machr  (Alomone Labs)


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    Structured Review

    Alomone Labs machr
    Machr, 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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    Average 93 stars, based on 1 article reviews
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    machr - by Bioz Stars, 2022-12
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    Alomone Labs anti kv1 3 kcna3 extracellular antibody
    Expression of <t>Kv1.3</t> in human pancreatic cancer tissue. Expression of Kv1.3 in human pancreatic tissue. Panel ( a ), high expression level of Kv1.3 in human pancreatic cancer tissue. ( n = 33 out of 55, scale bar = 50 µm). Panel ( b ), magnification of panel ( a ), scale bar = 20 µm. Panel ( c ), low expression level of Kv1.3 in human pancreatic cancer tissue. ( n = 22 out of 55, scale bar = 50 µm). Panel ( d ), magnification of panel c, scale bar = 20 µm. Panel ( e ), Immunoglobulin G (IgG) control with magnification (Panel ( f )). Panel ( g ) shows a pancreas adenocarcinoma ductule with high expression of Kv1.3 (brown color) and adjacent normal pancreas parenchyma without Kv1.3 expression (black arrow), scale bar = 50 µm. Panel ( h ), magnification of panel ( g ), scale bar = 20 µm.
    Anti Kv1 3 Kcna3 Extracellular Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti kv1 3 kcna3 extracellular antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti kv1 3 kcna3 extracellular antibody - by Bioz Stars, 2022-12
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    95
    Alomone Labs anti kv1 3 kcna3 antibody
    MSU effects on protein expression of K + channels and Hsp70, degradation of <t>Kv1.5</t> proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and <t>Kv1.3</t> proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p
    Anti Kv1 3 Kcna3 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/anti kv1 3 kcna3 antibody/product/Alomone Labs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti kv1 3 kcna3 antibody - by Bioz Stars, 2022-12
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    93
    Alomone Labs kv1 3 channel blocker margatoxin
    Mobility of wild type and mutant <t>Kv1.3</t> channels on Jurkat T cells forming immunological synapses with Raji B cells at resting membrane potential and upon depolarization. ( A ) Slow diffusion coefficients of the WT and NON-CON channels decreased significantly inside the IS. However, that of the C-terminally truncated (ΔC) mutant did not change significantly. We also studied the effect of a depolarizing milieu. The mobility of WT and ΔC channels decreased significantly upon depolarization by high-K + solution both inside and outside the IS. In contrast, the mobility of the NON-CON channels did not show significant alterations. ( B ) Average proportion of the slow diffusing component ( r slow ) was not significantly affected by being partitioned in the IS, by mutation, or by depolarization. * p
    Kv1 3 Channel Blocker Margatoxin, 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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    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    Expression of Kv1.3 in human pancreatic cancer tissue. Expression of Kv1.3 in human pancreatic tissue. Panel ( a ), high expression level of Kv1.3 in human pancreatic cancer tissue. ( n = 33 out of 55, scale bar = 50 µm). Panel ( b ), magnification of panel ( a ), scale bar = 20 µm. Panel ( c ), low expression level of Kv1.3 in human pancreatic cancer tissue. ( n = 22 out of 55, scale bar = 50 µm). Panel ( d ), magnification of panel c, scale bar = 20 µm. Panel ( e ), Immunoglobulin G (IgG) control with magnification (Panel ( f )). Panel ( g ) shows a pancreas adenocarcinoma ductule with high expression of Kv1.3 (brown color) and adjacent normal pancreas parenchyma without Kv1.3 expression (black arrow), scale bar = 50 µm. Panel ( h ), magnification of panel ( g ), scale bar = 20 µm.

    Journal: Cancers

    Article Title: Inhibition of a Mitochondrial Potassium Channel in Combination with Gemcitabine and Abraxane Drastically Reduces Pancreatic Ductal Adenocarcinoma in an Immunocompetent Orthotopic Murine Model

    doi: 10.3390/cancers14112618

    Figure Lengend Snippet: Expression of Kv1.3 in human pancreatic cancer tissue. Expression of Kv1.3 in human pancreatic tissue. Panel ( a ), high expression level of Kv1.3 in human pancreatic cancer tissue. ( n = 33 out of 55, scale bar = 50 µm). Panel ( b ), magnification of panel ( a ), scale bar = 20 µm. Panel ( c ), low expression level of Kv1.3 in human pancreatic cancer tissue. ( n = 22 out of 55, scale bar = 50 µm). Panel ( d ), magnification of panel c, scale bar = 20 µm. Panel ( e ), Immunoglobulin G (IgG) control with magnification (Panel ( f )). Panel ( g ) shows a pancreas adenocarcinoma ductule with high expression of Kv1.3 (brown color) and adjacent normal pancreas parenchyma without Kv1.3 expression (black arrow), scale bar = 50 µm. Panel ( h ), magnification of panel ( g ), scale bar = 20 µm.

    Article Snippet: Primary antibodies Kv1.3 (1:100, APC-101, Alomone labs, Jerusalem, Israel) and TOM20 (1:100, MABT166, Sigma, Burlington, MA, USA) were incubated overnight at 4 °C.

    Techniques: Expressing

    Mitochondrial Kv1.3 is expressed in the multiple myeloma cell lines L-363 and RPMI-8226. PAPTP and PCARBTP efficiently kill human multiple myeloma cells. ( a ) Whole cell lysates (left, 50 µg protein/lane) were lysed in RIPA-Buffer, mitochondria from L-363, RPMI-8226 and Jurkat cells (right, 30 µg protein/lane) were enriched as described; both were supplemented with 5× reducing SDS sample buffer, boiled and separated on 8.5% SDS-polyacrylamide gels and blotted on nitrocellulose membranes. Membranes were divided and, after blocking, membranes were incubated 1 h with anti-Kv1.3 or anti-Tim23 primary antibodies, respectively. After extensively washing, blots were incubated with secondary antibodies for 1 h, washed and developed with the Roti–Lumin system. Multiple myeloma cell lines RPMI-8226 and L-363 were treated with increasing concentrations PAPTP ( b ) or PCARBTP ( c ), solvent control (0.1% DMSO), 2 µM staurosporine as a positive control and 2 µM margatoxin as a membrane-impermeable Kv1.3 blocker. After 24 h, cells were stained with Annexin V-APC/7AAD and examined for cell death by flow cytometry. Results are reported as percentages with respect to untreated samples ± SD, ( n = 3 independent experiments, each experiment in triplicate). Graph insert EC50: EC50 values of the indicated compounds in RPMI-8226 and L-363 were calculated by using GraphPad Prism version 9.3 for Windows (GraphPad Software, San Diego, CA, USA).

    Journal: Cancers

    Article Title: Mitochondrial Kv1.3 Channels as Target for Treatment of Multiple Myeloma

    doi: 10.3390/cancers14081955

    Figure Lengend Snippet: Mitochondrial Kv1.3 is expressed in the multiple myeloma cell lines L-363 and RPMI-8226. PAPTP and PCARBTP efficiently kill human multiple myeloma cells. ( a ) Whole cell lysates (left, 50 µg protein/lane) were lysed in RIPA-Buffer, mitochondria from L-363, RPMI-8226 and Jurkat cells (right, 30 µg protein/lane) were enriched as described; both were supplemented with 5× reducing SDS sample buffer, boiled and separated on 8.5% SDS-polyacrylamide gels and blotted on nitrocellulose membranes. Membranes were divided and, after blocking, membranes were incubated 1 h with anti-Kv1.3 or anti-Tim23 primary antibodies, respectively. After extensively washing, blots were incubated with secondary antibodies for 1 h, washed and developed with the Roti–Lumin system. Multiple myeloma cell lines RPMI-8226 and L-363 were treated with increasing concentrations PAPTP ( b ) or PCARBTP ( c ), solvent control (0.1% DMSO), 2 µM staurosporine as a positive control and 2 µM margatoxin as a membrane-impermeable Kv1.3 blocker. After 24 h, cells were stained with Annexin V-APC/7AAD and examined for cell death by flow cytometry. Results are reported as percentages with respect to untreated samples ± SD, ( n = 3 independent experiments, each experiment in triplicate). Graph insert EC50: EC50 values of the indicated compounds in RPMI-8226 and L-363 were calculated by using GraphPad Prism version 9.3 for Windows (GraphPad Software, San Diego, CA, USA).

    Article Snippet: Membranes were blocked with 4% BSA/PBS for 1 h and incubated with anti-Kv1.3-antibody (Alomone Labs, Jerusalem, Israel, #APC-101) and anti-Tim23-antibody (BD, Franklin Lakes, NJ, USA, #611223).

    Techniques: Blocking Assay, Incubation, Positive Control, Staining, Flow Cytometry, Software

    MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: MSU effects on protein expression of K + channels and Hsp70, degradation of Kv1.5 proteins and Kv1.5 channel currents in J774.1 cells. a IB analysis of Kv1.5 and Kv1.3 proteins and Hsp70 in the cytosolic and membrane fraction of LPS-primed and MSU-stimulated cells and untreated cells. Na + /K + ATPase and β-actin were used as the plasma membrane and protein loading control, respectively. b Degradation of Kv1.5 proteins. The LPS-primed MSU-treated cells (LPS + MSU) or untreated cells (none) were chased for the indicated times after an addition of cycloheximide. Representative blots are shown. The densities of Kv1.5 was normalized to the density at time 0 and β-actin. Bar graph shows the half-life of the Kv1.5 proteins (n = 4). * p

    Article Snippet: The antibodies used were as follows: NLRP3 (Cell Signaling, Cat# 15101), ASC (AdipoGen, Cat# AG-25B-0006) and caspase-1 (AdipoGen, Cat# AG-20B-0042, AG-20B-0048), IL-1β (R & D systems, Cat# AF-401-NA), Kv1.5 and Kv1.3 (alomone Labs, Cat# APC-004, APC-002), Na+ /K+ ATPase α-1 (upstate, Cat# 05-369), Hsp70 (Stressgen, Cat# SPA-810), and β-actin (Calbiochem, Cat# CP01).

    Techniques: Expressing

    Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Journal: Molecular Biology Reports

    Article Title: Kv1.5 channel mediates monosodium urate-induced activation of NLRP3 inflammasome in macrophages and arrhythmogenic effects of urate on cardiomyocytes

    doi: 10.1007/s11033-022-07378-1

    Figure Lengend Snippet: Effects of Kv1.5 on intracellular K + concentration, ASC oligomerization and speck formation in J774.1 cells. Intracellular K + concentrations of LPS-primed cells stimulated with MSU in either the presence or absence of DPO-1 (1 μM) or the selective Kv1.3 channel blocker PAP-1 (50 nM) ( a ), and those with the introduction of a siRNA against Kv1.5 or Kv1.3 or a scramble siRNA 24 h before the LPS and MSU treatments ( b ) (n = 5–11). * p

    Article Snippet: The antibodies used were as follows: NLRP3 (Cell Signaling, Cat# 15101), ASC (AdipoGen, Cat# AG-25B-0006) and caspase-1 (AdipoGen, Cat# AG-20B-0042, AG-20B-0048), IL-1β (R & D systems, Cat# AF-401-NA), Kv1.5 and Kv1.3 (alomone Labs, Cat# APC-004, APC-002), Na+ /K+ ATPase α-1 (upstate, Cat# 05-369), Hsp70 (Stressgen, Cat# SPA-810), and β-actin (Calbiochem, Cat# CP01).

    Techniques: Concentration Assay

    Mobility of wild type and mutant Kv1.3 channels on Jurkat T cells forming immunological synapses with Raji B cells at resting membrane potential and upon depolarization. ( A ) Slow diffusion coefficients of the WT and NON-CON channels decreased significantly inside the IS. However, that of the C-terminally truncated (ΔC) mutant did not change significantly. We also studied the effect of a depolarizing milieu. The mobility of WT and ΔC channels decreased significantly upon depolarization by high-K + solution both inside and outside the IS. In contrast, the mobility of the NON-CON channels did not show significant alterations. ( B ) Average proportion of the slow diffusing component ( r slow ) was not significantly affected by being partitioned in the IS, by mutation, or by depolarization. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells

    doi: 10.3390/ijms23063313

    Figure Lengend Snippet: Mobility of wild type and mutant Kv1.3 channels on Jurkat T cells forming immunological synapses with Raji B cells at resting membrane potential and upon depolarization. ( A ) Slow diffusion coefficients of the WT and NON-CON channels decreased significantly inside the IS. However, that of the C-terminally truncated (ΔC) mutant did not change significantly. We also studied the effect of a depolarizing milieu. The mobility of WT and ΔC channels decreased significantly upon depolarization by high-K + solution both inside and outside the IS. In contrast, the mobility of the NON-CON channels did not show significant alterations. ( B ) Average proportion of the slow diffusing component ( r slow ) was not significantly affected by being partitioned in the IS, by mutation, or by depolarization. * p

    Article Snippet: We depolarized cells either with a K-HBSS buffer, referred to as “high-K+ solution”, in which all Na+ ions were replaced by K+ (total [K+ ] = 150 mM; composition in mM: 1 CaCl2 ; 142.26 KCl; 0.44 KH2 PO4 ; 0.75 MgSO4 ; 0.33 K2 HPO4; 5.55 glucose; 10 HEPES; pH 7.4 adjusted with KOH), or by the Kv1.3 channel blocker margatoxin (MgTx, 1.5 nM, Alomone Labs, Jerusalem, Israel).

    Techniques: Mutagenesis, Diffusion-based Assay

    Mobility of IL-2 receptor α subunits labeled with Alexa 546-anti-Tac Fab on IS-forming Jurkat cells expressing WT mGFP-Kv1.3. IL-2Rα diffuses significantly more slowly in the IS than outside it, which may be the consequence of a more crowded environment. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells

    doi: 10.3390/ijms23063313

    Figure Lengend Snippet: Mobility of IL-2 receptor α subunits labeled with Alexa 546-anti-Tac Fab on IS-forming Jurkat cells expressing WT mGFP-Kv1.3. IL-2Rα diffuses significantly more slowly in the IS than outside it, which may be the consequence of a more crowded environment. * p

    Article Snippet: We depolarized cells either with a K-HBSS buffer, referred to as “high-K+ solution”, in which all Na+ ions were replaced by K+ (total [K+ ] = 150 mM; composition in mM: 1 CaCl2 ; 142.26 KCl; 0.44 KH2 PO4 ; 0.75 MgSO4 ; 0.33 K2 HPO4; 5.55 glucose; 10 HEPES; pH 7.4 adjusted with KOH), or by the Kv1.3 channel blocker margatoxin (MgTx, 1.5 nM, Alomone Labs, Jerusalem, Israel).

    Techniques: Labeling, Expressing

    Distribution of Kv1.3 WT and F-actin in standalone and IS-engaged Jurkat cells. Kv1.3 was tagged with mGFP and F-actin was labeled with Alexa546-phalloidin. 3D reconstructions from z-stacks of confocal images are shown. ( A ) Standalone cells, ( B ) Jurkat cell in IS with Raji cell. The arrow marks the IS and the F-actin ring formed at its periphery.

    Journal: International Journal of Molecular Sciences

    Article Title: Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells

    doi: 10.3390/ijms23063313

    Figure Lengend Snippet: Distribution of Kv1.3 WT and F-actin in standalone and IS-engaged Jurkat cells. Kv1.3 was tagged with mGFP and F-actin was labeled with Alexa546-phalloidin. 3D reconstructions from z-stacks of confocal images are shown. ( A ) Standalone cells, ( B ) Jurkat cell in IS with Raji cell. The arrow marks the IS and the F-actin ring formed at its periphery.

    Article Snippet: We depolarized cells either with a K-HBSS buffer, referred to as “high-K+ solution”, in which all Na+ ions were replaced by K+ (total [K+ ] = 150 mM; composition in mM: 1 CaCl2 ; 142.26 KCl; 0.44 KH2 PO4 ; 0.75 MgSO4 ; 0.33 K2 HPO4; 5.55 glucose; 10 HEPES; pH 7.4 adjusted with KOH), or by the Kv1.3 channel blocker margatoxin (MgTx, 1.5 nM, Alomone Labs, Jerusalem, Israel).

    Techniques: Labeling

    Diffusion properties of WT and mutant Kv1.3 channels in standalone cells. ( A ) Diffusion coefficient of the slow component. The mobility of the wild type mGFP-tagged Kv1.3 channel (WT) was compared to that of non-conducting point mutant (NON-CON) and C-terminal deleted mutant (ΔC) Kv1.3 channels (empty boxes) expressed in Jurkat cells. The NON-CON mutant channel has the lowest mobility, and the ΔC mutant has the highest mobility. Depolarization by high external K + concentration using high K + solution decreased the mobility of the WT and ΔC channels significantly (filled boxes). ( B ) Average proportions ( r slow ) of the slow component of the different Kv1.3 channels did not differ significantly. ( C ) Membrane potential of Jurkat cells expressing WT mGFP-Kv1.3 and the NON-CON mutant measured by patch clamp. On the box-and-whiskers plots, boxes represent the values of the 25th to 75th percentiles, whereas whiskers represent the 10th and 90th percentiles, the midline is the median value, and “+” marks the arithmetic mean. Mean values were compared with ANOVA and Student’s t -test. ** p

    Journal: International Journal of Molecular Sciences

    Article Title: Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells

    doi: 10.3390/ijms23063313

    Figure Lengend Snippet: Diffusion properties of WT and mutant Kv1.3 channels in standalone cells. ( A ) Diffusion coefficient of the slow component. The mobility of the wild type mGFP-tagged Kv1.3 channel (WT) was compared to that of non-conducting point mutant (NON-CON) and C-terminal deleted mutant (ΔC) Kv1.3 channels (empty boxes) expressed in Jurkat cells. The NON-CON mutant channel has the lowest mobility, and the ΔC mutant has the highest mobility. Depolarization by high external K + concentration using high K + solution decreased the mobility of the WT and ΔC channels significantly (filled boxes). ( B ) Average proportions ( r slow ) of the slow component of the different Kv1.3 channels did not differ significantly. ( C ) Membrane potential of Jurkat cells expressing WT mGFP-Kv1.3 and the NON-CON mutant measured by patch clamp. On the box-and-whiskers plots, boxes represent the values of the 25th to 75th percentiles, whereas whiskers represent the 10th and 90th percentiles, the midline is the median value, and “+” marks the arithmetic mean. Mean values were compared with ANOVA and Student’s t -test. ** p

    Article Snippet: We depolarized cells either with a K-HBSS buffer, referred to as “high-K+ solution”, in which all Na+ ions were replaced by K+ (total [K+ ] = 150 mM; composition in mM: 1 CaCl2 ; 142.26 KCl; 0.44 KH2 PO4 ; 0.75 MgSO4 ; 0.33 K2 HPO4; 5.55 glucose; 10 HEPES; pH 7.4 adjusted with KOH), or by the Kv1.3 channel blocker margatoxin (MgTx, 1.5 nM, Alomone Labs, Jerusalem, Israel).

    Techniques: Diffusion-based Assay, Mutagenesis, Concentration Assay, Expressing, Patch Clamp

    Transmission and fluorescence microscopic images of immunological synapses formed between a Raji B and Jurkat T cells expressing different mGFP-Kv1.3 variants. The red marks illustrate points inside and outside the IS where FCS measurements were typically carried out. Different versions of Kv1.3 are displayed: WT ( A ), NON-CON ( B ), and ΔC mutant ( C ). Panel ( D ) shows the extent of Kv1.3 enrichment at the IS according to Equation (3). The ratio of the average pixel intensity inside the IS and in the whole cell membrane was calculated from confocal images by using MATLAB (for details see Materials and Methods). * p

    Journal: International Journal of Molecular Sciences

    Article Title: Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells

    doi: 10.3390/ijms23063313

    Figure Lengend Snippet: Transmission and fluorescence microscopic images of immunological synapses formed between a Raji B and Jurkat T cells expressing different mGFP-Kv1.3 variants. The red marks illustrate points inside and outside the IS where FCS measurements were typically carried out. Different versions of Kv1.3 are displayed: WT ( A ), NON-CON ( B ), and ΔC mutant ( C ). Panel ( D ) shows the extent of Kv1.3 enrichment at the IS according to Equation (3). The ratio of the average pixel intensity inside the IS and in the whole cell membrane was calculated from confocal images by using MATLAB (for details see Materials and Methods). * p

    Article Snippet: We depolarized cells either with a K-HBSS buffer, referred to as “high-K+ solution”, in which all Na+ ions were replaced by K+ (total [K+ ] = 150 mM; composition in mM: 1 CaCl2 ; 142.26 KCl; 0.44 KH2 PO4 ; 0.75 MgSO4 ; 0.33 K2 HPO4; 5.55 glucose; 10 HEPES; pH 7.4 adjusted with KOH), or by the Kv1.3 channel blocker margatoxin (MgTx, 1.5 nM, Alomone Labs, Jerusalem, Israel).

    Techniques: Transmission Assay, Fluorescence, Expressing, Mutagenesis

    Mobility of MHC I heavy chain. Mobility of the MHC I glycoprotein was measured in standard solution in standalone Jurkat cells expressing WT, non-conductive point mutant (NON-CON), or C-terminal deleted mutant (ΔC) Kv1.3 channels. MHC I was labeled with Alexa546-W6/32 Fab. * p

    Journal: International Journal of Molecular Sciences

    Article Title: Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells

    doi: 10.3390/ijms23063313

    Figure Lengend Snippet: Mobility of MHC I heavy chain. Mobility of the MHC I glycoprotein was measured in standard solution in standalone Jurkat cells expressing WT, non-conductive point mutant (NON-CON), or C-terminal deleted mutant (ΔC) Kv1.3 channels. MHC I was labeled with Alexa546-W6/32 Fab. * p

    Article Snippet: We depolarized cells either with a K-HBSS buffer, referred to as “high-K+ solution”, in which all Na+ ions were replaced by K+ (total [K+ ] = 150 mM; composition in mM: 1 CaCl2 ; 142.26 KCl; 0.44 KH2 PO4 ; 0.75 MgSO4 ; 0.33 K2 HPO4; 5.55 glucose; 10 HEPES; pH 7.4 adjusted with KOH), or by the Kv1.3 channel blocker margatoxin (MgTx, 1.5 nM, Alomone Labs, Jerusalem, Israel).

    Techniques: Expressing, Mutagenesis, Labeling