aqp3  (Alomone Labs)


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    Structured Review

    Alomone Labs aqp3
    Diacerein attenuated downregulation of renal AQP expression in endotoxemic mice. a - c Protein expression of aquaporin 1 (AQP1) ( a ), AQP2 ( b ) and <t>AQP3</t> ( c ) in kidney was determined by western blotting. Diacerein significantly inhibited lipopolysaccharide (LPS)-induced decrease of AQP1, AQP2 and AQP3 expression. ** P
    Aqp3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aqp3/product/Alomone Labs
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    aqp3 - by Bioz Stars, 2022-05
    90/100 stars

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    1) Product Images from "Inhibition of inflammation using diacerein markedly improved renal function in endotoxemic acute kidney injured mice"

    Article Title: Inhibition of inflammation using diacerein markedly improved renal function in endotoxemic acute kidney injured mice

    Journal: Cellular & Molecular Biology Letters

    doi: 10.1186/s11658-018-0107-z

    Diacerein attenuated downregulation of renal AQP expression in endotoxemic mice. a - c Protein expression of aquaporin 1 (AQP1) ( a ), AQP2 ( b ) and AQP3 ( c ) in kidney was determined by western blotting. Diacerein significantly inhibited lipopolysaccharide (LPS)-induced decrease of AQP1, AQP2 and AQP3 expression. ** P
    Figure Legend Snippet: Diacerein attenuated downregulation of renal AQP expression in endotoxemic mice. a - c Protein expression of aquaporin 1 (AQP1) ( a ), AQP2 ( b ) and AQP3 ( c ) in kidney was determined by western blotting. Diacerein significantly inhibited lipopolysaccharide (LPS)-induced decrease of AQP1, AQP2 and AQP3 expression. ** P

    Techniques Used: Expressing, Mouse Assay, Western Blot

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    Alomone Labs anti kv1 3 rabbit polyclonal
    Expression of the potassium channel <t>Kv1.3.</t> Protein extracts were prepared from control and iron-fed C8B4 microglia. Western blot analysis was carried out to determine the level of Kv1.3 in the microglia. Bands for the protein were observed in both control and iron-fed microglia. Levels of tubulin were also determined to verify protein loading. The results showed a significant ( p
    Anti Kv1 3 Rabbit Polyclonal, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti kv1 3 rabbit polyclonal/product/Alomone Labs
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    86
    Alomone Labs rabbit polyclonal anti kv1 3 antibody
    <t>Kv1.3</t> channels are recruited at the interface between CD3/CD28 beads and T cells
    Rabbit Polyclonal Anti Kv1 3 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti kv1 3 antibody/product/Alomone Labs
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    93
    Alomone Labs antigen preabsorbed anti clc 3 ab
    <t>Anti-ClC-3</t> Ab dialysis abolishes expressed I gpClC-3 in NIH/3T3 cells A , phase contrast (left panel) and fluorescence micrographs (right panel) of NIH/3T3 cell transfected with gpClC-3-GFP. B , representative I gpClC-3 recorded from GFP-positive NIH/3T3 cells (as shown in A ) under isotonic, hypotonic and hypertonic conditions over the range -100 to +120 mV. C , effects of anti-ClC-3 Ab on I gpClC-3 at ±80 mV when pipette solutions contained <t>preabsorbed</t> anti-ClC-3 Ab (control, ○) or anti-ClC-3 Ab alone (▪). D , mean current densities recorded from untransfected NIH/3T3 cells (blue, n = 38), gpClC-3-GFP-transfected cells dialysed with standard intracellular pipette solutions (green, n = 9), preabsorbed anti-ClC-3 Ab (black, n = 4), and anti-ClC-3 Ab alone (red, n = 9).
    Antigen Preabsorbed Anti Clc 3 Ab, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Expression of the potassium channel Kv1.3. Protein extracts were prepared from control and iron-fed C8B4 microglia. Western blot analysis was carried out to determine the level of Kv1.3 in the microglia. Bands for the protein were observed in both control and iron-fed microglia. Levels of tubulin were also determined to verify protein loading. The results showed a significant ( p

    Journal: Biomolecules

    Article Title: Model Senescent Microglia Induce Disease Related Changes in α-Synuclein Expression and Activity

    doi: 10.3390/biom8030067

    Figure Lengend Snippet: Expression of the potassium channel Kv1.3. Protein extracts were prepared from control and iron-fed C8B4 microglia. Western blot analysis was carried out to determine the level of Kv1.3 in the microglia. Bands for the protein were observed in both control and iron-fed microglia. Levels of tubulin were also determined to verify protein loading. The results showed a significant ( p

    Article Snippet: Anti-l-ferritin mouse monoclonal (SC-25616, Santa Cruz, Dallas, TX, USA) was used at 1:5000, anti-Kv1.3 rabbit polyclonal was used at 1:400 (APC101, Alomone, Jerusalem, Israel), and anti- Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) mouse monoclonal was used at 1:2000 (6C5, Abcam).

    Techniques: Expressing, Western Blot

    Kv1.3 channels are recruited at the interface between CD3/CD28 beads and T cells

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: Kv1.3 channels are recruited at the interface between CD3/CD28 beads and T cells

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    Kv1.3 channels in T lymphocytes from patients with SLE display biophysical and pharmacological properties similar to those in healthy T cells

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: Kv1.3 channels in T lymphocytes from patients with SLE display biophysical and pharmacological properties similar to those in healthy T cells

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    Comparison of the rates of Kv1.3 channel compartmentalization in the IS in normal and SLE T cells

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: Comparison of the rates of Kv1.3 channel compartmentalization in the IS in normal and SLE T cells

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    Electrophysiological and pharmacological properties of Kv1.3 channels in SLE T cells

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: Electrophysiological and pharmacological properties of Kv1.3 channels in SLE T cells

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    APC-T cell activation induces differential reorganization of Kv1.3 channels in the IS formed with resting healthy and SLE T cells

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: APC-T cell activation induces differential reorganization of Kv1.3 channels in the IS formed with resting healthy and SLE T cells

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques: Activation Assay

    Differential kinetics of Kv1.3 channel reorganization in the IS

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: Differential kinetics of Kv1.3 channel reorganization in the IS

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    Kv1.3 channel recruitment in the IS in activated healthy T cells parallels SLE T lymphocytes

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: Kv1.3 channel recruitment in the IS in activated healthy T cells parallels SLE T lymphocytes

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    The kinetics of Kv1.3 redistribution in the immunological synapse of SLE T cells resemble those of pre-activated normal T cells

    Journal:

    Article Title: ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1ALTERED DYNAMICS OF Kv1.3 CHANNEL COMPARTMENTALIZATION IN THE IMMUNOLOGICAL SYNAPSE IN SYSTEMIC LUPUS ERYTHEMATOSUS 1 , 2

    doi:

    Figure Lengend Snippet: The kinetics of Kv1.3 redistribution in the immunological synapse of SLE T cells resemble those of pre-activated normal T cells

    Article Snippet: The primary antibodies used for detecting Kv1.3 proteins were either a rabbit polyclonal anti-Kv1.3 antibody against an epitope on the C-terminal domain of the protein (Alomone, Jerusalem, Israel) or an extracellular epitope (Sigma-Aldrich).

    Techniques:

    Anti-ClC-3 Ab dialysis abolishes expressed I gpClC-3 in NIH/3T3 cells A , phase contrast (left panel) and fluorescence micrographs (right panel) of NIH/3T3 cell transfected with gpClC-3-GFP. B , representative I gpClC-3 recorded from GFP-positive NIH/3T3 cells (as shown in A ) under isotonic, hypotonic and hypertonic conditions over the range -100 to +120 mV. C , effects of anti-ClC-3 Ab on I gpClC-3 at ±80 mV when pipette solutions contained preabsorbed anti-ClC-3 Ab (control, ○) or anti-ClC-3 Ab alone (▪). D , mean current densities recorded from untransfected NIH/3T3 cells (blue, n = 38), gpClC-3-GFP-transfected cells dialysed with standard intracellular pipette solutions (green, n = 9), preabsorbed anti-ClC-3 Ab (black, n = 4), and anti-ClC-3 Ab alone (red, n = 9).

    Journal: The Journal of Physiology

    Article Title: Functional inhibition of native volume-sensitive outwardly rectifying anion channels in muscle cells and Xenopus oocytes by anti-ClC-3 antibody

    doi: 10.1111/j.1469-7793.2001.0437i.x

    Figure Lengend Snippet: Anti-ClC-3 Ab dialysis abolishes expressed I gpClC-3 in NIH/3T3 cells A , phase contrast (left panel) and fluorescence micrographs (right panel) of NIH/3T3 cell transfected with gpClC-3-GFP. B , representative I gpClC-3 recorded from GFP-positive NIH/3T3 cells (as shown in A ) under isotonic, hypotonic and hypertonic conditions over the range -100 to +120 mV. C , effects of anti-ClC-3 Ab on I gpClC-3 at ±80 mV when pipette solutions contained preabsorbed anti-ClC-3 Ab (control, ○) or anti-ClC-3 Ab alone (▪). D , mean current densities recorded from untransfected NIH/3T3 cells (blue, n = 38), gpClC-3-GFP-transfected cells dialysed with standard intracellular pipette solutions (green, n = 9), preabsorbed anti-ClC-3 Ab (black, n = 4), and anti-ClC-3 Ab alone (red, n = 9).

    Article Snippet: shows a phase contrast (left) and fluorescence micrograph (right) of a NIH/3T3 cell transiently co-transfected by electroporation with wild-type gpClC-3 and the GFP reporter plasmid (arrow). gpClC-3-GFP-transfected cells in symmetrical Cl− (135 mM) conditions, generated large volume-sensitive outwardly rectifying whole-cell Cl− currents ( ) that were similar to currents previously recorded from NIH/3T3 cells transfected with gpClC-3 alone ( ). illustrates the effects of intracellular dialysis of either anti-ClC-3 Ab alone or antigen-preabsorbed anti-ClC-3 Ab on the amplitude and time course of I gpClC-3 activated or inhibited by exposure to hypotonic and hypertonic solutions, respectively, in gpClC-3-GFP-transfected 3T3 cells.

    Techniques: Fluorescence, Transfection, Transferring

    Anti-ClC-3 Ab abolishes native VSOAC currents in canine PASMCs A , time course of VSOAC currents from two PASMCs dialysed with either anti-ClC-3 Ab (5 μg ml −1 ) preabsorbed with antigen (50 μg ml −1 ; ○), or anti-ClC-3 Ab alone (5 μg ml −1 ; •). Inset: Western blot analysis of native ClC-3 expression in isolated canine PASMCs. B , mean current densities in cells dialysed with either standard intracellular solutions ( n = 11), preabsorbed anti-ClC-3 Ab ( n = 4) or anti-ClC-3 Ab alone ( n = 5).

    Journal: The Journal of Physiology

    Article Title: Functional inhibition of native volume-sensitive outwardly rectifying anion channels in muscle cells and Xenopus oocytes by anti-ClC-3 antibody

    doi: 10.1111/j.1469-7793.2001.0437i.x

    Figure Lengend Snippet: Anti-ClC-3 Ab abolishes native VSOAC currents in canine PASMCs A , time course of VSOAC currents from two PASMCs dialysed with either anti-ClC-3 Ab (5 μg ml −1 ) preabsorbed with antigen (50 μg ml −1 ; ○), or anti-ClC-3 Ab alone (5 μg ml −1 ; •). Inset: Western blot analysis of native ClC-3 expression in isolated canine PASMCs. B , mean current densities in cells dialysed with either standard intracellular solutions ( n = 11), preabsorbed anti-ClC-3 Ab ( n = 4) or anti-ClC-3 Ab alone ( n = 5).

    Article Snippet: shows a phase contrast (left) and fluorescence micrograph (right) of a NIH/3T3 cell transiently co-transfected by electroporation with wild-type gpClC-3 and the GFP reporter plasmid (arrow). gpClC-3-GFP-transfected cells in symmetrical Cl− (135 mM) conditions, generated large volume-sensitive outwardly rectifying whole-cell Cl− currents ( ) that were similar to currents previously recorded from NIH/3T3 cells transfected with gpClC-3 alone ( ). illustrates the effects of intracellular dialysis of either anti-ClC-3 Ab alone or antigen-preabsorbed anti-ClC-3 Ab on the amplitude and time course of I gpClC-3 activated or inhibited by exposure to hypotonic and hypertonic solutions, respectively, in gpClC-3-GFP-transfected 3T3 cells.

    Techniques: Western Blot, Expressing, Isolation

    Anti-ClC-3 Ab dialysis abolishes native VSOAC currents in guinea-pig cardiac myocytes A , native VSOAC currents at ±80 mV in myocytes exposed to isotonic and hypotonic solutions. Aa , pipette solutions contained preabsorbed anti-ClC-3 Ab (control, ○) or anti-ClC-3 Ab alone (▪). Ab , mean current densities for preabsorbed anti-ClC-3 Ab (□, n = 3) or anti-ClC-3 Ab alone (▪, n = 5) at times indicated. B, same as A , except cells were preswelled by pre-exposure to hypotonic bath solutions prior to membrane rupture and dialysis; preabsorbed anti-ClC-3 Ab (□, n = 4), and anti-ClC-3 Ab alone (▪, n = 5).

    Journal: The Journal of Physiology

    Article Title: Functional inhibition of native volume-sensitive outwardly rectifying anion channels in muscle cells and Xenopus oocytes by anti-ClC-3 antibody

    doi: 10.1111/j.1469-7793.2001.0437i.x

    Figure Lengend Snippet: Anti-ClC-3 Ab dialysis abolishes native VSOAC currents in guinea-pig cardiac myocytes A , native VSOAC currents at ±80 mV in myocytes exposed to isotonic and hypotonic solutions. Aa , pipette solutions contained preabsorbed anti-ClC-3 Ab (control, ○) or anti-ClC-3 Ab alone (▪). Ab , mean current densities for preabsorbed anti-ClC-3 Ab (□, n = 3) or anti-ClC-3 Ab alone (▪, n = 5) at times indicated. B, same as A , except cells were preswelled by pre-exposure to hypotonic bath solutions prior to membrane rupture and dialysis; preabsorbed anti-ClC-3 Ab (□, n = 4), and anti-ClC-3 Ab alone (▪, n = 5).

    Article Snippet: shows a phase contrast (left) and fluorescence micrograph (right) of a NIH/3T3 cell transiently co-transfected by electroporation with wild-type gpClC-3 and the GFP reporter plasmid (arrow). gpClC-3-GFP-transfected cells in symmetrical Cl− (135 mM) conditions, generated large volume-sensitive outwardly rectifying whole-cell Cl− currents ( ) that were similar to currents previously recorded from NIH/3T3 cells transfected with gpClC-3 alone ( ). illustrates the effects of intracellular dialysis of either anti-ClC-3 Ab alone or antigen-preabsorbed anti-ClC-3 Ab on the amplitude and time course of I gpClC-3 activated or inhibited by exposure to hypotonic and hypertonic solutions, respectively, in gpClC-3-GFP-transfected 3T3 cells.

    Techniques: Transferring

    Anti-ClC-3 Ab injection inhibits native VSOAC currents in Xenopus laevis oocytes A , Western blot analysis of native ClC-3 expression in oocytes. B , 4-phorbol 12,13-dibutyrate (PDBu) inhibition of native VSOAC currents in oocytes (-100 to +120 mV). C, time course of VSOAC activation in response to hypotonic bath solutions from a non-injected control oocyte (○) and an oocyte injected with anti-ClC-3 Ab (15 μg ml -1 ; •) at time shown. Cells were held at -30 mV for 30 ms, hyperpolarized to -100 mV for 210 ms and then depolarized to +100 mV for 210 ms, repetitively at 2 Hz. D, mean current densities from control oocytes ( n = 10), oocytes injected with anti-ClC-3 Ab alone (15 μg ml -1 ) ( n = 4) or injected with preabsorbed anti-ClC-3 Ab (150 μg ml -1 ) ( n = 4). Peak current densities were measured after 5 min exposure to isotonic solutions, and after 85 min exposure to hypotonic solutions.

    Journal: The Journal of Physiology

    Article Title: Functional inhibition of native volume-sensitive outwardly rectifying anion channels in muscle cells and Xenopus oocytes by anti-ClC-3 antibody

    doi: 10.1111/j.1469-7793.2001.0437i.x

    Figure Lengend Snippet: Anti-ClC-3 Ab injection inhibits native VSOAC currents in Xenopus laevis oocytes A , Western blot analysis of native ClC-3 expression in oocytes. B , 4-phorbol 12,13-dibutyrate (PDBu) inhibition of native VSOAC currents in oocytes (-100 to +120 mV). C, time course of VSOAC activation in response to hypotonic bath solutions from a non-injected control oocyte (○) and an oocyte injected with anti-ClC-3 Ab (15 μg ml -1 ; •) at time shown. Cells were held at -30 mV for 30 ms, hyperpolarized to -100 mV for 210 ms and then depolarized to +100 mV for 210 ms, repetitively at 2 Hz. D, mean current densities from control oocytes ( n = 10), oocytes injected with anti-ClC-3 Ab alone (15 μg ml -1 ) ( n = 4) or injected with preabsorbed anti-ClC-3 Ab (150 μg ml -1 ) ( n = 4). Peak current densities were measured after 5 min exposure to isotonic solutions, and after 85 min exposure to hypotonic solutions.

    Article Snippet: shows a phase contrast (left) and fluorescence micrograph (right) of a NIH/3T3 cell transiently co-transfected by electroporation with wild-type gpClC-3 and the GFP reporter plasmid (arrow). gpClC-3-GFP-transfected cells in symmetrical Cl− (135 mM) conditions, generated large volume-sensitive outwardly rectifying whole-cell Cl− currents ( ) that were similar to currents previously recorded from NIH/3T3 cells transfected with gpClC-3 alone ( ). illustrates the effects of intracellular dialysis of either anti-ClC-3 Ab alone or antigen-preabsorbed anti-ClC-3 Ab on the amplitude and time course of I gpClC-3 activated or inhibited by exposure to hypotonic and hypertonic solutions, respectively, in gpClC-3-GFP-transfected 3T3 cells.

    Techniques: Injection, Western Blot, Expressing, Inhibition, Activation Assay, Mass Spectrometry