anti cav2 1  (Alomone Labs)


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    Name:
    Anti CACNA1A Cav2 1 Antibody
    Description:
    Anti CACNA1A CaV2 1 Antibody ACC 001 is a highly specific antibody directed against an epitope of the rat protein The antibody can be used in western blot immunohistochemistry and immunocytochemistry applications It has been designed to recognize CaV2 1 from mouse rat and human samples
    Catalog Number:
    ACC-001
    Price:
    397.0
    Category:
    Primary Antibody
    Applications:
    Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Western Blot
    Purity:
    Affinity purified on immobilized antigen.
    Immunogen:
    Synthetic peptide
    Size:
    25 mcl
    Antibody Type:
    Polyclonal Primary Antibodies
    Format:
    Lyophilized Powder
    Host:
    Rabbit
    Isotype:
    Rabbit IgG
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    Structured Review

    Alomone Labs anti cav2 1
    Anti CACNA1A Cav2 1 Antibody
    Anti CACNA1A CaV2 1 Antibody ACC 001 is a highly specific antibody directed against an epitope of the rat protein The antibody can be used in western blot immunohistochemistry and immunocytochemistry applications It has been designed to recognize CaV2 1 from mouse rat and human samples
    https://www.bioz.com/result/anti cav2 1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti cav2 1 - by Bioz Stars, 2021-09
    93/100 stars

    Images

    1) Product Images from "New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons"

    Article Title: New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2018.00342

    Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP.  (A)  Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm.  (B)  Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n  = 19) and  (C)  in neurites ( n  = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP.  (D)  Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al.,   2015 ).
    Figure Legend Snippet: Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP. (A) Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm. (B) Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n = 19) and (C) in neurites ( n = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP. (D) Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al., 2015 ).

    Techniques Used: Immunoprecipitation

    Ca v 2.1 protein is mis-expressed at the plasma membrane of  Fmr1 -KO cortical neurons.  (A)  Western blot analysis of biotinylated Ca v 2.1 in DIV 15–19 cortical neurons. β-tubulin is used as the loading control, whereas actin is used as the immunoprecipitation control.  (B)  Quantification of total and cell-surface Ca v 2.1 protein levels. Results are presented as the mean ± SEM, Mann-Whitney test: * P
    Figure Legend Snippet: Ca v 2.1 protein is mis-expressed at the plasma membrane of Fmr1 -KO cortical neurons. (A) Western blot analysis of biotinylated Ca v 2.1 in DIV 15–19 cortical neurons. β-tubulin is used as the loading control, whereas actin is used as the immunoprecipitation control. (B) Quantification of total and cell-surface Ca v 2.1 protein levels. Results are presented as the mean ± SEM, Mann-Whitney test: * P

    Techniques Used: Western Blot, Immunoprecipitation, MANN-WHITNEY

    2) Product Images from "Stimulation of Synaptic Vesicle Exocytosis by the Mental Disease Gene DISC1 is Mediated by N-Type Voltage-Gated Calcium Channels"

    Article Title: Stimulation of Synaptic Vesicle Exocytosis by the Mental Disease Gene DISC1 is Mediated by N-Type Voltage-Gated Calcium Channels

    Journal: Frontiers in Synaptic Neuroscience

    doi: 10.3389/fnsyn.2016.00015

    DISC1 regulates Cav2.2-dependent SV exocytosis. (A) Average vGpH traces in scr (101 boutons, 6 fields, 2 exps) and DISC1-E (87 boutons, 5 fields, 2 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.2 blocker ω-Conotoxin GVIA (125 nM). (B) Boxplot of SV exocytic rates before and after ω-Conotoxin GVIA application. Exocytic rates were measured by linear fitting of the first six time points of the vGpH response. (C) Average vGpH traces in scr (1294 boutons, 9 fields, 3 exps) and DISC1-E (1282 boutons, 9 fields, 3 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.1 blocker ω-Agatoxin TK (125 nM). (D) Boxplot of SV exocytic rates before and after ω-Agatoxin TK application. (E) Table showing the percentage of inhibition of exocytosis rate by DISC1 knockdown before and after Cav2.2- or Cav2.1 blockade.
    Figure Legend Snippet: DISC1 regulates Cav2.2-dependent SV exocytosis. (A) Average vGpH traces in scr (101 boutons, 6 fields, 2 exps) and DISC1-E (87 boutons, 5 fields, 2 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.2 blocker ω-Conotoxin GVIA (125 nM). (B) Boxplot of SV exocytic rates before and after ω-Conotoxin GVIA application. Exocytic rates were measured by linear fitting of the first six time points of the vGpH response. (C) Average vGpH traces in scr (1294 boutons, 9 fields, 3 exps) and DISC1-E (1282 boutons, 9 fields, 3 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.1 blocker ω-Agatoxin TK (125 nM). (D) Boxplot of SV exocytic rates before and after ω-Agatoxin TK application. (E) Table showing the percentage of inhibition of exocytosis rate by DISC1 knockdown before and after Cav2.2- or Cav2.1 blockade.

    Techniques Used: shRNA, Expressing, Inhibition

    DISC1 enhances Cav2.2 and Cav2.1 currents. (A) Western blot showing expression of ectopic (human) DISC1 in HEK293 cells. (B,C) Cav2.2 Current-voltage (I-V) curves for hDISC1-expressing and control cells. (B) Stimulation protocol and individual current responses shown at three different voltages (−30, 0 and 30 mV) (C) . Average I-V plots for hDISC1 (peak = 54.2 ± 4.5 pA/pF, 13 cells) and control (peak = 39.2 ± 4.9 pA/pF, 12 cells), p = 0.033. (D–F) Cav2.2 activation curves in response to the tail protocol. (D) Illustration of the tail protocol and individual tail currents measured at −50 mV after three different voltage steps (−20, 0 and 40 mV). (E) Average current density based on tail currents for DISC1 (164.3 ± 7.3 pA/pF, 12 cells) and control (110.5 ± 6.3 pA/pF, 12 cells), * p
    Figure Legend Snippet: DISC1 enhances Cav2.2 and Cav2.1 currents. (A) Western blot showing expression of ectopic (human) DISC1 in HEK293 cells. (B,C) Cav2.2 Current-voltage (I-V) curves for hDISC1-expressing and control cells. (B) Stimulation protocol and individual current responses shown at three different voltages (−30, 0 and 30 mV) (C) . Average I-V plots for hDISC1 (peak = 54.2 ± 4.5 pA/pF, 13 cells) and control (peak = 39.2 ± 4.9 pA/pF, 12 cells), p = 0.033. (D–F) Cav2.2 activation curves in response to the tail protocol. (D) Illustration of the tail protocol and individual tail currents measured at −50 mV after three different voltage steps (−20, 0 and 40 mV). (E) Average current density based on tail currents for DISC1 (164.3 ± 7.3 pA/pF, 12 cells) and control (110.5 ± 6.3 pA/pF, 12 cells), * p

    Techniques Used: Western Blot, Expressing, Activation Assay

    3) Product Images from "The sorting receptor Rer1 controls Purkinje cell function via voltage gated sodium channels"

    Article Title: The sorting receptor Rer1 controls Purkinje cell function via voltage gated sodium channels

    Journal: Scientific Reports

    doi: 10.1038/srep41248

    Absence of Rer1 reduces Na v  protein levels. ( a ) Brain lysates of Rer1 Δbrain  (ko) and control littermates (wt) of different ages as indicated were separated by SDS-PAGE, blotted and probed with indicated antibodies. In the Ca v 2.1 blot the irrelevant lane #7 was removed and the two last lanes flipped vertically, to match loading of the other gels. See full-length blot in the  supplemental Fig. 5 . P38, synaptophysin. ( b ) De-glycosylation of Na v 1.1 and 1.6 indicates maturation status of the different bands. Brain lysates of P15 wt mice were subjected to de-glycosylation with endoglycosidase H (H) or PNGaseF (F) and processed for Western Blotting with Na v 1.1 and 1.6 antibodies. Im, immature (endoH sensitive); m, mature (endoH resistant); degl, de-glycosylated Na v 1.1 or 1.6 after PNGase F digest. In a, b cropped blots are shown, full-length blots are shown in  supplemental Figs 5,6 .
    Figure Legend Snippet: Absence of Rer1 reduces Na v protein levels. ( a ) Brain lysates of Rer1 Δbrain (ko) and control littermates (wt) of different ages as indicated were separated by SDS-PAGE, blotted and probed with indicated antibodies. In the Ca v 2.1 blot the irrelevant lane #7 was removed and the two last lanes flipped vertically, to match loading of the other gels. See full-length blot in the supplemental Fig. 5 . P38, synaptophysin. ( b ) De-glycosylation of Na v 1.1 and 1.6 indicates maturation status of the different bands. Brain lysates of P15 wt mice were subjected to de-glycosylation with endoglycosidase H (H) or PNGaseF (F) and processed for Western Blotting with Na v 1.1 and 1.6 antibodies. Im, immature (endoH sensitive); m, mature (endoH resistant); degl, de-glycosylated Na v 1.1 or 1.6 after PNGase F digest. In a, b cropped blots are shown, full-length blots are shown in supplemental Figs 5,6 .

    Techniques Used: SDS Page, Mouse Assay, Western Blot

    4) Product Images from "New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons"

    Article Title: New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2018.00342

    Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP.  (A)  Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm.  (B)  Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n  = 19) and  (C)  in neurites ( n  = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP.  (D)  Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al.,   2015 ).
    Figure Legend Snippet: Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP. (A) Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm. (B) Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n = 19) and (C) in neurites ( n = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP. (D) Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al., 2015 ).

    Techniques Used: Immunoprecipitation

    Ca v 2.1 protein is mis-expressed at the plasma membrane of  Fmr1 -KO cortical neurons.  (A)  Western blot analysis of biotinylated Ca v 2.1 in DIV 15–19 cortical neurons. β-tubulin is used as the loading control, whereas actin is used as the immunoprecipitation control.  (B)  Quantification of total and cell-surface Ca v 2.1 protein levels. Results are presented as the mean ± SEM, Mann-Whitney test: * P
    Figure Legend Snippet: Ca v 2.1 protein is mis-expressed at the plasma membrane of Fmr1 -KO cortical neurons. (A) Western blot analysis of biotinylated Ca v 2.1 in DIV 15–19 cortical neurons. β-tubulin is used as the loading control, whereas actin is used as the immunoprecipitation control. (B) Quantification of total and cell-surface Ca v 2.1 protein levels. Results are presented as the mean ± SEM, Mann-Whitney test: * P

    Techniques Used: Western Blot, Immunoprecipitation, MANN-WHITNEY

    Related Articles

    Incubation:

    Article Title: New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons
    Article Snippet: .. Primary antibodies anti ß-Actin (Sigma, clone AC-74; 1/1,000) and anti-Cav2.1 (Alomone Labs, #ACC-001; 1/1,000) were incubated overnight at 4°C in PBS 0.05%. ..

    Article Title: Sleep deprivation of rats increases postsurgical expression and activity of L-type calcium channel in the dorsal root ganglion and slows recovery from postsurgical pain
    Article Snippet: .. The membranes were blocked with 1% bovine serum albumin (BSA) at 4 °C overnight, and then incubated with rabbit anti-Cav 1.2 antibody (L-type; 1:200, ACC-003, Alomone), rabbit anti-Cav 2.1 antibody (P/Q-type; 1:200, ACC-001, Alomone), rabbit anti-Cav 2.2 antibody (N-type; 1:200, ACC-002, Alomone), rabbit anti-Cav 2.3 antibody (R-type; 1:200, ACC-006, Alomone), rabbit anti-Cav3.2 antibody (T-type; 1:200, ACC-001, Alomone), mouse anti-Egr1 antibody(1:200, sc-101,033, Santa Cruz), or rabbit beta tubulin antibody (1:3000, AB0039, Abways) at 4 °C overnight under gentle agitation. ..

    other:

    Article Title: Ankyrin B and Ankyrin B variants differentially modulate intracellular and surface Cav2.1 levels
    Article Snippet: Antibodies Primary antibodies used included anti-Cav2.1 (1:500, Alomone Labs), anti-GFP rabbit polyclonal (1:2000, Invitrogen/Thermo Fisher Scientific), anti-GAPDH (1:3000, Novus Biologicals), anti-transferrin receptor (1:1000, Invitrogen/Thermo Scientific), anti-CACNA2D1 (1:1000, Abcam), anti-Cavβ4 (1:1000, Neuromab), anti-AnkB (1:500, Thermo Fisher Scientific), and anti-syntaxin 1A (1:5000, Millipore Sigma).

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  • 93
    Alomone Labs anti cav2 1
    Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP.  (A)  Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm.  (B)  Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n  = 19) and  (C)  in neurites ( n  = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP.  (D)  Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al.,   2015 ).
    Anti Cav2 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
    https://www.bioz.com/result/anti cav2 1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti cav2 1 - by Bioz Stars, 2021-09
    93/100 stars
      Buy from Supplier

    Image Search Results


    Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP.  (A)  Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm.  (B)  Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n  = 19) and  (C)  in neurites ( n  = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP.  (D)  Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al.,   2015 ).

    Journal: Frontiers in Molecular Neuroscience

    Article Title: New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons

    doi: 10.3389/fnmol.2018.00342

    Figure Lengend Snippet: Endogenous Ca v 2.1 interacts and partially co-localizes with FMRP. (A) Single plane confocal analysis of FMRP (revealed with the 1C3 antibody) and Ca v 2.1 (revealed with the antibody anti-Ca v 2.1) localization in DIV 13 primary neuronal cultures. The scale bar of each panel is 50 μm. (B) Quantification of the colocalization of FMRP and Ca v 2.1 in the soma ( n = 19) and (C) in neurites ( n = 14) was performed with the JACoP plugin for ImageJ. CC, correlation coefficient; M1, fraction of FMRP overlapping with Ca v 2.1; M2, fraction of Ca v 2.1 overlapping with FMRP. (D) Endogeneous FMRP co-immunoprecipitation with Ca v 2.1 in mouse cerebellar extracts. FMRP was revealed with the 1R antibody (Bonaccorso et al., 2015 ).

    Article Snippet: Primary antibodies anti ß-Actin (Sigma, #A5441; 1/1,000), anti-Cav2.1 (Alomone Labs, #ACC-001; 1/1,000) and anti ß3-tubulin (Synaptic Systems, #302302; 1/1,000) were used.

    Techniques: Immunoprecipitation

    Ca v 2.1 protein is mis-expressed at the plasma membrane of  Fmr1 -KO cortical neurons.  (A)  Western blot analysis of biotinylated Ca v 2.1 in DIV 15–19 cortical neurons. β-tubulin is used as the loading control, whereas actin is used as the immunoprecipitation control.  (B)  Quantification of total and cell-surface Ca v 2.1 protein levels. Results are presented as the mean ± SEM, Mann-Whitney test: * P

    Journal: Frontiers in Molecular Neuroscience

    Article Title: New Insights Into the Role of Cav2 Protein Family in Calcium Flux Deregulation in Fmr1-KO Neurons

    doi: 10.3389/fnmol.2018.00342

    Figure Lengend Snippet: Ca v 2.1 protein is mis-expressed at the plasma membrane of Fmr1 -KO cortical neurons. (A) Western blot analysis of biotinylated Ca v 2.1 in DIV 15–19 cortical neurons. β-tubulin is used as the loading control, whereas actin is used as the immunoprecipitation control. (B) Quantification of total and cell-surface Ca v 2.1 protein levels. Results are presented as the mean ± SEM, Mann-Whitney test: * P

    Article Snippet: Primary antibodies anti ß-Actin (Sigma, #A5441; 1/1,000), anti-Cav2.1 (Alomone Labs, #ACC-001; 1/1,000) and anti ß3-tubulin (Synaptic Systems, #302302; 1/1,000) were used.

    Techniques: Western Blot, Immunoprecipitation, MANN-WHITNEY

    DISC1 regulates Cav2.2-dependent SV exocytosis. (A) Average vGpH traces in scr (101 boutons, 6 fields, 2 exps) and DISC1-E (87 boutons, 5 fields, 2 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.2 blocker ω-Conotoxin GVIA (125 nM). (B) Boxplot of SV exocytic rates before and after ω-Conotoxin GVIA application. Exocytic rates were measured by linear fitting of the first six time points of the vGpH response. (C) Average vGpH traces in scr (1294 boutons, 9 fields, 3 exps) and DISC1-E (1282 boutons, 9 fields, 3 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.1 blocker ω-Agatoxin TK (125 nM). (D) Boxplot of SV exocytic rates before and after ω-Agatoxin TK application. (E) Table showing the percentage of inhibition of exocytosis rate by DISC1 knockdown before and after Cav2.2- or Cav2.1 blockade.

    Journal: Frontiers in Synaptic Neuroscience

    Article Title: Stimulation of Synaptic Vesicle Exocytosis by the Mental Disease Gene DISC1 is Mediated by N-Type Voltage-Gated Calcium Channels

    doi: 10.3389/fnsyn.2016.00015

    Figure Lengend Snippet: DISC1 regulates Cav2.2-dependent SV exocytosis. (A) Average vGpH traces in scr (101 boutons, 6 fields, 2 exps) and DISC1-E (87 boutons, 5 fields, 2 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.2 blocker ω-Conotoxin GVIA (125 nM). (B) Boxplot of SV exocytic rates before and after ω-Conotoxin GVIA application. Exocytic rates were measured by linear fitting of the first six time points of the vGpH response. (C) Average vGpH traces in scr (1294 boutons, 9 fields, 3 exps) and DISC1-E (1282 boutons, 9 fields, 3 exps) shRNA-expressing neurons during consecutive trains of APs (300 AP, 10 Hz) in the absence or presence of the Cav2.1 blocker ω-Agatoxin TK (125 nM). (D) Boxplot of SV exocytic rates before and after ω-Agatoxin TK application. (E) Table showing the percentage of inhibition of exocytosis rate by DISC1 knockdown before and after Cav2.2- or Cav2.1 blockade.

    Article Snippet: The rabbit polyclonal Abs against Cav2.1 (#ACC-001) and Cav2.2 (#ACC-002) were from Alomone Labs.

    Techniques: shRNA, Expressing, Inhibition

    DISC1 enhances Cav2.2 and Cav2.1 currents. (A) Western blot showing expression of ectopic (human) DISC1 in HEK293 cells. (B,C) Cav2.2 Current-voltage (I-V) curves for hDISC1-expressing and control cells. (B) Stimulation protocol and individual current responses shown at three different voltages (−30, 0 and 30 mV) (C) . Average I-V plots for hDISC1 (peak = 54.2 ± 4.5 pA/pF, 13 cells) and control (peak = 39.2 ± 4.9 pA/pF, 12 cells), p = 0.033. (D–F) Cav2.2 activation curves in response to the tail protocol. (D) Illustration of the tail protocol and individual tail currents measured at −50 mV after three different voltage steps (−20, 0 and 40 mV). (E) Average current density based on tail currents for DISC1 (164.3 ± 7.3 pA/pF, 12 cells) and control (110.5 ± 6.3 pA/pF, 12 cells), * p

    Journal: Frontiers in Synaptic Neuroscience

    Article Title: Stimulation of Synaptic Vesicle Exocytosis by the Mental Disease Gene DISC1 is Mediated by N-Type Voltage-Gated Calcium Channels

    doi: 10.3389/fnsyn.2016.00015

    Figure Lengend Snippet: DISC1 enhances Cav2.2 and Cav2.1 currents. (A) Western blot showing expression of ectopic (human) DISC1 in HEK293 cells. (B,C) Cav2.2 Current-voltage (I-V) curves for hDISC1-expressing and control cells. (B) Stimulation protocol and individual current responses shown at three different voltages (−30, 0 and 30 mV) (C) . Average I-V plots for hDISC1 (peak = 54.2 ± 4.5 pA/pF, 13 cells) and control (peak = 39.2 ± 4.9 pA/pF, 12 cells), p = 0.033. (D–F) Cav2.2 activation curves in response to the tail protocol. (D) Illustration of the tail protocol and individual tail currents measured at −50 mV after three different voltage steps (−20, 0 and 40 mV). (E) Average current density based on tail currents for DISC1 (164.3 ± 7.3 pA/pF, 12 cells) and control (110.5 ± 6.3 pA/pF, 12 cells), * p

    Article Snippet: The rabbit polyclonal Abs against Cav2.1 (#ACC-001) and Cav2.2 (#ACC-002) were from Alomone Labs.

    Techniques: Western Blot, Expressing, Activation Assay

    Absence of Rer1 reduces Na v  protein levels. ( a ) Brain lysates of Rer1 Δbrain  (ko) and control littermates (wt) of different ages as indicated were separated by SDS-PAGE, blotted and probed with indicated antibodies. In the Ca v 2.1 blot the irrelevant lane #7 was removed and the two last lanes flipped vertically, to match loading of the other gels. See full-length blot in the  supplemental Fig. 5 . P38, synaptophysin. ( b ) De-glycosylation of Na v 1.1 and 1.6 indicates maturation status of the different bands. Brain lysates of P15 wt mice were subjected to de-glycosylation with endoglycosidase H (H) or PNGaseF (F) and processed for Western Blotting with Na v 1.1 and 1.6 antibodies. Im, immature (endoH sensitive); m, mature (endoH resistant); degl, de-glycosylated Na v 1.1 or 1.6 after PNGase F digest. In a, b cropped blots are shown, full-length blots are shown in  supplemental Figs 5,6 .

    Journal: Scientific Reports

    Article Title: The sorting receptor Rer1 controls Purkinje cell function via voltage gated sodium channels

    doi: 10.1038/srep41248

    Figure Lengend Snippet: Absence of Rer1 reduces Na v protein levels. ( a ) Brain lysates of Rer1 Δbrain (ko) and control littermates (wt) of different ages as indicated were separated by SDS-PAGE, blotted and probed with indicated antibodies. In the Ca v 2.1 blot the irrelevant lane #7 was removed and the two last lanes flipped vertically, to match loading of the other gels. See full-length blot in the supplemental Fig. 5 . P38, synaptophysin. ( b ) De-glycosylation of Na v 1.1 and 1.6 indicates maturation status of the different bands. Brain lysates of P15 wt mice were subjected to de-glycosylation with endoglycosidase H (H) or PNGaseF (F) and processed for Western Blotting with Na v 1.1 and 1.6 antibodies. Im, immature (endoH sensitive); m, mature (endoH resistant); degl, de-glycosylated Na v 1.1 or 1.6 after PNGase F digest. In a, b cropped blots are shown, full-length blots are shown in supplemental Figs 5,6 .

    Article Snippet: Anti-Rer1, rabbit polyclonal SA5457 and SPY008 ; anti-calbindin-D-28K, mouse monoclonal (C-9848), anti-MAP2 mouse monoclonal M4403 and anti-GFAP, rabbit polyclonal (G-9269), all from Sigma; anti-Nav1.6 (ASC-009), anti-Nav1.1 (ASC-001), anti-Cav2.1 (ACC-001), anti-Kv1.1 (APC-009), anti-Kv3.3 (APC-102) and anti-Kv7.2 (APC-050), all rabbit polyclonal from Alomone Labs; anti-ankyrin G mouse monoclonal (sc-12719), Santa Cruz Biotechnology; anti-Scn1b, rabbit polyclonal (AP53815 PU-N), Acris; anti-APP, mouse monoclonal (MAB348), Millipore; anti-PSD-95, mouse monoclonal (6G6-1C9, VAM-PS002), Assay Designs; anti-KCC2, rabbit polyclonal (07–432) and anti-synaptophysin mouse monoclonal (MAB368) both from Millipore, anti-GM130, mouse monoclonal (610822) BD Transduction Laboratories; anti-Sstr3, rabbit polyclonal antibody kindly obtained from Stefan Schulz, Jena ; Alexa Fluor-labeled secondary antibodies, Molecular Probes, HRP-conjugated secondary antibodies, Promega.

    Techniques: SDS Page, Mouse Assay, Western Blot