girk1  (Alomone Labs)


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    Name:
    Anti GIRK1 Kir3 1 Antibody
    Description:
    Anti GIRK1 Kir3 1 Antibody APC 005 is a highly specific antibody directed against an epitope of the mouse protein The antibody can be used in western blot immunprecipitation immunocytochemistry and immunohistochemistry applications It has been designed to recognize Kir3 1 from human rat and mouse samples
    Catalog Number:
    APC-005
    Price:
    397.0
    Category:
    Primary Antibody
    Applications:
    Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot
    Purity:
    The serum was depleted of anti-GST antibodies by affinity chromatography on immobilized GST and then the IgG fraction was purified on immobilized antigen.
    Immunogen:
    GST fusion protein
    Size:
    25 mcl
    Antibody Type:
    Polyclonal Primary Antibodies
    Format:
    Lyophilized Powder
    Host:
    Rabbit
    Isotype:
    Rabbit IgG
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    Structured Review

    Alomone Labs girk1
    Anti GIRK1 Kir3 1 Antibody
    Anti GIRK1 Kir3 1 Antibody APC 005 is a highly specific antibody directed against an epitope of the mouse protein The antibody can be used in western blot immunprecipitation immunocytochemistry and immunohistochemistry applications It has been designed to recognize Kir3 1 from human rat and mouse samples
    https://www.bioz.com/result/girk1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    girk1 - by Bioz Stars, 2021-10
    94/100 stars

    Images

    1) Product Images from "GIRK2 splice variants and neuronal G protein-gated K+ channels: implications for channel function and behavior"

    Article Title: GIRK2 splice variants and neuronal G protein-gated K+ channels: implications for channel function and behavior

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-01820-2

    Functional comparison of GIRK2a and GIRK2c in HEK cells. ( A ) Whole-cell currents (V hold = −70 mV) evoked by baclofen (100 μM) in HEK cells expressing GABA B R, GIRK1, and either GIRK2a (red) or GIRK2c (blue). No current was evoked by baclofen in cells expressing only GABA B R (control, black). Scale: 500 pA/10 s. ( B ) Summary of baclofen-induced, steady-state current densities (I baclofen , pA/pF) in HEK cells expressing GIRK1/GIRK2a or GIRK1/GIRK2c ( t 19 = 1.1, P = 0.29; n = 10–11/group). Individual data points are represented as small squares overlapping the relevant bar in the plot. ( C,D ) Activation ( t 19 = 1.5, P = 0.16) and deactivation ( t 16 = 0.4, P = 0.72) kinetics for baclofen-induced currents in HEK cells expressing GIRK1/GIRK2a or GIRK1/GIRK2c (n = 9–11/group). ( E ) Representative concentration-response experiment for a HEK cell expressing GABA B R and GIRK1/GIRK2c. Scale: 500 pA/10 s. ( F,G ) Summary of concentration-response experiments for baclofen-induced currents in HEK cells expressing GIRK1/GIRK2a or GIRK1/GIRK2c ( t 17 = 1.0, P = 0.32; n = 9–10/group). Currents were normalized to the response evoked by 100 μM baclofen in each experiment.
    Figure Legend Snippet: Functional comparison of GIRK2a and GIRK2c in HEK cells. ( A ) Whole-cell currents (V hold = −70 mV) evoked by baclofen (100 μM) in HEK cells expressing GABA B R, GIRK1, and either GIRK2a (red) or GIRK2c (blue). No current was evoked by baclofen in cells expressing only GABA B R (control, black). Scale: 500 pA/10 s. ( B ) Summary of baclofen-induced, steady-state current densities (I baclofen , pA/pF) in HEK cells expressing GIRK1/GIRK2a or GIRK1/GIRK2c ( t 19 = 1.1, P = 0.29; n = 10–11/group). Individual data points are represented as small squares overlapping the relevant bar in the plot. ( C,D ) Activation ( t 19 = 1.5, P = 0.16) and deactivation ( t 16 = 0.4, P = 0.72) kinetics for baclofen-induced currents in HEK cells expressing GIRK1/GIRK2a or GIRK1/GIRK2c (n = 9–11/group). ( E ) Representative concentration-response experiment for a HEK cell expressing GABA B R and GIRK1/GIRK2c. Scale: 500 pA/10 s. ( F,G ) Summary of concentration-response experiments for baclofen-induced currents in HEK cells expressing GIRK1/GIRK2a or GIRK1/GIRK2c ( t 17 = 1.0, P = 0.32; n = 9–10/group). Currents were normalized to the response evoked by 100 μM baclofen in each experiment.

    Techniques Used: Functional Assay, Expressing, Activation Assay, Concentration Assay

    2) Product Images from "Activation and inhibition of G protein-coupled inwardly rectifying potassium (Kir3) channels by G protein ?? subunits"

    Article Title: Activation and inhibition of G protein-coupled inwardly rectifying potassium (Kir3) channels by G protein ?? subunits

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi:

    Gβ5-containing dimers inhibit basal GIRK1,4 currents and bind to GIRK1,4 channel cytoplasmic domains. ( A ) Sample current traces from control cells and G1,4 cells expressing either β1γ2 or β5γ2. Inwardly rectifying current was enhanced by β1γ2 but inhibited by β5γ2. ( Inset ) Conductance (±SEM) is decreased in cells transfected with β5γ2 or β5γ11. *, Statistically significant differences from control. *, Significantly different from control ( P
    Figure Legend Snippet: Gβ5-containing dimers inhibit basal GIRK1,4 currents and bind to GIRK1,4 channel cytoplasmic domains. ( A ) Sample current traces from control cells and G1,4 cells expressing either β1γ2 or β5γ2. Inwardly rectifying current was enhanced by β1γ2 but inhibited by β5γ2. ( Inset ) Conductance (±SEM) is decreased in cells transfected with β5γ2 or β5γ11. *, Statistically significant differences from control. *, Significantly different from control ( P

    Techniques Used: Expressing, Transfection

    Related Articles

    Incubation:

    Article Title: Increased ACh-Associated Immunoreactivity in Autonomic Centers in PTZ Kindling Model of Epilepsy
    Article Snippet: .. Immediately, Kir3.1 (mouse monoclonal, 1:200, Alomone Labs, Jerusalem, Israel [APC-005]) and M2 receptor (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel [APC-002]) primary antibodies were dropped and kept at +4 °C for one night and incubated the next day for 20 min. As a negative control, PBS was used instead of the primary antibody. ..

    Article Title: Unraveling the Role of Inwardly Rectifying Potassium Channels in the Hippocampus of an Aβ(1–42)-Infused Rat Model of Alzheimer’s Disease
    Article Snippet: .. Then, the membranes were blocked with 5% milk solution prepared in TBST (Tris-buffered saline, 0.1% Tween 20) buffer and incubated with one of the following primary antibodies against Kir2.1 (rabbit polyclonal, 1:200, Abcam, Cambridge, UK [ab65796]), Kir3.1 (mouse monoclonal, 1:200, Alomone Labs, Jerusalem, Israel [APC-005]), Kir6.2 (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel [APC-020]), or β-actin (mouse monoclonal, 1:5000, Thermo Fisher Scientific, Waltham, MA, USA [AC-15]). ..

    Article Title: Immunoreactivity of Muscarinic Acetylcholine M2 and Serotonin 5-HT2B Receptors, Norepinephrine Transporter and Kir Channels in a Model of Epilepsy
    Article Snippet: .. Primary antibodies against Kir3.1 (mouse monoclonal, 1:200, Alomone Labs, Jerusalem, Israel (APC-005)), Kir6.2 (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel (APC-020)), muscarinic acetylcholine receptor M2, mAChR (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel (APC-002)), norepinephrine transporter (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel (AMT-002)) and serotonin receptor 2B (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel (ASR-035)) were diluted in PBS and incubated with the slides at 4 °C. ..

    Negative Control:

    Article Title: Increased ACh-Associated Immunoreactivity in Autonomic Centers in PTZ Kindling Model of Epilepsy
    Article Snippet: .. Immediately, Kir3.1 (mouse monoclonal, 1:200, Alomone Labs, Jerusalem, Israel [APC-005]) and M2 receptor (rabbit polyclonal, 1:200, Alomone Labs, Jerusalem, Israel [APC-002]) primary antibodies were dropped and kept at +4 °C for one night and incubated the next day for 20 min. As a negative control, PBS was used instead of the primary antibody. ..

    Produced:

    Article Title: GIRK1 triggers multiple cancer-related pathways in the benign mammary epithelial cell line MCF10A
    Article Snippet: .. The following combinations of primary and secondary antibodies were used: #1.: GIRK1CT Ab (APC-005, directed against GIRK1 C-terminus; Alomone labs, Jerusalem, Israel, rabbit polyclonal) dilution 1:800 in 5% [w/v] BSA with Peroxidase Goat anti-rabbit as secondary Ab (1:10000 in 3% [w/v] skim milk); #2.: GIRK1NT Ab (directed against GIRK1 N-terminus; rabbit polyclonal, produced by Kurt Schmidt, dilution 1:250 in 5% [w/v] BSA) with Clean Blot IP detection reagent as secondary Ab (1:5000 in 3% [w/v] skim milk); #3.: monoclonal GIRK1 Ab (Abcam No. 119246) mouse monoclonal (dilution 1:500 in 5% [w/v] BSA) with Peroxidase Goat anti-mouse as secondary Ab (1:10000 in 3% [w/v] skim milk). ..

    Nucleic Acid Electrophoresis:

    Article Title: DNA damage-induced PARP1 activation confers cardiomyocyte dysfunction through NAD+ depletion in experimental atrial fibrillation
    Article Snippet: .. In short, equal amounts of protein homogenates were separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), transferred onto nitrocellulose membranes, and probed with antibodies directed against poly (ADP-Ribose) (PAR, 1:1000, BD bioscience, 551813), PARP1 (1:500, Santa Cruz, sc-25780), γH2AX (1:1000, Millipore, 05–636), Cav1.2 (1:200, Alomone Labs, ACC-003), Kv11.1 (1:400, Alomone Labs, APC-062), Kir3.1 (1:200, Alomone Labs, APC-005), β-actin (1:1000, Santa Cruz, sc-47778), or GAPDH (1:5000, Fitzgerald, 10R-G109A). ..

    SDS Page:

    Article Title: DNA damage-induced PARP1 activation confers cardiomyocyte dysfunction through NAD+ depletion in experimental atrial fibrillation
    Article Snippet: .. In short, equal amounts of protein homogenates were separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), transferred onto nitrocellulose membranes, and probed with antibodies directed against poly (ADP-Ribose) (PAR, 1:1000, BD bioscience, 551813), PARP1 (1:500, Santa Cruz, sc-25780), γH2AX (1:1000, Millipore, 05–636), Cav1.2 (1:200, Alomone Labs, ACC-003), Kv11.1 (1:400, Alomone Labs, APC-062), Kir3.1 (1:200, Alomone Labs, APC-005), β-actin (1:1000, Santa Cruz, sc-47778), or GAPDH (1:5000, Fitzgerald, 10R-G109A). ..

    other:

    Article Title: Targeted disruption of glycogen synthase kinase-3β in cardiomyocytes attenuates cardiac parasympathetic dysfunction in type 1 diabetic Akita mice
    Article Snippet: Materials The GIRK4 specific antibody was from Santa Cruz Biotechnology and the GIRK1 specific antibody was from Alomone Labs (Israel).

    Western Blot:

    Article Title: A revised mechanism of action of hyperaldosteronism-linked mutations in cytosolic domains of GIRK4 (KCNJ5)
    Article Snippet: .. Protein samples (35µg) were electrophoresed on 12% polyacrylamide-SDS gel and transferred to nitrocellulose membranes for Western blotting with antibodies; anti-GIRK1 at 1:300 dilution (Alomone Labs, APC-005) or anti-GIRK4 at 1:100 dilution (Alomone Labs, APC-027), and GAPDH in 1:1000 or 1:2000 dilution (Cell Signaling Technology, P04406). ..

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    Alomone Labs sstr5 control peptide
    Localisation of SSTRs in the cortical layers of mice primary somatosensory cortex. SSTR1 showed the most intense signal in L4 and a weaker signal in L2/3 and L5/6. SSTR2 was localised mainly in deep cortical layers (L5-6). SSTR3, SSTR4, and <t>SSTR5</t> were distributed evenly throughout the cortical layers (column A and C). Column a present representative coronal brain sections through somatosensory cortex immunofluorescently labelled with antibodies specific for SSTR1-SSTR5. Column b presents the validation of antibody specificity. Coronal brain sections were treated with primary antibodies (anti-SSTR1-5) preincubated with control blocking peptides, followed by specific secondary antibodies. The addition of control peptides resulted in the disappearance of the antibody-specific signal. Scale bar 100 μm
    Sstr5 Control Peptide, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sstr5 control peptide/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sstr5 control peptide - by Bioz Stars, 2021-10
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    80
    Alomone Labs γ2 subunits
    Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 R43Q GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and <t>γ2</t> R43Q subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 R43Q GABA A Rs. The control data for α1β2γ2 and α1β2γ2 R43Q GABA A Rs have been replotted from Figure 1 . All data in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 R43Q GABA A Rs at 40°C. * p
    γ2 Subunits, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/γ2 subunits/product/Alomone Labs
    Average 80 stars, based on 1 article reviews
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    94
    Alomone Labs anti girk1
    Confirmation of NIP–β2 subunit interactions. ( A ) Representative blots showing immunoreactivity to dynamin 1, <t>GIRK1,</t> and G oα subunits within the immunoprecipitated complexes from the brain of WT (+/+) and β2 −/−
    Anti Girk1, 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 girk1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    95
    Alomone Labs rabbit polyclonal anti aqp5 antibody
    Spatiotemporal expression of CXC-chemokine receptor 4 (CXCR4) and its ligand, CXCL12, and developmental genes in embryonic organs. ( A ) Schematic diagram of embryonic submandibular gland (eSMG) isolation and ex vivo culture. ( B ) Ex vivo branching morphogenesis of eSMGs from embryonic day (E) 13 to 17, showing epithelial growth and retraction of mesenchyme. Scale bars: 500 µm. ( C ) Temporal mRNA expression patterns of keratin 7 ( Krt7 ), aquaporin 5 ( <t>Aqp5</t> ), e-cadherin ( Cdh1 ), Krt15 , Cxcr4 , and Cxcl12 were measured from E13 to E17 by qPCR ( n = 3). ( D ) Epithelial (Epi) and mesenchymal (Mes) expression of Cxcr4 , Cxcl12 , odd-skipped related transcription factor 1 ( Osr1 ), and Cdh1 were quantified by qPCR at E13. The comparative C t values are expressed as fold increase relative to the epithelium ( n = 3). ( E ) Representative images showing expression of CXCR4 and CXCL12 in eSMG (upper) and their colocalization (lower) ( n = 3, scale bar: 500 µm). ( F ) Representative immunofluorescence images of CXCR4 and CXCL12 expression in E12 embryonic lung and pancreas ( n = 4); whole view (left two panels; scale bar: 500 µm) and magnified lumen structures (right two panels; scale bar: 50 µm). Data are presented as the mean ± SEM; * p
    Rabbit Polyclonal Anti Aqp5 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti aqp5 antibody/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
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    rabbit polyclonal anti aqp5 antibody - by Bioz Stars, 2021-10
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    Image Search Results


    Localisation of SSTRs in the cortical layers of mice primary somatosensory cortex. SSTR1 showed the most intense signal in L4 and a weaker signal in L2/3 and L5/6. SSTR2 was localised mainly in deep cortical layers (L5-6). SSTR3, SSTR4, and SSTR5 were distributed evenly throughout the cortical layers (column A and C). Column a present representative coronal brain sections through somatosensory cortex immunofluorescently labelled with antibodies specific for SSTR1-SSTR5. Column b presents the validation of antibody specificity. Coronal brain sections were treated with primary antibodies (anti-SSTR1-5) preincubated with control blocking peptides, followed by specific secondary antibodies. The addition of control peptides resulted in the disappearance of the antibody-specific signal. Scale bar 100 μm

    Journal: Brain Structure & Function

    Article Title: Somatostatin receptors (SSTR1-5) on inhibitory interneurons in the barrel cortex

    doi: 10.1007/s00429-019-02011-7

    Figure Lengend Snippet: Localisation of SSTRs in the cortical layers of mice primary somatosensory cortex. SSTR1 showed the most intense signal in L4 and a weaker signal in L2/3 and L5/6. SSTR2 was localised mainly in deep cortical layers (L5-6). SSTR3, SSTR4, and SSTR5 were distributed evenly throughout the cortical layers (column A and C). Column a present representative coronal brain sections through somatosensory cortex immunofluorescently labelled with antibodies specific for SSTR1-SSTR5. Column b presents the validation of antibody specificity. Coronal brain sections were treated with primary antibodies (anti-SSTR1-5) preincubated with control blocking peptides, followed by specific secondary antibodies. The addition of control peptides resulted in the disappearance of the antibody-specific signal. Scale bar 100 μm

    Article Snippet: The blocking peptides used in this research to confirm antibody specificity were as follows: SSTR1 control peptide (catalogue no. ASR-001, Alomone Labs), SSTR2 control peptide (catalogue no. ab171899, Abcam), SSTR3 control peptide (catalogue no. ASR-003, Alomone Labs), peptide corresponding to the anti-SSTR4 antibody (amino acid sequence (C) QQEALQPEPGRKRIPLTRTTTF, Ontores, commercially not available), and SSTR5 control peptide (catalogue no. ASR-005, Alomone Labs).

    Techniques: Mouse Assay, Blocking Assay

    SSTRs localisation in the somatosensory cortex of mice. High magnification confocal pictures of coronal sections presenting localisation of SSTR1-5 in the mouse somatosensory cortex. a SSTR1 labelled clearly the pyramidal-like cell bodies and apical dendrites. b Lack of co-localisation of SSTR2s and PV INs in the mouse primary somatosensory cortex. Yellow lines represent two orthogonal sections of a z-series showing the distribution of green and red fluorescence in the tissue. c SSTR3 immunoreactivity was found in cell bodies and neuropil. d, e Immunofluorescent signal for SSTR4 and SSTR5 was found mainly in the neuropil and much less visible in cell bodies. Scale bar for all pictures: 10 μm

    Journal: Brain Structure & Function

    Article Title: Somatostatin receptors (SSTR1-5) on inhibitory interneurons in the barrel cortex

    doi: 10.1007/s00429-019-02011-7

    Figure Lengend Snippet: SSTRs localisation in the somatosensory cortex of mice. High magnification confocal pictures of coronal sections presenting localisation of SSTR1-5 in the mouse somatosensory cortex. a SSTR1 labelled clearly the pyramidal-like cell bodies and apical dendrites. b Lack of co-localisation of SSTR2s and PV INs in the mouse primary somatosensory cortex. Yellow lines represent two orthogonal sections of a z-series showing the distribution of green and red fluorescence in the tissue. c SSTR3 immunoreactivity was found in cell bodies and neuropil. d, e Immunofluorescent signal for SSTR4 and SSTR5 was found mainly in the neuropil and much less visible in cell bodies. Scale bar for all pictures: 10 μm

    Article Snippet: The blocking peptides used in this research to confirm antibody specificity were as follows: SSTR1 control peptide (catalogue no. ASR-001, Alomone Labs), SSTR2 control peptide (catalogue no. ab171899, Abcam), SSTR3 control peptide (catalogue no. ASR-003, Alomone Labs), peptide corresponding to the anti-SSTR4 antibody (amino acid sequence (C) QQEALQPEPGRKRIPLTRTTTF, Ontores, commercially not available), and SSTR5 control peptide (catalogue no. ASR-005, Alomone Labs).

    Techniques: Mouse Assay, Fluorescence

    Two types of SSTRs distribution in the mouse barrel field. Tangential brain sections through L4 of the mouse barrel cortex. Type A distribution is characterised by a high concentration of immunoreactivity in the barrel walls (sides + septa). This type is represented by SSTR1 and SSTR2. Type B distribution is characterised by a homogeneous intensity of immunoreactivity in the barrel hollows. This type is represented by SSTR3, SSTR4, and SSTR5. Scale bar: 100 μm. Nuclear DAPI staining is visible in blue

    Journal: Brain Structure & Function

    Article Title: Somatostatin receptors (SSTR1-5) on inhibitory interneurons in the barrel cortex

    doi: 10.1007/s00429-019-02011-7

    Figure Lengend Snippet: Two types of SSTRs distribution in the mouse barrel field. Tangential brain sections through L4 of the mouse barrel cortex. Type A distribution is characterised by a high concentration of immunoreactivity in the barrel walls (sides + septa). This type is represented by SSTR1 and SSTR2. Type B distribution is characterised by a homogeneous intensity of immunoreactivity in the barrel hollows. This type is represented by SSTR3, SSTR4, and SSTR5. Scale bar: 100 μm. Nuclear DAPI staining is visible in blue

    Article Snippet: The blocking peptides used in this research to confirm antibody specificity were as follows: SSTR1 control peptide (catalogue no. ASR-001, Alomone Labs), SSTR2 control peptide (catalogue no. ab171899, Abcam), SSTR3 control peptide (catalogue no. ASR-003, Alomone Labs), peptide corresponding to the anti-SSTR4 antibody (amino acid sequence (C) QQEALQPEPGRKRIPLTRTTTF, Ontores, commercially not available), and SSTR5 control peptide (catalogue no. ASR-005, Alomone Labs).

    Techniques: Concentration Assay, Staining

    Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 R43Q GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 R43Q subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 R43Q GABA A Rs. The control data for α1β2γ2 and α1β2γ2 R43Q GABA A Rs have been replotted from Figure 1 . All data in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 R43Q GABA A Rs at 40°C. * p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: SAHA (Vorinostat) Corrects Inhibitory Synaptic Deficits Caused by Missense Epilepsy Mutations to the GABAA Receptor γ2 Subunit

    doi: 10.3389/fnmol.2018.00089

    Figure Lengend Snippet: Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 R43Q GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 R43Q subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 R43Q GABA A Rs. The control data for α1β2γ2 and α1β2γ2 R43Q GABA A Rs have been replotted from Figure 1 . All data in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 R43Q GABA A Rs at 40°C. * p

    Article Snippet: Immunohistochemistry To determine the cell surface expression levels of GABAARs, live HEK293 cells were incubated for 1 h with primary antibodies directed against surface epitopes of γ2 subunits (1:100, rabbit, #GA-005, Alomone Labs, Jerusalem, Israel) in equilibrated DMEM containing 1% BSA at 37°C.

    Techniques: Transfection

    Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 K289M GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 K289M subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 K289M GABA A Rs. The control data for α1β2γ2 and α1β2γ2 K289M GABA A Rs have been replotted from Figure 1 . All results in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 K289M GABA A Rs at 40°C. ** p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: SAHA (Vorinostat) Corrects Inhibitory Synaptic Deficits Caused by Missense Epilepsy Mutations to the GABAA Receptor γ2 Subunit

    doi: 10.3389/fnmol.2018.00089

    Figure Lengend Snippet: Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 K289M GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 K289M subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 K289M GABA A Rs. The control data for α1β2γ2 and α1β2γ2 K289M GABA A Rs have been replotted from Figure 1 . All results in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 K289M GABA A Rs at 40°C. ** p

    Article Snippet: Immunohistochemistry To determine the cell surface expression levels of GABAARs, live HEK293 cells were incubated for 1 h with primary antibodies directed against surface epitopes of γ2 subunits (1:100, rabbit, #GA-005, Alomone Labs, Jerusalem, Israel) in equilibrated DMEM containing 1% BSA at 37°C.

    Techniques: Transfection

    Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 R138G GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 R138G subunits s with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 R138G GABA A Rs. The control data for α1β2γ2 and α1β2γ2 R138G GABA A Rs have been replotted from Figure 1 . All results in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10% –90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 R138G GABA A Rs at 40°C. * p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: SAHA (Vorinostat) Corrects Inhibitory Synaptic Deficits Caused by Missense Epilepsy Mutations to the GABAA Receptor γ2 Subunit

    doi: 10.3389/fnmol.2018.00089

    Figure Lengend Snippet: Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 R138G GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 R138G subunits s with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 R138G GABA A Rs. The control data for α1β2γ2 and α1β2γ2 R138G GABA A Rs have been replotted from Figure 1 . All results in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10% –90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 R138G GABA A Rs at 40°C. * p

    Article Snippet: Immunohistochemistry To determine the cell surface expression levels of GABAARs, live HEK293 cells were incubated for 1 h with primary antibodies directed against surface epitopes of γ2 subunits (1:100, rabbit, #GA-005, Alomone Labs, Jerusalem, Israel) in equilibrated DMEM containing 1% BSA at 37°C.

    Techniques: Transfection

    Effect of suberanilohydroxamic acid (SAHA) on the surface expression of wild type and mutant GABA A Rs. (A) Sample image of HEK293 cells expressing α1β2γ2 GABA A Rs. The scale bar represents 10 μm. (B) Sample image of HEK293 cells expressing α1β2γ2 R43Q GABA A Rs. (C) Sample image of HEK293 cells expressing α1β2γ2 R43Q GABA A Rs following SAHA pre-application. (D) In the absence of SAHA pre-application, all mutants except γ2 K298M showed reduced surface expression relative to wild type (20–60 cells per mutant). (E) After SAHA pre-application, the surface expression levels of all mutants were not significantly different to wild type. * p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: SAHA (Vorinostat) Corrects Inhibitory Synaptic Deficits Caused by Missense Epilepsy Mutations to the GABAA Receptor γ2 Subunit

    doi: 10.3389/fnmol.2018.00089

    Figure Lengend Snippet: Effect of suberanilohydroxamic acid (SAHA) on the surface expression of wild type and mutant GABA A Rs. (A) Sample image of HEK293 cells expressing α1β2γ2 GABA A Rs. The scale bar represents 10 μm. (B) Sample image of HEK293 cells expressing α1β2γ2 R43Q GABA A Rs. (C) Sample image of HEK293 cells expressing α1β2γ2 R43Q GABA A Rs following SAHA pre-application. (D) In the absence of SAHA pre-application, all mutants except γ2 K298M showed reduced surface expression relative to wild type (20–60 cells per mutant). (E) After SAHA pre-application, the surface expression levels of all mutants were not significantly different to wild type. * p

    Article Snippet: Immunohistochemistry To determine the cell surface expression levels of GABAARs, live HEK293 cells were incubated for 1 h with primary antibodies directed against surface epitopes of γ2 subunits (1:100, rabbit, #GA-005, Alomone Labs, Jerusalem, Israel) in equilibrated DMEM containing 1% BSA at 37°C.

    Techniques: Expressing, Mutagenesis

    Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 N40S GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 N40S subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 N40S GABA A Rs. The control data for α1β2γ2 and α1β2γ2 N40S GABA A Rs have been replotted from Figure 1 . All data in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 N40S GABA A Rs at 40°C. * p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: SAHA (Vorinostat) Corrects Inhibitory Synaptic Deficits Caused by Missense Epilepsy Mutations to the GABAA Receptor γ2 Subunit

    doi: 10.3389/fnmol.2018.00089

    Figure Lengend Snippet: Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 N40S GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 N40S subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 N40S GABA A Rs. The control data for α1β2γ2 and α1β2γ2 N40S GABA A Rs have been replotted from Figure 1 . All data in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 N40S GABA A Rs at 40°C. * p

    Article Snippet: Immunohistochemistry To determine the cell surface expression levels of GABAARs, live HEK293 cells were incubated for 1 h with primary antibodies directed against surface epitopes of γ2 subunits (1:100, rabbit, #GA-005, Alomone Labs, Jerusalem, Israel) in equilibrated DMEM containing 1% BSA at 37°C.

    Techniques: Transfection

    Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 P44S GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 P44S subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 P44S GABA A Rs. The control data for α1β2γ2 and α1β2γ2 P44S GABA A Rs have been replotted from Figure 1 . All results in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 P44S GABA A Rs at 40°C. * p

    Journal: Frontiers in Molecular Neuroscience

    Article Title: SAHA (Vorinostat) Corrects Inhibitory Synaptic Deficits Caused by Missense Epilepsy Mutations to the GABAA Receptor γ2 Subunit

    doi: 10.3389/fnmol.2018.00089

    Figure Lengend Snippet: Effects of SAHA and temperature on IPSCs mediated by α1β2γ2 P44S GABA A Rs. (A) Examples of digitally averaged and normalised IPSCs from HEK293 cells transfected with α1, β2 and γ2 P44S subunits with and without SAHA pre-application. (B–D) Effect of SAHA pre-application on the amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 P44S GABA A Rs. The control data for α1β2γ2 and α1β2γ2 P44S GABA A Rs have been replotted from Figure 1 . All results in panels (A–D) were recorded at room temperature (22°C). (E–G) Mean amplitudes, 10%–90% rise times and decay time constants of IPSCs mediated by α1β2γ2 and α1β2γ2 P44S GABA A Rs at 40°C. * p

    Article Snippet: Immunohistochemistry To determine the cell surface expression levels of GABAARs, live HEK293 cells were incubated for 1 h with primary antibodies directed against surface epitopes of γ2 subunits (1:100, rabbit, #GA-005, Alomone Labs, Jerusalem, Israel) in equilibrated DMEM containing 1% BSA at 37°C.

    Techniques: Transfection

    Confirmation of NIP–β2 subunit interactions. ( A ) Representative blots showing immunoreactivity to dynamin 1, GIRK1, and G oα subunits within the immunoprecipitated complexes from the brain of WT (+/+) and β2 −/−

    Journal:

    Article Title: Intracellular complexes of the ?2 subunit of the nicotinic acetylcholine receptor in brain identified by proteomics

    doi: 10.1073/pnas.0710314104

    Figure Lengend Snippet: Confirmation of NIP–β2 subunit interactions. ( A ) Representative blots showing immunoreactivity to dynamin 1, GIRK1, and G oα subunits within the immunoprecipitated complexes from the brain of WT (+/+) and β2 −/−

    Article Snippet: Western blot analysis was performed with the following primary antibodies: anti-β2 (H-92) (Santa Cruz Biotechnology); anti-α4 (H-133) (Santa Cruz Biotechnology); anti-clathrin HC (Santa Cruz Biotechnology); anti-NSF (Upstate Biotechnology); anti-dynamin 1 (PharMingen–Becton Dickinson); anti-synaptotagmin 1 (Chemicon); anti-GTP-binding protein (G protein) Goα (Santa Cruz Biotechnology), anti-GIRK1 (Alomone Laboratories); and anti-GST (Amersham Pharmacia).

    Techniques: Immunoprecipitation

    Spatiotemporal expression of CXC-chemokine receptor 4 (CXCR4) and its ligand, CXCL12, and developmental genes in embryonic organs. ( A ) Schematic diagram of embryonic submandibular gland (eSMG) isolation and ex vivo culture. ( B ) Ex vivo branching morphogenesis of eSMGs from embryonic day (E) 13 to 17, showing epithelial growth and retraction of mesenchyme. Scale bars: 500 µm. ( C ) Temporal mRNA expression patterns of keratin 7 ( Krt7 ), aquaporin 5 ( Aqp5 ), e-cadherin ( Cdh1 ), Krt15 , Cxcr4 , and Cxcl12 were measured from E13 to E17 by qPCR ( n = 3). ( D ) Epithelial (Epi) and mesenchymal (Mes) expression of Cxcr4 , Cxcl12 , odd-skipped related transcription factor 1 ( Osr1 ), and Cdh1 were quantified by qPCR at E13. The comparative C t values are expressed as fold increase relative to the epithelium ( n = 3). ( E ) Representative images showing expression of CXCR4 and CXCL12 in eSMG (upper) and their colocalization (lower) ( n = 3, scale bar: 500 µm). ( F ) Representative immunofluorescence images of CXCR4 and CXCL12 expression in E12 embryonic lung and pancreas ( n = 4); whole view (left two panels; scale bar: 500 µm) and magnified lumen structures (right two panels; scale bar: 50 µm). Data are presented as the mean ± SEM; * p

    Journal: International Journal of Molecular Sciences

    Article Title: CXCR4 Regulates Temporal Differentiation via PRC1 Complex in Organogenesis of Epithelial Glands

    doi: 10.3390/ijms22020619

    Figure Lengend Snippet: Spatiotemporal expression of CXC-chemokine receptor 4 (CXCR4) and its ligand, CXCL12, and developmental genes in embryonic organs. ( A ) Schematic diagram of embryonic submandibular gland (eSMG) isolation and ex vivo culture. ( B ) Ex vivo branching morphogenesis of eSMGs from embryonic day (E) 13 to 17, showing epithelial growth and retraction of mesenchyme. Scale bars: 500 µm. ( C ) Temporal mRNA expression patterns of keratin 7 ( Krt7 ), aquaporin 5 ( Aqp5 ), e-cadherin ( Cdh1 ), Krt15 , Cxcr4 , and Cxcl12 were measured from E13 to E17 by qPCR ( n = 3). ( D ) Epithelial (Epi) and mesenchymal (Mes) expression of Cxcr4 , Cxcl12 , odd-skipped related transcription factor 1 ( Osr1 ), and Cdh1 were quantified by qPCR at E13. The comparative C t values are expressed as fold increase relative to the epithelium ( n = 3). ( E ) Representative images showing expression of CXCR4 and CXCL12 in eSMG (upper) and their colocalization (lower) ( n = 3, scale bar: 500 µm). ( F ) Representative immunofluorescence images of CXCR4 and CXCL12 expression in E12 embryonic lung and pancreas ( n = 4); whole view (left two panels; scale bar: 500 µm) and magnified lumen structures (right two panels; scale bar: 50 µm). Data are presented as the mean ± SEM; * p

    Article Snippet: The following primary antibodies were used in the procedures: rat monoclonal anti-CXCR4 antibody (R & D Systems, MAB21651), rabbit monoclonal anti-KRT7 antibody (Abcam, ab181598; Cambridge, UK); rabbit monoclonal anti-CDH1 antibody (CST, 3195; Beverly, MA, USA), rabbit monoclonal anti-H2AK119ub antibody (CST, 8240); mouse monoclonal anti-CXCL12 antibody (Novus Biologicals, MAB350; Littleton, CO, USA), rabbit polyclonal anti-AQP5 antibody (Alomone Labs, AQP-005; Jerusalem, Israel), rabbit monoclonal anti-CASP3 antibody (CST, 9664), and rat monoclonal anti-KI67 antibody (ThermoFisher, 14-5698-82).

    Techniques: Expressing, Isolation, Ex Vivo, Real-time Polymerase Chain Reaction, Immunofluorescence

    AMD3100-induced precocious differentiation of epithelial cells. ( A , B ) Representative contour tracing ( A ) and bud number changes ( B ) of control and AMD3100-treated eSMGs during 48 h at 6-h intervals ( n = 3). ( C ) EdU staining results at 6 and 24 h after AMD3100 treatment. EdU in green and PNA in gray ( n = 4, scale bar: 500 µm). ( D ) Immunostaining results of Ki67 (red) and F-actin (green) in acini and duct of eSMGs 24 h after AMD3100 treatment. Morphologies of acinar buds and duct cells are outlined with white dotted lines. Scale bar: 50 µm. ( E ) Duct widths of control and AMD3100-treated eSMGs were visualized via F-actin-based intensity profiles of horizontal sectioning of ducts 24 h after the treatment. ( F ) Duct widths of control and AMD3100-treated eSMGs were quantified 24 h after the treatment ( n = 9). ( G ) Immunostaining results of AQP5 (green) and KRT7 (red). Magnified regions of acinar buds are marked with white dotted squares. The white arrows (middle panels) indicate areas with the highest AQP5 expression ( n = 4, scale bar: left, 100 µm; middle and right, 50 µm). Data are presented as the mean ± SEM; * p

    Journal: International Journal of Molecular Sciences

    Article Title: CXCR4 Regulates Temporal Differentiation via PRC1 Complex in Organogenesis of Epithelial Glands

    doi: 10.3390/ijms22020619

    Figure Lengend Snippet: AMD3100-induced precocious differentiation of epithelial cells. ( A , B ) Representative contour tracing ( A ) and bud number changes ( B ) of control and AMD3100-treated eSMGs during 48 h at 6-h intervals ( n = 3). ( C ) EdU staining results at 6 and 24 h after AMD3100 treatment. EdU in green and PNA in gray ( n = 4, scale bar: 500 µm). ( D ) Immunostaining results of Ki67 (red) and F-actin (green) in acini and duct of eSMGs 24 h after AMD3100 treatment. Morphologies of acinar buds and duct cells are outlined with white dotted lines. Scale bar: 50 µm. ( E ) Duct widths of control and AMD3100-treated eSMGs were visualized via F-actin-based intensity profiles of horizontal sectioning of ducts 24 h after the treatment. ( F ) Duct widths of control and AMD3100-treated eSMGs were quantified 24 h after the treatment ( n = 9). ( G ) Immunostaining results of AQP5 (green) and KRT7 (red). Magnified regions of acinar buds are marked with white dotted squares. The white arrows (middle panels) indicate areas with the highest AQP5 expression ( n = 4, scale bar: left, 100 µm; middle and right, 50 µm). Data are presented as the mean ± SEM; * p

    Article Snippet: The following primary antibodies were used in the procedures: rat monoclonal anti-CXCR4 antibody (R & D Systems, MAB21651), rabbit monoclonal anti-KRT7 antibody (Abcam, ab181598; Cambridge, UK); rabbit monoclonal anti-CDH1 antibody (CST, 3195; Beverly, MA, USA), rabbit monoclonal anti-H2AK119ub antibody (CST, 8240); mouse monoclonal anti-CXCL12 antibody (Novus Biologicals, MAB350; Littleton, CO, USA), rabbit polyclonal anti-AQP5 antibody (Alomone Labs, AQP-005; Jerusalem, Israel), rabbit monoclonal anti-CASP3 antibody (CST, 9664), and rat monoclonal anti-KI67 antibody (ThermoFisher, 14-5698-82).

    Techniques: Staining, Immunostaining, Expressing