The illustration shows the amino acids encoded by each exon. Shown in red is the tyrosine that was mutated for the experiments in Fig. . b MOR full-length distal C-terminal variants are produced by alternative splicing and amino acid sequences encoded by exon 4, 7 and 7–8-9 are depicted
    Figure Legend Snippet: Schematic representation of Cav2.2 channels and mMORs. a The Cav2.2 proximal C-terminus is in part encoded by the mutually exclusive exons 37a and 37b. The illustration shows the amino acids encoded by each exon. Shown in red is the tyrosine that was mutated for the experiments in Fig. . b MOR full-length distal C-terminal variants are produced by alternative splicing and amino acid sequences encoded by exon 4, 7 and 7–8-9 are depicted

    Techniques Used: Produced

    Inhibition of Src and Cav2.2-37a Y1747F abolish the effect of mMOR1C on Cav2.2-37a peak current density. a Peak current density of Cav2.2-37a channels treated overnight with vehicle (0.1% water or 500 ng/ml of PTX overnight. b Peak current density of Cav2.2-37a channels treated for 4 h with vehicle (0.004% DMSO) or 2 μM of the Src inhibitor PP1. c Peak current density of the Cav2.2-37a Y1747F mutant in the absence and the presence of mMOR1C. The number of cells recorded is indicated in parentheses, asterisks denote significance at the *0.05 and **0.01 levels ( a and b – ANOVA, c - Mann-Whitney test)
    Figure Legend Snippet: Inhibition of Src and Cav2.2-37a Y1747F abolish the effect of mMOR1C on Cav2.2-37a peak current density. a Peak current density of Cav2.2-37a channels treated overnight with vehicle (0.1% water or 500 ng/ml of PTX overnight. b Peak current density of Cav2.2-37a channels treated for 4 h with vehicle (0.004% DMSO) or 2 μM of the Src inhibitor PP1. c Peak current density of the Cav2.2-37a Y1747F mutant in the absence and the presence of mMOR1C. The number of cells recorded is indicated in parentheses, asterisks denote significance at the *0.05 and **0.01 levels ( a and b – ANOVA, c - Mann-Whitney test)

    Techniques Used: Inhibition, Mutagenesis, MANN-WHITNEY

    Peak current densities (I peak) of Cav2.2e37a and Cav2.2e37b channels coexpressed with mMOR1, mMOR1C or mMOR1O. a Representative whole cell current traces recorded in response to depolarizing steps from − 60 mV to + 40 mV from a holding potential of − 80 mV from tsA-201 cells expressing Cav2.2-37a/Cavβ1/Cavα2δ-1 or Cav2.2-37b /Cavβ1/Cavα2δ-1 channels plus/minus mMOR1C. b Average current density-voltage relationships for cells expressing Cav2.2-37a channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. c Average current density-voltage relationships for cells expressing Cav2.2-37b channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. d Average peak current density for whole cell calcium currents recorded from cells expressing Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O. e Average peak current density recorded from tsA-201 cells expressing Cav2.2e37b/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C or mMOR1O. The numbers in parentheses represent the number of cells recorded. n.s. – not significant, asterisks denote significance at the *0.05 and ***0.001 levels ( d – ANOVA; e - Kruskal-Wallis test)
    Figure Legend Snippet: Peak current densities (I peak) of Cav2.2e37a and Cav2.2e37b channels coexpressed with mMOR1, mMOR1C or mMOR1O. a Representative whole cell current traces recorded in response to depolarizing steps from − 60 mV to + 40 mV from a holding potential of − 80 mV from tsA-201 cells expressing Cav2.2-37a/Cavβ1/Cavα2δ-1 or Cav2.2-37b /Cavβ1/Cavα2δ-1 channels plus/minus mMOR1C. b Average current density-voltage relationships for cells expressing Cav2.2-37a channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. c Average current density-voltage relationships for cells expressing Cav2.2-37b channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. d Average peak current density for whole cell calcium currents recorded from cells expressing Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O. e Average peak current density recorded from tsA-201 cells expressing Cav2.2e37b/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C or mMOR1O. The numbers in parentheses represent the number of cells recorded. n.s. – not significant, asterisks denote significance at the *0.05 and ***0.001 levels ( d – ANOVA; e - Kruskal-Wallis test)

    Techniques Used: Expressing, Activation Assay

    Biotinylation of Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O.Biotinylated cell surface proteins were isolated and normalized to Na/K-ATPase levels. a Representative blot of Cav2.2-37a surface and total expression (top blots) and Na/K-ATPase surface and total expression (bottom blots). b Quantification of plasma membrane Cav2.2-37a/ Cavβ1/Cavα2δ-1 channel expression in the absence and the presence of mMOR1, mMOR1C or mMOR1O (normalized by Na/K-ATPase cell surface expression). c Quantification of total Cav2.2-37a/Cavβ1/Cavα2δ-1 expression in the absence or the presence of mMOR1, mMOR1C or mMOR1O (normalized by total Na/K-ATPase expression). d Normalized surface to total expression of Cav2.2-37a channels. Data are from 4 independent experiments. n.s. – not significant (Kruskal-Wallis test)
    Figure Legend Snippet: Biotinylation of Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O.Biotinylated cell surface proteins were isolated and normalized to Na/K-ATPase levels. a Representative blot of Cav2.2-37a surface and total expression (top blots) and Na/K-ATPase surface and total expression (bottom blots). b Quantification of plasma membrane Cav2.2-37a/ Cavβ1/Cavα2δ-1 channel expression in the absence and the presence of mMOR1, mMOR1C or mMOR1O (normalized by Na/K-ATPase cell surface expression). c Quantification of total Cav2.2-37a/Cavβ1/Cavα2δ-1 expression in the absence or the presence of mMOR1, mMOR1C or mMOR1O (normalized by total Na/K-ATPase expression). d Normalized surface to total expression of Cav2.2-37a channels. Data are from 4 independent experiments. n.s. – not significant (Kruskal-Wallis test)

    Techniques Used: Isolation, Expressing

    G protein modulation of Cav2.2-37a and Cav2.2-37b channels following activation of mMOR1, mMOR1C and mMOR1O. a Representative set of Cav2.2-37a currents in the presence of mMOR1C, recorded before or after the application of 10 μM DAMGO. As outlined in the Results section, P1 represents the first current in each trace evoked by a test depolarization to + 10 mV, P2 is the second inward current in a given trace evoked by a 10 mV test depolarization (P2) preceded by a strong depolarizing prepulse (PP, note that the pre-pulse-evoked outward current is not shown in the figure). Relief of Gβγ modulation by the pre-pulse is observed by the increase in current amplitude seen during P2 in the presence of DAMGO. b Percentage of peak current inhibition (during P1) of Cav2.2e-37a currents after application of 10 μM DAMGO. c Percentage of peak current inhibition (during P1) of Cav2.2e-37b currents after application of 10 μM DAMGO. d Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37a channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by test pulse P2 normalized to the current evoked by test pulse P1. e Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37b channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by the test pulse P2 normalized to the current evoked by test pulse P1. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05, **0.01, and ***0.001 levels (unpaired Wilcoxon test)
    Figure Legend Snippet: G protein modulation of Cav2.2-37a and Cav2.2-37b channels following activation of mMOR1, mMOR1C and mMOR1O. a Representative set of Cav2.2-37a currents in the presence of mMOR1C, recorded before or after the application of 10 μM DAMGO. As outlined in the Results section, P1 represents the first current in each trace evoked by a test depolarization to + 10 mV, P2 is the second inward current in a given trace evoked by a 10 mV test depolarization (P2) preceded by a strong depolarizing prepulse (PP, note that the pre-pulse-evoked outward current is not shown in the figure). Relief of Gβγ modulation by the pre-pulse is observed by the increase in current amplitude seen during P2 in the presence of DAMGO. b Percentage of peak current inhibition (during P1) of Cav2.2e-37a currents after application of 10 μM DAMGO. c Percentage of peak current inhibition (during P1) of Cav2.2e-37b currents after application of 10 μM DAMGO. d Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37a channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by test pulse P2 normalized to the current evoked by test pulse P1. e Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37b channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by the test pulse P2 normalized to the current evoked by test pulse P1. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05, **0.01, and ***0.001 levels (unpaired Wilcoxon test)

    Techniques Used: Activation Assay, Inhibition, Expressing

    Voltage dependent and voltage independent components of DAMGO-induced modulation of Cav2.2 variants by the various MORs. a Voltage-dependent and independent inhibition of Cav2.2-37a channels coexpressed with mMOR1, mMOR1C and mMOR1O. b Voltage-dependent and independent inhibition of Cav2.2-37b channels coexpressed with mMOR1, mMOR1C and mMOR1O. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05 and ***0.001 levels (t-test) between voltage-dependent and voltage-independent modulation for each receptor-channel combination
    Figure Legend Snippet: Voltage dependent and voltage independent components of DAMGO-induced modulation of Cav2.2 variants by the various MORs. a Voltage-dependent and independent inhibition of Cav2.2-37a channels coexpressed with mMOR1, mMOR1C and mMOR1O. b Voltage-dependent and independent inhibition of Cav2.2-37b channels coexpressed with mMOR1, mMOR1C and mMOR1O. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05 and ***0.001 levels (t-test) between voltage-dependent and voltage-independent modulation for each receptor-channel combination

    Techniques Used: Inhibition

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    Primary antibodies used in the present study.
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    Schematic representation of <t>Cav2.2</t> channels and mMORs. a The Cav2.2 proximal C-terminus is in part encoded by the mutually exclusive exons 37a and 37b. The illustration shows the amino acids encoded by each exon. Shown in red is the tyrosine that was mutated for the experiments in Fig. . b MOR full-length distal C-terminal variants are produced by alternative splicing and amino acid sequences encoded by exon 4, 7 and 7–8-9 are depicted
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    Image Search Results


    Primary antibodies used in the present study.

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK

    doi: 10.12659/MSM.912862

    Figure Lengend Snippet: Primary antibodies used in the present study.

    Article Snippet: Rabbit anti-Cacna1b , 1: 1000 , Alomone Labs, Jerusalem, Israel.

    Techniques:

    Effects of knockdown ACAT1 on CACNAs, PKC, and ERK phosphorylation and in Aβ-induced SH-SY5Y cells. ( A ) Western blot results showed that the relative expression of CACNA1b and CACNA2d1 was increased significantly, while the total PKC and the ratio of phospho-ERK (p-ERK)/ERK were decreased significantly after Aβ 25-35 treatment. ( B ) Knockdown of ACAT1 rescued the reduction of PKC and phosphorylation level of ERK, and also retarded the upregulation of CACNA1b and CACNA2d1 induced by Aβ. (** P <0.01 and * P <0.05).

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Silencing the ACAT1 Gene in Human SH-SY5Y Neuroblastoma Cells Inhibits the Expression of Cyclo-Oxygenase 2 (COX2) and Reduces β-Amyloid-Induced Toxicity Due to Activation of Protein Kinase C (PKC) and ERK

    doi: 10.12659/MSM.912862

    Figure Lengend Snippet: Effects of knockdown ACAT1 on CACNAs, PKC, and ERK phosphorylation and in Aβ-induced SH-SY5Y cells. ( A ) Western blot results showed that the relative expression of CACNA1b and CACNA2d1 was increased significantly, while the total PKC and the ratio of phospho-ERK (p-ERK)/ERK were decreased significantly after Aβ 25-35 treatment. ( B ) Knockdown of ACAT1 rescued the reduction of PKC and phosphorylation level of ERK, and also retarded the upregulation of CACNA1b and CACNA2d1 induced by Aβ. (** P <0.01 and * P <0.05).

    Article Snippet: Rabbit anti-Cacna1b , 1: 1000 , Alomone Labs, Jerusalem, Israel.

    Techniques: Western Blot, Expressing

    Primer sequences.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Upregulation of N-Type Voltage-Gated Calcium Channels Induces Neuropathic Pain in Experimental Autoimmune Neuritis

    doi: 10.1155/2022/8547095

    Figure Lengend Snippet: Primer sequences.

    Article Snippet: On completion of a 1 h blocking step with 5% skimmed milk at ambient temperature, primary antibodies iNOS (ab49999, Abcam, UK), MCP-1 (ab7202, Abcam, UK), and Cav2.2 (ACC-002, AlomoneLabs, Israel) were served for overnight coincubation with the membrane at 4°C.

    Techniques: Sequencing

    Effect of Cav2.2 on clinical score and sciatic nerve tissue of rats. (a) Clinical score record of rats during 18 days of immunization; (b) changes in body weight of rats during 18 days of immunization; (c) luxol fast blue (LFB) staining-based observation of the degree of cell infiltration and demyelination in sciatic nerve tissue of rats on the 18 th day of immunization. ∗∗ P < 0.01 vs. control group, ## P < 0.01 vs. EAN-shRNA group.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Upregulation of N-Type Voltage-Gated Calcium Channels Induces Neuropathic Pain in Experimental Autoimmune Neuritis

    doi: 10.1155/2022/8547095

    Figure Lengend Snippet: Effect of Cav2.2 on clinical score and sciatic nerve tissue of rats. (a) Clinical score record of rats during 18 days of immunization; (b) changes in body weight of rats during 18 days of immunization; (c) luxol fast blue (LFB) staining-based observation of the degree of cell infiltration and demyelination in sciatic nerve tissue of rats on the 18 th day of immunization. ∗∗ P < 0.01 vs. control group, ## P < 0.01 vs. EAN-shRNA group.

    Article Snippet: On completion of a 1 h blocking step with 5% skimmed milk at ambient temperature, primary antibodies iNOS (ab49999, Abcam, UK), MCP-1 (ab7202, Abcam, UK), and Cav2.2 (ACC-002, AlomoneLabs, Israel) were served for overnight coincubation with the membrane at 4°C.

    Techniques: Staining, shRNA

    Effect of Cav2.2 on allodynia in rats. (a–d) Measurement of withdrawal threshold to mechanical (a), thermal (b), and cold (c) stimulation, and mechanical hyperalgesia threshold (d) during 18 days of immunization. ∗∗ P < 0.01 vs. Control group, ## P < 0.01 vs. EAN-shRNA group.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Upregulation of N-Type Voltage-Gated Calcium Channels Induces Neuropathic Pain in Experimental Autoimmune Neuritis

    doi: 10.1155/2022/8547095

    Figure Lengend Snippet: Effect of Cav2.2 on allodynia in rats. (a–d) Measurement of withdrawal threshold to mechanical (a), thermal (b), and cold (c) stimulation, and mechanical hyperalgesia threshold (d) during 18 days of immunization. ∗∗ P < 0.01 vs. Control group, ## P < 0.01 vs. EAN-shRNA group.

    Article Snippet: On completion of a 1 h blocking step with 5% skimmed milk at ambient temperature, primary antibodies iNOS (ab49999, Abcam, UK), MCP-1 (ab7202, Abcam, UK), and Cav2.2 (ACC-002, AlomoneLabs, Israel) were served for overnight coincubation with the membrane at 4°C.

    Techniques: shRNA

    Effect of Cav2.2 on rat inflammatory response. (a) ELISA-based measurement of IL-6 and TNF- α expression in rat serum; (b) qRT-PCR-based measurement of mRNA expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve; (c) western blot-based measurement of protein expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve. ∗ P < 0.05 and ∗∗ P < 0.01 vs. control group, # P < 0.05 and ## P < 0.01 vs. EAN-shRNA group.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Upregulation of N-Type Voltage-Gated Calcium Channels Induces Neuropathic Pain in Experimental Autoimmune Neuritis

    doi: 10.1155/2022/8547095

    Figure Lengend Snippet: Effect of Cav2.2 on rat inflammatory response. (a) ELISA-based measurement of IL-6 and TNF- α expression in rat serum; (b) qRT-PCR-based measurement of mRNA expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve; (c) western blot-based measurement of protein expression of iNOS, MCP-1, and Cav2.2 in rat sciatic nerve. ∗ P < 0.05 and ∗∗ P < 0.01 vs. control group, # P < 0.05 and ## P < 0.01 vs. EAN-shRNA group.

    Article Snippet: On completion of a 1 h blocking step with 5% skimmed milk at ambient temperature, primary antibodies iNOS (ab49999, Abcam, UK), MCP-1 (ab7202, Abcam, UK), and Cav2.2 (ACC-002, AlomoneLabs, Israel) were served for overnight coincubation with the membrane at 4°C.

    Techniques: Enzyme-linked Immunosorbent Assay, Expressing, Quantitative RT-PCR, Western Blot, shRNA

    Ca channel α 1 subunits co-express with the ganglion cell antibody RBPMS in vertical sections showing the inner plexiform layer (IPL), the ganglion cell layer (GCL) and the nerve fiber layer (NFL). ( Top row ) Double immunostaining with α1C subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). RGC axons (arrowhead) as well as putative Müller and neuronal cell processes in the IPL showed immunostaining. Control preadsorption of α1C antibody with the immunization peptide showed no staining. ( Second row ) Double immunostaining with α1D subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Numerous processes in the IPL as well as the RGC axons throughout the NFL (arrowhead) were also labelled. Control preadsorption of α1D antibody with the immunization peptide showed no staining. ( Third row ) Double immunostaining with α1B subunit and RBPMS antibodies shows colocalization in RGC somata (filled arrow). Processes in the IPL, putative displaced amacrine cells in the GCL (open arrows) and RGC axons throughout the NFL (arrowheads) showed immunostaining. Control preadsorption of α1B antibody with the immunization peptide showed no staining. ( Bottom row ) Double immunostaining with α1A subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Labelling in the IPL and in putative displaced amacrine cells in the GCL (open arrows) was also seen. Control preadsorption of α1A antibody with the immunization peptide showed no staining. Scale bar is 20 µm.

    Journal: PLoS ONE

    Article Title: Differential Calcium Signaling Mediated by Voltage-Gated Calcium Channels in Rat Retinal Ganglion Cells and Their Unmyelinated Axons

    doi: 10.1371/journal.pone.0084507

    Figure Lengend Snippet: Ca channel α 1 subunits co-express with the ganglion cell antibody RBPMS in vertical sections showing the inner plexiform layer (IPL), the ganglion cell layer (GCL) and the nerve fiber layer (NFL). ( Top row ) Double immunostaining with α1C subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). RGC axons (arrowhead) as well as putative Müller and neuronal cell processes in the IPL showed immunostaining. Control preadsorption of α1C antibody with the immunization peptide showed no staining. ( Second row ) Double immunostaining with α1D subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Numerous processes in the IPL as well as the RGC axons throughout the NFL (arrowhead) were also labelled. Control preadsorption of α1D antibody with the immunization peptide showed no staining. ( Third row ) Double immunostaining with α1B subunit and RBPMS antibodies shows colocalization in RGC somata (filled arrow). Processes in the IPL, putative displaced amacrine cells in the GCL (open arrows) and RGC axons throughout the NFL (arrowheads) showed immunostaining. Control preadsorption of α1B antibody with the immunization peptide showed no staining. ( Bottom row ) Double immunostaining with α1A subunit and RBPMS antibodies shows colocalization in the RGC somata (filled arrow). Labelling in the IPL and in putative displaced amacrine cells in the GCL (open arrows) was also seen. Control preadsorption of α1A antibody with the immunization peptide showed no staining. Scale bar is 20 µm.

    Article Snippet: The following polyclonal antibodies were used to obtain staining of the α1 subunits: α1C (Cav1.2, Alomone, ACC-003, 1∶1000, Jerusalem, Israel), α1D (Cav1.3, Sigma, C1728, St. Louis, MO, 1∶100), α1A (Cav2.1, Synaptic Systems, 152–103, 1∶7500, Göttingen, Germany), α1B (Cav2.2, Alomone, ACC-002, 1∶1000, Jerusalem, Israel).

    Techniques: Double Immunostaining, Immunostaining, Staining

    R at wholemount retina labelled with RBPMS (red), α1B VGCC subunit (green), and NF-M (white) antibodies. α1B colocalized with RBPMS in RGC somata (filled arrow), NF-M in RGC axons (arrowhead) and putative displaced amacrine cells (open arrow). Stack of six optical sections each of 0.3 µm thickness. Scale bar is 20 µm.

    Journal: PLoS ONE

    Article Title: Differential Calcium Signaling Mediated by Voltage-Gated Calcium Channels in Rat Retinal Ganglion Cells and Their Unmyelinated Axons

    doi: 10.1371/journal.pone.0084507

    Figure Lengend Snippet: R at wholemount retina labelled with RBPMS (red), α1B VGCC subunit (green), and NF-M (white) antibodies. α1B colocalized with RBPMS in RGC somata (filled arrow), NF-M in RGC axons (arrowhead) and putative displaced amacrine cells (open arrow). Stack of six optical sections each of 0.3 µm thickness. Scale bar is 20 µm.

    Article Snippet: The following polyclonal antibodies were used to obtain staining of the α1 subunits: α1C (Cav1.2, Alomone, ACC-003, 1∶1000, Jerusalem, Israel), α1D (Cav1.3, Sigma, C1728, St. Louis, MO, 1∶100), α1A (Cav2.1, Synaptic Systems, 152–103, 1∶7500, Göttingen, Germany), α1B (Cav2.2, Alomone, ACC-002, 1∶1000, Jerusalem, Israel).

    Techniques:

    Schematic representation of Cav2.2 channels and mMORs. a The Cav2.2 proximal C-terminus is in part encoded by the mutually exclusive exons 37a and 37b. The illustration shows the amino acids encoded by each exon. Shown in red is the tyrosine that was mutated for the experiments in Fig. . b MOR full-length distal C-terminal variants are produced by alternative splicing and amino acid sequences encoded by exon 4, 7 and 7–8-9 are depicted

    Journal: Molecular Brain

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    doi: 10.1186/s13041-019-0524-6

    Figure Lengend Snippet: Schematic representation of Cav2.2 channels and mMORs. a The Cav2.2 proximal C-terminus is in part encoded by the mutually exclusive exons 37a and 37b. The illustration shows the amino acids encoded by each exon. Shown in red is the tyrosine that was mutated for the experiments in Fig. . b MOR full-length distal C-terminal variants are produced by alternative splicing and amino acid sequences encoded by exon 4, 7 and 7–8-9 are depicted

    Article Snippet: Biotinylated proteins and lysates were resolved by SDS-PAGE and analyzed by western blot using the antibodies anti-Cav2.2 (1:500, Alomone ACC-002) and anti-Na/K ATPase (1:5000, Abcam AB 7671).

    Techniques: Produced

    Inhibition of Src and Cav2.2-37a Y1747F abolish the effect of mMOR1C on Cav2.2-37a peak current density. a Peak current density of Cav2.2-37a channels treated overnight with vehicle (0.1% water or 500 ng/ml of PTX overnight. b Peak current density of Cav2.2-37a channels treated for 4 h with vehicle (0.004% DMSO) or 2 μM of the Src inhibitor PP1. c Peak current density of the Cav2.2-37a Y1747F mutant in the absence and the presence of mMOR1C. The number of cells recorded is indicated in parentheses, asterisks denote significance at the *0.05 and **0.01 levels ( a and b – ANOVA, c - Mann-Whitney test)

    Journal: Molecular Brain

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    doi: 10.1186/s13041-019-0524-6

    Figure Lengend Snippet: Inhibition of Src and Cav2.2-37a Y1747F abolish the effect of mMOR1C on Cav2.2-37a peak current density. a Peak current density of Cav2.2-37a channels treated overnight with vehicle (0.1% water or 500 ng/ml of PTX overnight. b Peak current density of Cav2.2-37a channels treated for 4 h with vehicle (0.004% DMSO) or 2 μM of the Src inhibitor PP1. c Peak current density of the Cav2.2-37a Y1747F mutant in the absence and the presence of mMOR1C. The number of cells recorded is indicated in parentheses, asterisks denote significance at the *0.05 and **0.01 levels ( a and b – ANOVA, c - Mann-Whitney test)

    Article Snippet: Biotinylated proteins and lysates were resolved by SDS-PAGE and analyzed by western blot using the antibodies anti-Cav2.2 (1:500, Alomone ACC-002) and anti-Na/K ATPase (1:5000, Abcam AB 7671).

    Techniques: Inhibition, Mutagenesis, MANN-WHITNEY

    Peak current densities (I peak) of Cav2.2e37a and Cav2.2e37b channels coexpressed with mMOR1, mMOR1C or mMOR1O. a Representative whole cell current traces recorded in response to depolarizing steps from − 60 mV to + 40 mV from a holding potential of − 80 mV from tsA-201 cells expressing Cav2.2-37a/Cavβ1/Cavα2δ-1 or Cav2.2-37b /Cavβ1/Cavα2δ-1 channels plus/minus mMOR1C. b Average current density-voltage relationships for cells expressing Cav2.2-37a channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. c Average current density-voltage relationships for cells expressing Cav2.2-37b channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. d Average peak current density for whole cell calcium currents recorded from cells expressing Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O. e Average peak current density recorded from tsA-201 cells expressing Cav2.2e37b/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C or mMOR1O. The numbers in parentheses represent the number of cells recorded. n.s. – not significant, asterisks denote significance at the *0.05 and ***0.001 levels ( d – ANOVA; e - Kruskal-Wallis test)

    Journal: Molecular Brain

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    doi: 10.1186/s13041-019-0524-6

    Figure Lengend Snippet: Peak current densities (I peak) of Cav2.2e37a and Cav2.2e37b channels coexpressed with mMOR1, mMOR1C or mMOR1O. a Representative whole cell current traces recorded in response to depolarizing steps from − 60 mV to + 40 mV from a holding potential of − 80 mV from tsA-201 cells expressing Cav2.2-37a/Cavβ1/Cavα2δ-1 or Cav2.2-37b /Cavβ1/Cavα2δ-1 channels plus/minus mMOR1C. b Average current density-voltage relationships for cells expressing Cav2.2-37a channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. c Average current density-voltage relationships for cells expressing Cav2.2-37b channels with or without mMOR1C. Inset: Corresponding mean half activation potentials. d Average peak current density for whole cell calcium currents recorded from cells expressing Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O. e Average peak current density recorded from tsA-201 cells expressing Cav2.2e37b/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C or mMOR1O. The numbers in parentheses represent the number of cells recorded. n.s. – not significant, asterisks denote significance at the *0.05 and ***0.001 levels ( d – ANOVA; e - Kruskal-Wallis test)

    Article Snippet: Biotinylated proteins and lysates were resolved by SDS-PAGE and analyzed by western blot using the antibodies anti-Cav2.2 (1:500, Alomone ACC-002) and anti-Na/K ATPase (1:5000, Abcam AB 7671).

    Techniques: Expressing, Activation Assay

    Biotinylation of Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O.Biotinylated cell surface proteins were isolated and normalized to Na/K-ATPase levels. a Representative blot of Cav2.2-37a surface and total expression (top blots) and Na/K-ATPase surface and total expression (bottom blots). b Quantification of plasma membrane Cav2.2-37a/ Cavβ1/Cavα2δ-1 channel expression in the absence and the presence of mMOR1, mMOR1C or mMOR1O (normalized by Na/K-ATPase cell surface expression). c Quantification of total Cav2.2-37a/Cavβ1/Cavα2δ-1 expression in the absence or the presence of mMOR1, mMOR1C or mMOR1O (normalized by total Na/K-ATPase expression). d Normalized surface to total expression of Cav2.2-37a channels. Data are from 4 independent experiments. n.s. – not significant (Kruskal-Wallis test)

    Journal: Molecular Brain

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    doi: 10.1186/s13041-019-0524-6

    Figure Lengend Snippet: Biotinylation of Cav2.2e37a/Cavβ1/Cavα2δ-1 in the presence of mMOR1, mMOR1C and mMOR1O.Biotinylated cell surface proteins were isolated and normalized to Na/K-ATPase levels. a Representative blot of Cav2.2-37a surface and total expression (top blots) and Na/K-ATPase surface and total expression (bottom blots). b Quantification of plasma membrane Cav2.2-37a/ Cavβ1/Cavα2δ-1 channel expression in the absence and the presence of mMOR1, mMOR1C or mMOR1O (normalized by Na/K-ATPase cell surface expression). c Quantification of total Cav2.2-37a/Cavβ1/Cavα2δ-1 expression in the absence or the presence of mMOR1, mMOR1C or mMOR1O (normalized by total Na/K-ATPase expression). d Normalized surface to total expression of Cav2.2-37a channels. Data are from 4 independent experiments. n.s. – not significant (Kruskal-Wallis test)

    Article Snippet: Biotinylated proteins and lysates were resolved by SDS-PAGE and analyzed by western blot using the antibodies anti-Cav2.2 (1:500, Alomone ACC-002) and anti-Na/K ATPase (1:5000, Abcam AB 7671).

    Techniques: Isolation, Expressing

    G protein modulation of Cav2.2-37a and Cav2.2-37b channels following activation of mMOR1, mMOR1C and mMOR1O. a Representative set of Cav2.2-37a currents in the presence of mMOR1C, recorded before or after the application of 10 μM DAMGO. As outlined in the Results section, P1 represents the first current in each trace evoked by a test depolarization to + 10 mV, P2 is the second inward current in a given trace evoked by a 10 mV test depolarization (P2) preceded by a strong depolarizing prepulse (PP, note that the pre-pulse-evoked outward current is not shown in the figure). Relief of Gβγ modulation by the pre-pulse is observed by the increase in current amplitude seen during P2 in the presence of DAMGO. b Percentage of peak current inhibition (during P1) of Cav2.2e-37a currents after application of 10 μM DAMGO. c Percentage of peak current inhibition (during P1) of Cav2.2e-37b currents after application of 10 μM DAMGO. d Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37a channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by test pulse P2 normalized to the current evoked by test pulse P1. e Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37b channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by the test pulse P2 normalized to the current evoked by test pulse P1. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05, **0.01, and ***0.001 levels (unpaired Wilcoxon test)

    Journal: Molecular Brain

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    doi: 10.1186/s13041-019-0524-6

    Figure Lengend Snippet: G protein modulation of Cav2.2-37a and Cav2.2-37b channels following activation of mMOR1, mMOR1C and mMOR1O. a Representative set of Cav2.2-37a currents in the presence of mMOR1C, recorded before or after the application of 10 μM DAMGO. As outlined in the Results section, P1 represents the first current in each trace evoked by a test depolarization to + 10 mV, P2 is the second inward current in a given trace evoked by a 10 mV test depolarization (P2) preceded by a strong depolarizing prepulse (PP, note that the pre-pulse-evoked outward current is not shown in the figure). Relief of Gβγ modulation by the pre-pulse is observed by the increase in current amplitude seen during P2 in the presence of DAMGO. b Percentage of peak current inhibition (during P1) of Cav2.2e-37a currents after application of 10 μM DAMGO. c Percentage of peak current inhibition (during P1) of Cav2.2e-37b currents after application of 10 μM DAMGO. d Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37a channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by test pulse P2 normalized to the current evoked by test pulse P1. e Voltage dependent pre-pulse facilitation measured in the presence of DAMGO in tsA-201 cells expressing Cav2.2-37b channels with mMOR1, mMOR1C or mMOR1O. The data points reflect the current evoked by the test pulse P2 normalized to the current evoked by test pulse P1. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05, **0.01, and ***0.001 levels (unpaired Wilcoxon test)

    Article Snippet: Biotinylated proteins and lysates were resolved by SDS-PAGE and analyzed by western blot using the antibodies anti-Cav2.2 (1:500, Alomone ACC-002) and anti-Na/K ATPase (1:5000, Abcam AB 7671).

    Techniques: Activation Assay, Inhibition, Expressing

    Voltage dependent and voltage independent components of DAMGO-induced modulation of Cav2.2 variants by the various MORs. a Voltage-dependent and independent inhibition of Cav2.2-37a channels coexpressed with mMOR1, mMOR1C and mMOR1O. b Voltage-dependent and independent inhibition of Cav2.2-37b channels coexpressed with mMOR1, mMOR1C and mMOR1O. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05 and ***0.001 levels (t-test) between voltage-dependent and voltage-independent modulation for each receptor-channel combination

    Journal: Molecular Brain

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors

    doi: 10.1186/s13041-019-0524-6

    Figure Lengend Snippet: Voltage dependent and voltage independent components of DAMGO-induced modulation of Cav2.2 variants by the various MORs. a Voltage-dependent and independent inhibition of Cav2.2-37a channels coexpressed with mMOR1, mMOR1C and mMOR1O. b Voltage-dependent and independent inhibition of Cav2.2-37b channels coexpressed with mMOR1, mMOR1C and mMOR1O. The number of cells recorded are indicated in parentheses, asterisks denote significance at the *0.05 and ***0.001 levels (t-test) between voltage-dependent and voltage-independent modulation for each receptor-channel combination

    Article Snippet: Biotinylated proteins and lysates were resolved by SDS-PAGE and analyzed by western blot using the antibodies anti-Cav2.2 (1:500, Alomone ACC-002) and anti-Na/K ATPase (1:5000, Abcam AB 7671).

    Techniques: Inhibition