rabbit polyclonal anti kv1 3 antibody  (Alomone Labs)


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    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: 93/100, 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
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti kv1 3 antibody - by Bioz Stars, 2022-07
    93/100 stars

    Images

    1) Product Images from "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"

    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

    Journal:

    doi:

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

    Techniques Used:

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

    Techniques Used:

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

    Techniques Used:

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

    Techniques Used:

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

    Techniques Used: Activation Assay

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

    Techniques Used:

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

    Techniques Used:

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

    Techniques Used:

    2) Product Images from "Model Senescent Microglia Induce Disease Related Changes in α-Synuclein Expression and Activity"

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

    Journal: Biomolecules

    doi: 10.3390/biom8030067

    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
    Figure Legend 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

    Techniques Used: Expressing, Western Blot

    3) Product Images from "Biophysical basis for Kv1.3 regulation of membrane potential changes induced by P2X4‐mediated calcium entry in microglia, et al. Biophysical basis for Kv1.3 regulation of membrane potential changes induced by P2X4‐mediated calcium entry in microglia"

    Article Title: Biophysical basis for Kv1.3 regulation of membrane potential changes induced by P2X4‐mediated calcium entry in microglia, et al. Biophysical basis for Kv1.3 regulation of membrane potential changes induced by P2X4‐mediated calcium entry in microglia

    Journal: Glia

    doi: 10.1002/glia.23847

    Kv1.3 channel inhibition reduces intracellular Ca 2+ signaling. (a) Fluo‐4 AM calcium indicator fluorescence signal elicited by 0.1 mM ATP is 2.65 ± 0.99‐fold ( n = 3) higher in total area under the curve (AUC) compared to that elicited by 0.1 mM BzATP ( n = 3). Statistical significance determined by unpaired t test comparing ATP and BzATP cells. (b) Ivermectin (IVC, 3 μM) increases fluorescence signaling elicited by 0.1 mM ATP by 2.65 ± 0.99‐fold ( n = 4). Statistical significance between before and after ivermectin determined by paired t test. (c) Twenty‐four hours treatment with lipopolysaccharides (LPS) (300 ng/ml) or interleukin‐4 (IL‐4) (20 ng/ml) suppresses fluorescence increase. Statistical significance determined by one‐way analysis of variance (ANOVA) followed by Tukey–Cramer's post hoc test (alpha = 0.05). (d–f) Preincubation with the Kv1.3 blocker ShK‐223 (100 nM) reduces ATP‐mediated fluorescence increases in LPS‐treated microglia but not in undifferentiated or IL‐4 stimulated microglia. All ATP applied at 0.1 mM and after baseline fluorescence was recorded for 2 min. Changes in [Ca 2+ ] i are represented as ΔF/F (change in fluorescence measured as AUC after baseline subtraction). Scale bars indicate 20% of the maximal normalized change in ΔF/F, which is 1ΔF/F. Statistical significance determined by paired t test. All data presented as mean ± SEM . Measurements from three to seven separate experiments (coverslips from different cultures on different days) and 50–100 cells each were measured per experiment for panels (c)–(f). * p
    Figure Legend Snippet: Kv1.3 channel inhibition reduces intracellular Ca 2+ signaling. (a) Fluo‐4 AM calcium indicator fluorescence signal elicited by 0.1 mM ATP is 2.65 ± 0.99‐fold ( n = 3) higher in total area under the curve (AUC) compared to that elicited by 0.1 mM BzATP ( n = 3). Statistical significance determined by unpaired t test comparing ATP and BzATP cells. (b) Ivermectin (IVC, 3 μM) increases fluorescence signaling elicited by 0.1 mM ATP by 2.65 ± 0.99‐fold ( n = 4). Statistical significance between before and after ivermectin determined by paired t test. (c) Twenty‐four hours treatment with lipopolysaccharides (LPS) (300 ng/ml) or interleukin‐4 (IL‐4) (20 ng/ml) suppresses fluorescence increase. Statistical significance determined by one‐way analysis of variance (ANOVA) followed by Tukey–Cramer's post hoc test (alpha = 0.05). (d–f) Preincubation with the Kv1.3 blocker ShK‐223 (100 nM) reduces ATP‐mediated fluorescence increases in LPS‐treated microglia but not in undifferentiated or IL‐4 stimulated microglia. All ATP applied at 0.1 mM and after baseline fluorescence was recorded for 2 min. Changes in [Ca 2+ ] i are represented as ΔF/F (change in fluorescence measured as AUC after baseline subtraction). Scale bars indicate 20% of the maximal normalized change in ΔF/F, which is 1ΔF/F. Statistical significance determined by paired t test. All data presented as mean ± SEM . Measurements from three to seven separate experiments (coverslips from different cultures on different days) and 50–100 cells each were measured per experiment for panels (c)–(f). * p

    Techniques Used: Inhibition, Fluorescence

    Kv1.3 prevents extreme membrane depolarization triggered by current injections. Sample current‐clamp traces of a Kv1.3+ Chinese Hamster Ovary (CHO) cell before (a) and after (b) 100 nM ShK‐223 ( n = 8). (Top) Current injection protocol consisted of 3‐s ramps from 0 to 50 pA in 10 pA steps. Insets : Voltage‐clamp traces of same cell elicited by a voltage ramp from −120 to +40 mV. (c) Quantification of maximal membrane depolarization measured. Sample current‐clamp traces of Kv1.3+ microglia before (d) and after (e) 100 nM ShK‐223 ( n = 11). (Top) Current injection protocol consisted of 3‐s ramps from 0 to 25 pA in 5 pA steps. Insets : Voltage‐clamp traces of same cell. (f) Quantification of maximal membrane depolarization measured. Dashed green lines indicate the −40‐mV membrane potential level near the Kv1.3 activation threshold potential. Error bars indicate mean ± SD . Statistical significance determined by paired t test. * p
    Figure Legend Snippet: Kv1.3 prevents extreme membrane depolarization triggered by current injections. Sample current‐clamp traces of a Kv1.3+ Chinese Hamster Ovary (CHO) cell before (a) and after (b) 100 nM ShK‐223 ( n = 8). (Top) Current injection protocol consisted of 3‐s ramps from 0 to 50 pA in 10 pA steps. Insets : Voltage‐clamp traces of same cell elicited by a voltage ramp from −120 to +40 mV. (c) Quantification of maximal membrane depolarization measured. Sample current‐clamp traces of Kv1.3+ microglia before (d) and after (e) 100 nM ShK‐223 ( n = 11). (Top) Current injection protocol consisted of 3‐s ramps from 0 to 25 pA in 5 pA steps. Insets : Voltage‐clamp traces of same cell. (f) Quantification of maximal membrane depolarization measured. Dashed green lines indicate the −40‐mV membrane potential level near the Kv1.3 activation threshold potential. Error bars indicate mean ± SD . Statistical significance determined by paired t test. * p

    Techniques Used: Injection, Activation Assay

    Effects of Kv1.3 channel inhibition on mRNA expression of microglial channels and pro‐inflammatory cytokines. Quantitative PCR ( qPCR) quantification of mRNA expression of (a) channels and (b) microglia‐associated cytokines in undifferentiated (U), lipopolysaccharides (LPS) only (L; 300 ng/ml), LPS + 100 nM ShK‐223 (L + S) and 100 nM ShK‐223 only (S) treated microglia. Data from three independent mixed‐gender postnatal microglia cultures. Bar graphs represent means ± SEM . Statistical analysis was performed using unpaired t test. * p
    Figure Legend Snippet: Effects of Kv1.3 channel inhibition on mRNA expression of microglial channels and pro‐inflammatory cytokines. Quantitative PCR ( qPCR) quantification of mRNA expression of (a) channels and (b) microglia‐associated cytokines in undifferentiated (U), lipopolysaccharides (LPS) only (L; 300 ng/ml), LPS + 100 nM ShK‐223 (L + S) and 100 nM ShK‐223 only (S) treated microglia. Data from three independent mixed‐gender postnatal microglia cultures. Bar graphs represent means ± SEM . Statistical analysis was performed using unpaired t test. * p

    Techniques Used: Inhibition, Expressing, Real-time Polymerase Chain Reaction

    Influence of Kv1.3 expression on membrane potential changes. (a) Corresponding voltage‐clamp ( top ) and current‐clamp ( bottom ) traces induced by 0.1 mM ATP from three individual microglia. (b) Scatterplots for resting membrane potential (RMP) and ATP‐induced membrane potential (AMP). RMP's measured in undifferentiated cells and lipopolysaccharides (LPS)‐differentiated cells averaged −88.08 ± 5.14 mV ( n = 27) and −67.64 ± 12.62 mV ( n = 28), respectively. AMP's in undifferentiated cells and LPS‐differentiated cells averaged −19.32 ± 14.49 mV and −44.09 ± 7.67 mV, respectively. Data represented by means ± SD . Statistical significance between before and after ATP addition determined by paired t test and between undifferentiated and lipopolysaccharides (LPS)‐differentiated microglia determined by one‐way analysis of variance (ANOVA) followed by post hoc Tukey–Cramer's test. *** p
    Figure Legend Snippet: Influence of Kv1.3 expression on membrane potential changes. (a) Corresponding voltage‐clamp ( top ) and current‐clamp ( bottom ) traces induced by 0.1 mM ATP from three individual microglia. (b) Scatterplots for resting membrane potential (RMP) and ATP‐induced membrane potential (AMP). RMP's measured in undifferentiated cells and lipopolysaccharides (LPS)‐differentiated cells averaged −88.08 ± 5.14 mV ( n = 27) and −67.64 ± 12.62 mV ( n = 28), respectively. AMP's in undifferentiated cells and LPS‐differentiated cells averaged −19.32 ± 14.49 mV and −44.09 ± 7.67 mV, respectively. Data represented by means ± SD . Statistical significance between before and after ATP addition determined by paired t test and between undifferentiated and lipopolysaccharides (LPS)‐differentiated microglia determined by one‐way analysis of variance (ANOVA) followed by post hoc Tukey–Cramer's test. *** p

    Techniques Used: Expressing

    Expression changes of Kv1.3 channels and P2X4 receptors in in microglia isolated from Cx3CR1 +/EGFP transgenic mice 8 days after middle cerebral artery occlusion (MCAO) as a model of ischemic stroke. Sample immunofluorescence staining of 14‐μM thick coronal brain sections from the 6‐mm depth showing (a) increased Kv1.3 ( red ) and (b) P2X4 ( red ) immunoreactivity in ipsilateral Cx3CR1 +/EGFP ( green ) cells but not contralateral cells. Each channel was analyzed on n = 3–4 coronal sections from N = 3 male and 3 female mice. (c) P2X4 (d) Kv1.3 and (e) Kir2.1 current densities measured from CD11b + Cx3CR1 +/EGFP microglia acutely isolated from the ipsilateral hemisphere (8 days after MCAO) compared to microglia isolated from the contralateral side. Statistical significance determined by one‐way analysis of variance (ANOVA) followed by Tukey–Cramer's post hoc (alpha = 0.05). * p
    Figure Legend Snippet: Expression changes of Kv1.3 channels and P2X4 receptors in in microglia isolated from Cx3CR1 +/EGFP transgenic mice 8 days after middle cerebral artery occlusion (MCAO) as a model of ischemic stroke. Sample immunofluorescence staining of 14‐μM thick coronal brain sections from the 6‐mm depth showing (a) increased Kv1.3 ( red ) and (b) P2X4 ( red ) immunoreactivity in ipsilateral Cx3CR1 +/EGFP ( green ) cells but not contralateral cells. Each channel was analyzed on n = 3–4 coronal sections from N = 3 male and 3 female mice. (c) P2X4 (d) Kv1.3 and (e) Kir2.1 current densities measured from CD11b + Cx3CR1 +/EGFP microglia acutely isolated from the ipsilateral hemisphere (8 days after MCAO) compared to microglia isolated from the contralateral side. Statistical significance determined by one‐way analysis of variance (ANOVA) followed by Tukey–Cramer's post hoc (alpha = 0.05). * p

    Techniques Used: Expressing, Isolation, Transgenic Assay, Mouse Assay, Immunofluorescence, Staining

    Kv1.3 blockade depolarizes microglia and disrupts resistance to ATP‐induced membrane depolarization. (a) Kv1.3 inhibitors do not cross‐react with P2X4. Sample recording of P2X4 currents elicited by 0.1 mM ATP in a Chinese Hamster Ovary (CHO) cell at the 0, 5, and 10‐min time points displaying characteristic time‐dependent current rundown. (b) Bar graphs showing normalized current for control cells ( n = 5), PAP‐1 (1 μM) treated cells ( n = 4), and ShK‐223 (100 nM) treated cells ( n = 5). Inhibitors were added immediately after the first ATP pulse and remained in the recording chamber throughout the duration between and during subsequent ATP pulses. Error bars denote means ± SD . (c) Voltage‐clamp currents before and after inhibition of Kv1.3 with 100 nM ShK‐223 in an undifferentiated microglial cell. (g) Current‐clamp displaying ATP‐induced depolarization (AID) of resting membrane potential (RMP) before and after ShK‐223 in the same undifferentiated cell. (e) Scatterplots summarizing RMP and AMP levels before and after ShK‐223 for undifferentiated cells ( n = 14). (f) Voltage‐clamp currents before and after inhibition of Kv1.3 with 100 nM ShK‐223 in an lipopolysaccharides (LPS)‐stimulated microglial cell. (g) Current‐clamp displaying AID of RMP before and after ShK‐223 in the same LPS‐stimulated cell. (h) Scatterplots summarizing RMP and AMP levels for LPS‐treated cells ( n = 8). Statistical significance determined by paired t test. *** p
    Figure Legend Snippet: Kv1.3 blockade depolarizes microglia and disrupts resistance to ATP‐induced membrane depolarization. (a) Kv1.3 inhibitors do not cross‐react with P2X4. Sample recording of P2X4 currents elicited by 0.1 mM ATP in a Chinese Hamster Ovary (CHO) cell at the 0, 5, and 10‐min time points displaying characteristic time‐dependent current rundown. (b) Bar graphs showing normalized current for control cells ( n = 5), PAP‐1 (1 μM) treated cells ( n = 4), and ShK‐223 (100 nM) treated cells ( n = 5). Inhibitors were added immediately after the first ATP pulse and remained in the recording chamber throughout the duration between and during subsequent ATP pulses. Error bars denote means ± SD . (c) Voltage‐clamp currents before and after inhibition of Kv1.3 with 100 nM ShK‐223 in an undifferentiated microglial cell. (g) Current‐clamp displaying ATP‐induced depolarization (AID) of resting membrane potential (RMP) before and after ShK‐223 in the same undifferentiated cell. (e) Scatterplots summarizing RMP and AMP levels before and after ShK‐223 for undifferentiated cells ( n = 14). (f) Voltage‐clamp currents before and after inhibition of Kv1.3 with 100 nM ShK‐223 in an lipopolysaccharides (LPS)‐stimulated microglial cell. (g) Current‐clamp displaying AID of RMP before and after ShK‐223 in the same LPS‐stimulated cell. (h) Scatterplots summarizing RMP and AMP levels for LPS‐treated cells ( n = 8). Statistical significance determined by paired t test. *** p

    Techniques Used: Inhibition

    4) Product Images from "Potassium secretion by voltage-gated potassium channel Kv1.3 in the rat kidney"

    Article Title: Potassium secretion by voltage-gated potassium channel Kv1.3 in the rat kidney

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00697.2009

    Kv1.3 expression in collecting duct intercalated cells from kidneys of HK-fed rats. Shown is detection of principal cells with Dolichus biflorus aggutinin coupled to fluorescein (DBA-F; A ; green), intercalated cells with goat-anti-B1-H-VATPase antibody ( D and G ; green), and Kv1.3 with an anti-Kv1.3 antibody ( B , E , and H ; red) in collecting ducts of HK-fed rats by indirect immunofluorescence confocal microscopy. Note that Kv1.3 is localized only to cells lacking DBA-F staining ( C ; merged) and in presumably intercalated cells expressing apical H + -VATPase ( F and I ; merged). Arrows point to apical Kv1.3-H + -VATPase colocalization (yellow). Bars = 25 μm.
    Figure Legend Snippet: Kv1.3 expression in collecting duct intercalated cells from kidneys of HK-fed rats. Shown is detection of principal cells with Dolichus biflorus aggutinin coupled to fluorescein (DBA-F; A ; green), intercalated cells with goat-anti-B1-H-VATPase antibody ( D and G ; green), and Kv1.3 with an anti-Kv1.3 antibody ( B , E , and H ; red) in collecting ducts of HK-fed rats by indirect immunofluorescence confocal microscopy. Note that Kv1.3 is localized only to cells lacking DBA-F staining ( C ; merged) and in presumably intercalated cells expressing apical H + -VATPase ( F and I ; merged). Arrows point to apical Kv1.3-H + -VATPase colocalization (yellow). Bars = 25 μm.

    Techniques Used: Expressing, Immunofluorescence, Confocal Microscopy, Staining

    Dietary K + intake has no effect on Kv1.3 channel transcript and protein expression. A : real-time PCR assays were performed to detect the relative abundance of Kv1.3 transcript in Cx, OM, and IM from rats fed control K + (CK) and high-K + (HK) diets. There was no significant difference in the Kv1.3 mRNA expression in any region between the CK and HK groups ( n = 6). B : representative Western blot showing Kv1.3 in crude membranes from Cx, OM, and IM from rats CK and HK diets. Crude protein (30 μg) was loaded on each lane. No differences were observed in Kv1.3 protein expression between the CK and HK groups.
    Figure Legend Snippet: Dietary K + intake has no effect on Kv1.3 channel transcript and protein expression. A : real-time PCR assays were performed to detect the relative abundance of Kv1.3 transcript in Cx, OM, and IM from rats fed control K + (CK) and high-K + (HK) diets. There was no significant difference in the Kv1.3 mRNA expression in any region between the CK and HK groups ( n = 6). B : representative Western blot showing Kv1.3 in crude membranes from Cx, OM, and IM from rats CK and HK diets. Crude protein (30 μg) was loaded on each lane. No differences were observed in Kv1.3 protein expression between the CK and HK groups.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot

    Effect of dietary K + intake on Kv1.3 expression in plasma membranes. A : representative immunoblot of Kv1.3 in plasma membranes from Cx, OM, and IM of rats fed CK and HK diets. Thirty micrograms of protein was loaded on each lane. B : significant relative increase was detected in the 3 regions of kidney studied in response to dietary K + loading, suggesting increased trafficking or stability of Kv1.3 protein to/on plasma membranes. Values are mean ± SE; n = 6/dietary group. * P
    Figure Legend Snippet: Effect of dietary K + intake on Kv1.3 expression in plasma membranes. A : representative immunoblot of Kv1.3 in plasma membranes from Cx, OM, and IM of rats fed CK and HK diets. Thirty micrograms of protein was loaded on each lane. B : significant relative increase was detected in the 3 regions of kidney studied in response to dietary K + loading, suggesting increased trafficking or stability of Kv1.3 protein to/on plasma membranes. Values are mean ± SE; n = 6/dietary group. * P

    Techniques Used: Expressing

    Immunohistochemistry of Kv1.3 in the kidney Cx in rats fed CK ( A ) and HK diets ( B ). Cortical collecting ducts (CCDs) are observed with positive cytoplasmic ( A ) and polarized ( B , arrows) immunoreactivity. Higher magnification shows a cytoplasmic distribution in all CCD cells of Kv1.3 in CK rats ( C ); the inset at the bottom left shows a negative control (preincubation of the anti-Kv1.3 antibody with the control peptide). The HK diet enhances apical expression of Kv1.3 in a few cells ( D , arrows). Bars = 50 μm.
    Figure Legend Snippet: Immunohistochemistry of Kv1.3 in the kidney Cx in rats fed CK ( A ) and HK diets ( B ). Cortical collecting ducts (CCDs) are observed with positive cytoplasmic ( A ) and polarized ( B , arrows) immunoreactivity. Higher magnification shows a cytoplasmic distribution in all CCD cells of Kv1.3 in CK rats ( C ); the inset at the bottom left shows a negative control (preincubation of the anti-Kv1.3 antibody with the control peptide). The HK diet enhances apical expression of Kv1.3 in a few cells ( D , arrows). Bars = 50 μm.

    Techniques Used: Immunohistochemistry, Negative Control, Expressing

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    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: 93/100, 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
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti kv1 3 antibody - by Bioz Stars, 2022-07
    93/100 stars
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    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:

    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

    Recognition of Kv1.3 protein by α-AU13 antiserum by Western blot analysis Cell lysates from Kv1.3 transfected HEK293 cells, separated by SDS-PAGE and visualized by Western blot analysis with various dilutions of the antiserum from 1 : 500 to 1:10 000.

    Journal: The Journal of Physiology

    Article Title: Neurotrophin modulation of voltage-gated potassium channels in rat through TrkB receptors is time and sensory experience dependent

    doi: 10.1113/jphysiol.2002.017376

    Figure Lengend Snippet: Recognition of Kv1.3 protein by α-AU13 antiserum by Western blot analysis Cell lysates from Kv1.3 transfected HEK293 cells, separated by SDS-PAGE and visualized by Western blot analysis with various dilutions of the antiserum from 1 : 500 to 1:10 000.

    Article Snippet: Second, the antiserum generated against Kv1.3 (α-AU13; see Methods), as well as several other anti-Kv1.3 antisera that were either internally generated (α-AU11 and α-AU12) or commercially available (Alomone Laboratories), were tested for the ability to recognize cloned Kv1.3 protein as transiently expressed in HEK293 cells and visualized in Western blots. α-AU13 specifically recognized Kv1.3 at serial dilutions of the antiserum from 1 : 500 to 1 : 10 000 ( ) and was therefore the antibody used in all subsequent experiments. α-AU13 was further characterized in native olfactory bulb membranes, where the appropriate molecular weight band was preabsorbed by incubation with the 46 amino acid peptide used to generate the antiserum (data not shown).

    Techniques: Western Blot, Transfection, SDS Page

    Sensory deprivation by unilateral naris occlusion alters BDNF-stimulated tyrosine phosphorylation of Kv1.3 channel P1 animals were left naris occluded by cauterization and raised with odour sensory deprivation to this naris from P20 to P25. A , olfactory bulbs contralateral (non-occluded) and ipsilateral (occluded) to the cauterized naris were then harvested, stimulated with BDNF and immunoprecipitated with anti-Kv1.3 and blotted with anti-4G10. Total tyrosine phosphorylation of Kv1.3 is indicated by the arrow. B , histogram of the mean increase in tyrosine phosphorylation of Kv1.3 by acute BDNF stimulation comparing non-occluded versus sensory-deprived conditions (occluded). Pixel values were calculated by quantitative densitometry. The difference in pixel density between unstimulated and BDNF-stimulated olfactory bulbs was plotted for occluded and non-occluded naris conditions, where 0 = no change in Kv1.3 phosphorylation with BDNF treatment. * Significantly different by Student's paired t test, P

    Journal: The Journal of Physiology

    Article Title: Neurotrophin modulation of voltage-gated potassium channels in rat through TrkB receptors is time and sensory experience dependent

    doi: 10.1113/jphysiol.2002.017376

    Figure Lengend Snippet: Sensory deprivation by unilateral naris occlusion alters BDNF-stimulated tyrosine phosphorylation of Kv1.3 channel P1 animals were left naris occluded by cauterization and raised with odour sensory deprivation to this naris from P20 to P25. A , olfactory bulbs contralateral (non-occluded) and ipsilateral (occluded) to the cauterized naris were then harvested, stimulated with BDNF and immunoprecipitated with anti-Kv1.3 and blotted with anti-4G10. Total tyrosine phosphorylation of Kv1.3 is indicated by the arrow. B , histogram of the mean increase in tyrosine phosphorylation of Kv1.3 by acute BDNF stimulation comparing non-occluded versus sensory-deprived conditions (occluded). Pixel values were calculated by quantitative densitometry. The difference in pixel density between unstimulated and BDNF-stimulated olfactory bulbs was plotted for occluded and non-occluded naris conditions, where 0 = no change in Kv1.3 phosphorylation with BDNF treatment. * Significantly different by Student's paired t test, P

    Article Snippet: Second, the antiserum generated against Kv1.3 (α-AU13; see Methods), as well as several other anti-Kv1.3 antisera that were either internally generated (α-AU11 and α-AU12) or commercially available (Alomone Laboratories), were tested for the ability to recognize cloned Kv1.3 protein as transiently expressed in HEK293 cells and visualized in Western blots. α-AU13 specifically recognized Kv1.3 at serial dilutions of the antiserum from 1 : 500 to 1 : 10 000 ( ) and was therefore the antibody used in all subsequent experiments. α-AU13 was further characterized in native olfactory bulb membranes, where the appropriate molecular weight band was preabsorbed by incubation with the 46 amino acid peptide used to generate the antiserum (data not shown).

    Techniques: Immunoprecipitation

    Acute BDNF stimulation increases the tyrosine phosphorylation of Kv1.3 in the rat olfactory bulb A , olfactory bulbs were stimulated with or without 100 ng ml −1 of BDNF in PBS for 20 min, homogenized, immunoprecipitated with anti-phosphotyrosine antiserum (anti-4G10), separated by SDS-PAGE, and Western blots were probed with anti-Kv1.3 (α-AU13). Total tyrosine phosphorylation of Kv1.3 is shown in the bottom panel. The heavy chain of IgG is also indicated below that of Kv1.3. Ten micrograms of cell lysate were blotted for α-AU13 and α-TrkB, respectively, to confirm equivalent protein expression of the channel and receptor under BDNF-stimulated and unstimulated conditions (top panels). B , histogram of quantitative densitometry of four experiments as in A . Mean pixel density of Kv1.3 tyrosine phosphorylation under control versus BDNF-stimulated conditions. * Significantly different, Arc Sin transformation for percentile data, Student's t test P

    Journal: The Journal of Physiology

    Article Title: Neurotrophin modulation of voltage-gated potassium channels in rat through TrkB receptors is time and sensory experience dependent

    doi: 10.1113/jphysiol.2002.017376

    Figure Lengend Snippet: Acute BDNF stimulation increases the tyrosine phosphorylation of Kv1.3 in the rat olfactory bulb A , olfactory bulbs were stimulated with or without 100 ng ml −1 of BDNF in PBS for 20 min, homogenized, immunoprecipitated with anti-phosphotyrosine antiserum (anti-4G10), separated by SDS-PAGE, and Western blots were probed with anti-Kv1.3 (α-AU13). Total tyrosine phosphorylation of Kv1.3 is shown in the bottom panel. The heavy chain of IgG is also indicated below that of Kv1.3. Ten micrograms of cell lysate were blotted for α-AU13 and α-TrkB, respectively, to confirm equivalent protein expression of the channel and receptor under BDNF-stimulated and unstimulated conditions (top panels). B , histogram of quantitative densitometry of four experiments as in A . Mean pixel density of Kv1.3 tyrosine phosphorylation under control versus BDNF-stimulated conditions. * Significantly different, Arc Sin transformation for percentile data, Student's t test P

    Article Snippet: Second, the antiserum generated against Kv1.3 (α-AU13; see Methods), as well as several other anti-Kv1.3 antisera that were either internally generated (α-AU11 and α-AU12) or commercially available (Alomone Laboratories), were tested for the ability to recognize cloned Kv1.3 protein as transiently expressed in HEK293 cells and visualized in Western blots. α-AU13 specifically recognized Kv1.3 at serial dilutions of the antiserum from 1 : 500 to 1 : 10 000 ( ) and was therefore the antibody used in all subsequent experiments. α-AU13 was further characterized in native olfactory bulb membranes, where the appropriate molecular weight band was preabsorbed by incubation with the 46 amino acid peptide used to generate the antiserum (data not shown).

    Techniques: Immunoprecipitation, SDS Page, Western Blot, Expressing, Transformation Assay

    Fyn modulates the posttranslational modification of Kv1.3. (A) Western blot analysis of postmortem human PD and age-matched control brains showing increased phosphorylation of Kv1.3. (B) Immunoprecipitation of Fyn and Kv1.3 showing direct Fyn-Kv1.3 interaction after αSyn Agg treatment. ( C ) Duolink PLA showing αSyn Agg -induced interaction between Kv1.3 and Fyn. Scale bar: 25 μm. ( D ) Western blot of Fyn WT and KO PMCs revealed that Kv1.3 phosphorylation at residue 135 was Fyn dependent. ( E ) IHC analysis of substantia nigra from Fyn +/+ and Fyn –/– mice showing reduced phosphorylation of Kv1.3 after αSyn PFF injection. Scale bars: 100 μm; 60 μm (insets). ( F ) IHC of substantia nigra from MitoPark mice and their littermate controls showing that pharmacological inhibition of Fyn by saracatinib reduced Kv1.3 phosphorylation. Scale bar: 100 μm. ( G – J ) Immortalized MMCs were either transfected with WT Kv1.3 or aY135A Kv1.3 plasmid. ( G ) qRT-PCR analysis and ( H ) Griess assay showing reduced levels of inducible NOS (iNOS) and nitrite release, respectively, in Y135A Kv1.3-transfected cells compared with WT cells. ( I ) qRT-PCR analysis showing reduced IL-1β production in Y135A Kv1.3–transfected versus WT Kv1.3–transfected MMCs. ( J ) Luminex assay showing reduced IL-1β secretion in Y135A Kv1.3–transfected compared with WT Kv1.3–transfected MMCs. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. A 2-tailed Student’s t test was used to compare 2 groups in A . Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–4 biological replicates from 2–3 independent experiments. * P ≤ 0.05, ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Fyn modulates the posttranslational modification of Kv1.3. (A) Western blot analysis of postmortem human PD and age-matched control brains showing increased phosphorylation of Kv1.3. (B) Immunoprecipitation of Fyn and Kv1.3 showing direct Fyn-Kv1.3 interaction after αSyn Agg treatment. ( C ) Duolink PLA showing αSyn Agg -induced interaction between Kv1.3 and Fyn. Scale bar: 25 μm. ( D ) Western blot of Fyn WT and KO PMCs revealed that Kv1.3 phosphorylation at residue 135 was Fyn dependent. ( E ) IHC analysis of substantia nigra from Fyn +/+ and Fyn –/– mice showing reduced phosphorylation of Kv1.3 after αSyn PFF injection. Scale bars: 100 μm; 60 μm (insets). ( F ) IHC of substantia nigra from MitoPark mice and their littermate controls showing that pharmacological inhibition of Fyn by saracatinib reduced Kv1.3 phosphorylation. Scale bar: 100 μm. ( G – J ) Immortalized MMCs were either transfected with WT Kv1.3 or aY135A Kv1.3 plasmid. ( G ) qRT-PCR analysis and ( H ) Griess assay showing reduced levels of inducible NOS (iNOS) and nitrite release, respectively, in Y135A Kv1.3-transfected cells compared with WT cells. ( I ) qRT-PCR analysis showing reduced IL-1β production in Y135A Kv1.3–transfected versus WT Kv1.3–transfected MMCs. ( J ) Luminex assay showing reduced IL-1β secretion in Y135A Kv1.3–transfected compared with WT Kv1.3–transfected MMCs. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. A 2-tailed Student’s t test was used to compare 2 groups in A . Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–4 biological replicates from 2–3 independent experiments. * P ≤ 0.05, ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: Modification, Western Blot, Immunoprecipitation, Proximity Ligation Assay, Immunohistochemistry, Mouse Assay, Injection, Inhibition, Transfection, Plasmid Preparation, Quantitative RT-PCR, Griess Assay, Luminex

    Kv1.3 inhibition protects against αSyn PFF -induced behavior deficit and dopaminergic neuronal loss. ( A ) Treatment paradigm corresponding to the αSyn PFF mouse model of PD. ( B ) Representative movement tracks showing that PAP-1 rescued movement deficits induced by αSyn PFF . ( C – E ) A VersaMax open-field test showed decreased ( C ) rest time and increased ( D ) horizontal activity and ( E ) total distance traveled for αSyn PFF mice treated with PAP-1. ( F and G ) HPLC showing that PAP-1 treatment protected against loss of ( F ) dopamine and ( G ) DOPAC induced by αSyn PFF . ( H ) Western blot analysis of TH showing loss of TH induced by αSyn PFF in the SNpc region. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–7 animals per group. * P ≤ 0.05, ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Kv1.3 inhibition protects against αSyn PFF -induced behavior deficit and dopaminergic neuronal loss. ( A ) Treatment paradigm corresponding to the αSyn PFF mouse model of PD. ( B ) Representative movement tracks showing that PAP-1 rescued movement deficits induced by αSyn PFF . ( C – E ) A VersaMax open-field test showed decreased ( C ) rest time and increased ( D ) horizontal activity and ( E ) total distance traveled for αSyn PFF mice treated with PAP-1. ( F and G ) HPLC showing that PAP-1 treatment protected against loss of ( F ) dopamine and ( G ) DOPAC induced by αSyn PFF . ( H ) Western blot analysis of TH showing loss of TH induced by αSyn PFF in the SNpc region. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–7 animals per group. * P ≤ 0.05, ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: Inhibition, Activity Assay, Mouse Assay, High Performance Liquid Chromatography, Western Blot

    Upregulated expression of the potassium channel Kv1.3 upon aggregated αSyn stimulation in ex vivo slices and B cells derived from patients with PD. ( A ) Midbrain slice cultures were treated with 1 μM αSyn Agg for 24 hours. qRT-PCR shows upregulated Kv1.3 mRNA expression. ( B ) Western blot shows upregulated Kv1.3 protein level in midbrain slice cultures treated with 1 μM αSyn Agg for 24 hours. ( C ) qRT-PCR of midbrain slice cultures treated with 1 μM αSyn Agg for 24 hours, revealing upregulation of the proinflammatory factors Nos2 , Csf2 , IL-6 , IL-1β , and Tnfa . ( D ) qRT-PCR shows increased Kv1.3 mRNA expression in B cell lymphocytes isolated from patients with PD compared with expression in B cell lymphocytes from age-matched controls. ( E ) Whole-cell patch clamping of B cell lymphocytes isolated from patients with PD showed higher Kv1.3 channel activity compared with that observed in age-matched controls ( n = 3 control and n = 3 PD). A 1-way ANOVA was used to compare multiple groups in C and D . Tukey’s post hoc analysis was applied. A 2-tailed Student’s t test was used to compare 2 groups. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–7 biological replicates from 2–3 independent experiments unless otherwise indicated. * P ≤ 0.05 and ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Upregulated expression of the potassium channel Kv1.3 upon aggregated αSyn stimulation in ex vivo slices and B cells derived from patients with PD. ( A ) Midbrain slice cultures were treated with 1 μM αSyn Agg for 24 hours. qRT-PCR shows upregulated Kv1.3 mRNA expression. ( B ) Western blot shows upregulated Kv1.3 protein level in midbrain slice cultures treated with 1 μM αSyn Agg for 24 hours. ( C ) qRT-PCR of midbrain slice cultures treated with 1 μM αSyn Agg for 24 hours, revealing upregulation of the proinflammatory factors Nos2 , Csf2 , IL-6 , IL-1β , and Tnfa . ( D ) qRT-PCR shows increased Kv1.3 mRNA expression in B cell lymphocytes isolated from patients with PD compared with expression in B cell lymphocytes from age-matched controls. ( E ) Whole-cell patch clamping of B cell lymphocytes isolated from patients with PD showed higher Kv1.3 channel activity compared with that observed in age-matched controls ( n = 3 control and n = 3 PD). A 1-way ANOVA was used to compare multiple groups in C and D . Tukey’s post hoc analysis was applied. A 2-tailed Student’s t test was used to compare 2 groups. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–7 biological replicates from 2–3 independent experiments unless otherwise indicated. * P ≤ 0.05 and ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: Expressing, Ex Vivo, Derivative Assay, Quantitative RT-PCR, Western Blot, Isolation, Activity Assay

    Kv1.3 expression is highly induced in microglial cells in experimental models of PD and postmortem PD brains. ( A ) Western blot showing increased Kv1.3 protein levels in the substantia nigra of the Syn-AAV mouse model of PD. ( B ) qRT-PCR analysis of 8- to 24-week-old nigral tissues from the MitoPark mouse model of PD showing Kv1.3 induction compared with age-matched littermate controls. ( C ) Western blot of 24-week-old nigral tissues from the MitoPark mouse model of PD (MP) showing induction of Kv1.3 protein expression compared with age-matched littermate control mice (LM). ( D ) IHC in 24-week-old nigral tissues from the MitoPark mouse model of PD showing higher Kv1.3 protein levels (red) in IBA1-positive microglial cells (green) compared with age-matched controls as revealed by their colocalization (yellow). Scale bar: 20 μm. ( E ) qRT-PCR analysis of nigral tissues from the MPTP mouse model revealing induction of Kv1.3 mRNA expression. ( F ) Western blot showing increased Kv1.3 protein levels in substantia nigra of the MPTP mouse model of PD. ( G ) qRT-PCR analysis of postmortem human PD brains showing elevated Kv1.3 mRNA expression. ( H ) Western blot of the SN region of postmortem human PD brain showing induction of Kv1.3 protein expression compared with age-matched controls. n = 6–8. ( I ) Immunostaining revealing higher Kv1.3 levels in the prefrontal cortex of postmortem human PD brains compared with age-matched controls. Lower panel shows the deconvoluted binary image used for analysis. Three regions per brain were analyzed. Scale bar: 200 μm. ( J ) Dual DAB staining showing induction of Kv1.3 expression in HLA-DR–positive microglial cells in patients with DLBs compared with age-matched controls. Scale bars: 100 μm; 20 μm (enlarged insets). A 1-way ANOVA was used to compare multiple groups. Tukey’s post hoc analysis was applied B . A 2-tailed Student’s t test was used to compare 2 groups. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–9 biological replicates from 2–3 independent experiments unless otherwise indicated. * P ≤ 0.05, ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Kv1.3 expression is highly induced in microglial cells in experimental models of PD and postmortem PD brains. ( A ) Western blot showing increased Kv1.3 protein levels in the substantia nigra of the Syn-AAV mouse model of PD. ( B ) qRT-PCR analysis of 8- to 24-week-old nigral tissues from the MitoPark mouse model of PD showing Kv1.3 induction compared with age-matched littermate controls. ( C ) Western blot of 24-week-old nigral tissues from the MitoPark mouse model of PD (MP) showing induction of Kv1.3 protein expression compared with age-matched littermate control mice (LM). ( D ) IHC in 24-week-old nigral tissues from the MitoPark mouse model of PD showing higher Kv1.3 protein levels (red) in IBA1-positive microglial cells (green) compared with age-matched controls as revealed by their colocalization (yellow). Scale bar: 20 μm. ( E ) qRT-PCR analysis of nigral tissues from the MPTP mouse model revealing induction of Kv1.3 mRNA expression. ( F ) Western blot showing increased Kv1.3 protein levels in substantia nigra of the MPTP mouse model of PD. ( G ) qRT-PCR analysis of postmortem human PD brains showing elevated Kv1.3 mRNA expression. ( H ) Western blot of the SN region of postmortem human PD brain showing induction of Kv1.3 protein expression compared with age-matched controls. n = 6–8. ( I ) Immunostaining revealing higher Kv1.3 levels in the prefrontal cortex of postmortem human PD brains compared with age-matched controls. Lower panel shows the deconvoluted binary image used for analysis. Three regions per brain were analyzed. Scale bar: 200 μm. ( J ) Dual DAB staining showing induction of Kv1.3 expression in HLA-DR–positive microglial cells in patients with DLBs compared with age-matched controls. Scale bars: 100 μm; 20 μm (enlarged insets). A 1-way ANOVA was used to compare multiple groups. Tukey’s post hoc analysis was applied B . A 2-tailed Student’s t test was used to compare 2 groups. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–9 biological replicates from 2–3 independent experiments unless otherwise indicated. * P ≤ 0.05, ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: Expressing, Western Blot, Quantitative RT-PCR, Mouse Assay, Immunohistochemistry, Immunostaining, Staining

    Fyn modulates the transcriptional regulation of Kv1.3 in microglial cells through the Fyn/PKCδ kinase signaling cascade. ( A ) In silico analysis of the promoter sequence of Kv1.3 revealed probable Nf-κB– and SP1-binding sites. ( B ) qRT-PCR analysis of immortalized MMCs cotreated with αSyn Agg and either SN50 (100 μg/mL) or SB203580 (1 μM), showing that both compounds attenuated αSyn Agg -induced Kv1.3 expression. ( C ) Western blot of Fyn WT and KO PMCs treated with αSyn Agg , showing that Fyn KO reduced the induction of the p38 MAPK pathway. ( D ) qRT-PCR analysis revealed that Fyn KO reduced αSyn Agg -induced Kv1.3 mRNA levels. ( E ) Whole-cell patch-clamp recording showing that Fyn KO attenuated αSyn Agg - and LPS-induced Kv1.3 activity compared with Fyn WT PMCs (WT control n = 24, WT αSyn Agg n = 12, WT LPS n = 29, Fyn KO αSyn Agg n = 20, Fyn KO LPS n = 15). ( F ) ICC showing that Fyn KO reduced αSyn Agg -induced Kv1.3 protein levels in PMCs. Scale bar: 15 μm. ( G ) ICC of PMCs revealed that αSyn Agg -induced Kv1.3 protein expression was reduced by PKCδ KO. Scale bar: 15 μm. ( H ) qRT-PCR analysis of PMCs showing that PKC KO reduced the expression of αSyn Agg -induced Kv1.3 mRNA. ( I ) Whole-cell patch clam recording of PMCs showing that PKC KO attenuated αSyn Agg - and LPS-induced Kv1.3 activity compared with PKC WT PMCs (WT control n = 24, WT αSyn Agg n = 12, WT LPS n = 20, PKC-KO αSyn Agg n = 29, PKC-KO LPS n = 35). Data are presented as the mean ± SD. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–4 biological replicates from 2–3 independent experiments unless otherwise indicated. * P ≤ 0.05, ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Fyn modulates the transcriptional regulation of Kv1.3 in microglial cells through the Fyn/PKCδ kinase signaling cascade. ( A ) In silico analysis of the promoter sequence of Kv1.3 revealed probable Nf-κB– and SP1-binding sites. ( B ) qRT-PCR analysis of immortalized MMCs cotreated with αSyn Agg and either SN50 (100 μg/mL) or SB203580 (1 μM), showing that both compounds attenuated αSyn Agg -induced Kv1.3 expression. ( C ) Western blot of Fyn WT and KO PMCs treated with αSyn Agg , showing that Fyn KO reduced the induction of the p38 MAPK pathway. ( D ) qRT-PCR analysis revealed that Fyn KO reduced αSyn Agg -induced Kv1.3 mRNA levels. ( E ) Whole-cell patch-clamp recording showing that Fyn KO attenuated αSyn Agg - and LPS-induced Kv1.3 activity compared with Fyn WT PMCs (WT control n = 24, WT αSyn Agg n = 12, WT LPS n = 29, Fyn KO αSyn Agg n = 20, Fyn KO LPS n = 15). ( F ) ICC showing that Fyn KO reduced αSyn Agg -induced Kv1.3 protein levels in PMCs. Scale bar: 15 μm. ( G ) ICC of PMCs revealed that αSyn Agg -induced Kv1.3 protein expression was reduced by PKCδ KO. Scale bar: 15 μm. ( H ) qRT-PCR analysis of PMCs showing that PKC KO reduced the expression of αSyn Agg -induced Kv1.3 mRNA. ( I ) Whole-cell patch clam recording of PMCs showing that PKC KO attenuated αSyn Agg - and LPS-induced Kv1.3 activity compared with PKC WT PMCs (WT control n = 24, WT αSyn Agg n = 12, WT LPS n = 20, PKC-KO αSyn Agg n = 29, PKC-KO LPS n = 35). Data are presented as the mean ± SD. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–4 biological replicates from 2–3 independent experiments unless otherwise indicated. * P ≤ 0.05, ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: In Silico, Sequencing, Binding Assay, Quantitative RT-PCR, Expressing, Western Blot, Patch Clamp, Activity Assay, Immunocytochemistry

    Kv1.3 modulates neuroinflammation in a cell culture model of PD. ( A – C ) Kv1.3 WT and KO PMCs were treated with 1 μM αSyn Agg for 24 hours. Luminex analysis shows that Kv1.3 KO reduced the release of the αSyn Agg -induced proinflammatory factors ( A ) TNF-α, ( B ) IL-12, and ( C ) IL-1β. ( D – H ) Immortalized MMCs were transfected with WT a Kv1.3 plasmid, and then 48 hours after transfection, cells were treated with 1 μM αSyn Agg for 24 hours. ( D – F ) qRT-PCR analysis showing that Kv1.3 overexpression aggravated αSyn Agg -induced production of the proinflammatory factors ( D ) Nos2 , ( E ) pro– IL-1β , and ( F ) TNF-α . ( G and H ) Luminex analysis showing that Kv1.3 overexpression potentiated the release of the proinflammatory factors ( G ) IL-6 and ( H ) IL-12. ( I ) Voltage ramp from –120 mV to 40 mV elicited a characteristic outward rectifying current in αSyn Agg -treated microglia that was sensitive to the Kv1.3-selective inhibitor PAP-1. ( J ) LDH assay showing that PAP-1 reduced αSyn Agg -induced LDH release from microglial cells. ( K – M ) Luminex assay revealing that PAP-1 attenuated the αSyn Agg -induced proinflammatory factors ( K ) IL-12, ( L ) TNF-α, and ( M ) IL-6. ( N ) Western blot analysis demonstrating that PAP-1 reduced αSyn Agg -induced NLRP3 expression. ( O ) ICC analysis revealed that PAP-1 reduced NLRP3 expression induced by αSyn Agg . Scale bar: 25 μm. A 1-way ANOVA was performed to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–4 biological replicates from 2–3 independent experiments. * P ≤ 0.05, ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Kv1.3 modulates neuroinflammation in a cell culture model of PD. ( A – C ) Kv1.3 WT and KO PMCs were treated with 1 μM αSyn Agg for 24 hours. Luminex analysis shows that Kv1.3 KO reduced the release of the αSyn Agg -induced proinflammatory factors ( A ) TNF-α, ( B ) IL-12, and ( C ) IL-1β. ( D – H ) Immortalized MMCs were transfected with WT a Kv1.3 plasmid, and then 48 hours after transfection, cells were treated with 1 μM αSyn Agg for 24 hours. ( D – F ) qRT-PCR analysis showing that Kv1.3 overexpression aggravated αSyn Agg -induced production of the proinflammatory factors ( D ) Nos2 , ( E ) pro– IL-1β , and ( F ) TNF-α . ( G and H ) Luminex analysis showing that Kv1.3 overexpression potentiated the release of the proinflammatory factors ( G ) IL-6 and ( H ) IL-12. ( I ) Voltage ramp from –120 mV to 40 mV elicited a characteristic outward rectifying current in αSyn Agg -treated microglia that was sensitive to the Kv1.3-selective inhibitor PAP-1. ( J ) LDH assay showing that PAP-1 reduced αSyn Agg -induced LDH release from microglial cells. ( K – M ) Luminex assay revealing that PAP-1 attenuated the αSyn Agg -induced proinflammatory factors ( K ) IL-12, ( L ) TNF-α, and ( M ) IL-6. ( N ) Western blot analysis demonstrating that PAP-1 reduced αSyn Agg -induced NLRP3 expression. ( O ) ICC analysis revealed that PAP-1 reduced NLRP3 expression induced by αSyn Agg . Scale bar: 25 μm. A 1-way ANOVA was performed to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–4 biological replicates from 2–3 independent experiments. * P ≤ 0.05, ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: Cell Culture, Luminex, Transfection, Plasmid Preparation, Quantitative RT-PCR, Over Expression, Lactate Dehydrogenase Assay, Western Blot, Expressing, Immunocytochemistry

    Upregulated expression of the potassium channel Kv1.3 upon aggregated αSyn stimulation in microglial cells in vitro. ( A ) Whole-cell patch-clamp recordings of PMCs treated with 1 μM αSyn Agg for 24–48 hours, showing αSyn Agg -induced increased Kv1.3 activity (control n = 24 and αSyn Agg n = 12). Kv1.3 was identified by its characteristic use dependence, which was revealed when applying a train of ten 200-ms pulses from –80 to 40 mV at 1-second intervals (1 Hz). ( B ) qRT-PCR showing that αSyn Agg induced Kv1.3 mRNA expression without significantly altering other potassium channels. ( C ) Western blot of αSyn Agg -induced Kv1.3 protein expression in PMCs. ( D ) ICC of αSyn Agg -induced Kv1.3 protein expression in PMCs. Scale bar: 100 μm. ( E ) Flow cytometric analysis of immortalized MMCs treated with 1 μM αSyn Agg for 24 hours, showing αSyn Agg -induced Kv1.3 surface expression. ( F ) qRT-PCR of human microglia treated with LPS (1 μg/mL) and IL-4 (20 ng/mL) for 6 hours, showing LPS-induced Kv1.3 expression. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied in B and F . A 2-tailed Student’s t test was used for all other figures when comparing 2 groups. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–5 biological replicates from 2–3 independent experiments unless otherwise noted. * P ≤ 0.05, ** P

    Journal: The Journal of Clinical Investigation

    Article Title: Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease

    doi: 10.1172/JCI136174

    Figure Lengend Snippet: Upregulated expression of the potassium channel Kv1.3 upon aggregated αSyn stimulation in microglial cells in vitro. ( A ) Whole-cell patch-clamp recordings of PMCs treated with 1 μM αSyn Agg for 24–48 hours, showing αSyn Agg -induced increased Kv1.3 activity (control n = 24 and αSyn Agg n = 12). Kv1.3 was identified by its characteristic use dependence, which was revealed when applying a train of ten 200-ms pulses from –80 to 40 mV at 1-second intervals (1 Hz). ( B ) qRT-PCR showing that αSyn Agg induced Kv1.3 mRNA expression without significantly altering other potassium channels. ( C ) Western blot of αSyn Agg -induced Kv1.3 protein expression in PMCs. ( D ) ICC of αSyn Agg -induced Kv1.3 protein expression in PMCs. Scale bar: 100 μm. ( E ) Flow cytometric analysis of immortalized MMCs treated with 1 μM αSyn Agg for 24 hours, showing αSyn Agg -induced Kv1.3 surface expression. ( F ) qRT-PCR of human microglia treated with LPS (1 μg/mL) and IL-4 (20 ng/mL) for 6 hours, showing LPS-induced Kv1.3 expression. A 1-way ANOVA was used to compare multiple groups. In most cases, Tukey’s post hoc analysis was applied in B and F . A 2-tailed Student’s t test was used for all other figures when comparing 2 groups. Each dot on the bar graphs represents a biological replicate. Data are presented as the mean ± SEM, with 3–5 biological replicates from 2–3 independent experiments unless otherwise noted. * P ≤ 0.05, ** P

    Article Snippet: The primary antibodies included anti-Kv1.3 (Alomone Labs, 1:1000) (Research Resource Identifier [RRID]: AB_2040151), anti-Kv1.3 (MilliporeSigma 1:1000) (RRID: AB_2265087), anti–p-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_331641), anti-p38 (Cell Signaling Technology, 1:1000) (RRID: AB_330713), anti–p-Kv1.3 (MilliporeSigma, 1:1000, catalog SAB4504254), anti-PKCδ (Santa Cruz Biotechnology, 1:500) (RRID: AB_628145), anti-NLRP3 (AdipoGen, 1:1000) (RRID: AB_2490202), and anti–active MAPK (Promega, 1:2000).

    Techniques: Expressing, In Vitro, Patch Clamp, Activity Assay, Quantitative RT-PCR, Western Blot, Immunocytochemistry