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kv3 4  (Alomone Labs)


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    Structured Review

    Alomone Labs kv3 4
    Kv3 4, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/kv3+4/Anti-KV1%2E4+Antibody/bio_rxiv__2025__10__22__683960-291-23-25
    Average 93 stars, based on 38 article reviews
    kv3 4 - by Bioz Stars, 2026-09
    93/100 stars

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    Related Articles

    other:

    Article Title: FUNCTIONAL EXPRESSION PROFILE OF VOLTAGE GATED K + CHANNEL SUBUNITS IN RAT SMALL MESENTERIC ARTERIES
    Article Snippet: Anti-Kv1.2, Kv7.4, Kvβ1.1 and Kvβ1.2 were obtained from Antibodies, Inc. (Davis, CA); anti-Kv1.5 and anti-actin from Sigma Chemical Co. (St. Louis, MO); anti-Kv2.1 from Upstate Biotechnology (Lake Placid, NY); anti-Kv3.4 and anti-Kv4.1 from Alomone Labs (Jerusalen, Isreal); anti-Kv4.3 from Millipore (Temecula,CA); anti-Kv6.1 from Abcam Inc., (Cambridge, MA); and anti-Kv9.3 from Santa Cruz Biotech (Santa Cruz, CA).

    Membrane:

    Article Title: Neural Inflammation in Thoracic Dorsal Root Ganglia Mediates Cardiopulmonary Spinal Afferent Sensitization in Chronic Heart Failure
    Article Snippet: The proteins were loaded onto a 10% SDS-PAGE gel along with protein standards (Bio-Rad Laboratories, Berkeley, California, USA) in a separate lane for electrophoresis and then transferred to polyvinylidene fluoride membrane. .. The membrane was probed with mouse antibody against IRF8 (1:500, Santa Cruz Biotechnology, Dallas, USA) and rabbit antibodies against Kv1.4, Kv4.2, Kv4.3, and Kv3.4 (1:200, Alomone labs, Jerusalem, Israel) and secondary antibody of goat anti-mouse (1:5000, Invitrogen, Carlsbad, CA, USA), goat anti-rabbit IgG (1:5000, Invitrogen). .. The protein signals were detected by enhanced chemiluminescence reagent (Thermo Scientific) and analyzed using UVP BioImaging Systems.

    Blocking Assay:

    Article Title: Kv3.1 and Kv3.4, Are Involved in Cancer Cell Migration and Invasion
    Article Snippet: The quantified protein was loaded on a 10% acrylamide gel for sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred to a nitrocellulose membrane (Whatman, Maidstone, Kent, UK). .. Then, 1× TBS-Tween 20 containing 5% nonfat milk (Difco, Franklin Lakes, NJ, USA) was used to block non-specific antibody binding, and protein-transferred membranes were probed overnight with commercially purchased primary antibodies targeting the proteins HIF-1α, Kv3.1, Kv3.3 (Abcam, Cambridge, MA, USA), Kv3.4 (Alomone labs, Jerusalem, Israel), tERK, pERK (Cell Signaling Technology, Inc., Danvers, MA, USA), β-actin, or vinculin (Santa Cruz Biotechnology, Finnell St., Dallas, TX, USA). .. Membranes probed with primary antibodies were incubated with horseradish peroxidase–conjugated goat, anti-rabbit or anti-mouse secondary antibody (GenDEPOT, Barker, TX, USA) for 1 h and visualized using a WesternBrightTM QuantumTM (Advansta, Menlo Park, CA, USA).

    Article Title: Neural Inflammation in Thoracic Dorsal Root Ganglia Mediates Cardiopulmonary Spinal Afferent Sensitization in Chronic Heart Failure
    Article Snippet: For triple-immunostaining of potassium channels, sections were stained with the isolectin B4 (a C-fiber neuronal marker, Invitrogen, I21411) and NF200 (an A-fiber neuronal marker, Sigma- Aldrich, N5389). .. After washing with PBS, sections were incubated in blocking serum (10% donkey serum in PBS) for 1 h and further incubated overnight with rabbit antibodies of Kv1.4, Kv4.2, Kv4.3, and Kv3.4 (1:100, Alomone labs) and mouse anti-NF200 antibody (1:200, Sigma- Aldrich, N5389) overnight at 4°C. .. After being washed in PBS, the sections were treated with PBS and sections were incubated with fluorescence-conjugated secondary antibody (Alexa 568- conjugated goat anti-rabbit IgG and pacific blue-conjugated goat anti-mouse IgG, 1:200, Invitrogen) and Alexa FluorR 488 conjugated isolectin-B4 (1:200, Invitrogen) for 60 min at room temperature.

    Article Title: Pharmacological inhibition of Kv3 on oxidative stress-induced cataract progression.
    Article Snippet: Oxidative stress is one of the most important risk factors for cataractogenesis.. Previous studies have indicated that BDS-II, a Kv3 channel blocker, plays pivotal roles in oxidative stress-related diseases.. This study demonstrates that BDS-II exerts a protective effect on cataractogenesis.

    Article Title: Kv3 channels contribute to cancer cell migration via vimentin regulation.
    Article Snippet: Cell migration is a complex and important process in cancer progression.. Vimentin has pivotal roles in cancer cell migration, and various signaling pathways including the AKT pathway are involved in cancer cell migration via vimentin regulation.. Recent studies have revealed that voltage-gated potassium (Kv) channels have important functions in cancer cell migration; however, the exact mechanism is still unclear.

    Binding Assay:

    Article Title: Kv3.1 and Kv3.4, Are Involved in Cancer Cell Migration and Invasion
    Article Snippet: The quantified protein was loaded on a 10% acrylamide gel for sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred to a nitrocellulose membrane (Whatman, Maidstone, Kent, UK). .. Then, 1× TBS-Tween 20 containing 5% nonfat milk (Difco, Franklin Lakes, NJ, USA) was used to block non-specific antibody binding, and protein-transferred membranes were probed overnight with commercially purchased primary antibodies targeting the proteins HIF-1α, Kv3.1, Kv3.3 (Abcam, Cambridge, MA, USA), Kv3.4 (Alomone labs, Jerusalem, Israel), tERK, pERK (Cell Signaling Technology, Inc., Danvers, MA, USA), β-actin, or vinculin (Santa Cruz Biotechnology, Finnell St., Dallas, TX, USA). .. Membranes probed with primary antibodies were incubated with horseradish peroxidase–conjugated goat, anti-rabbit or anti-mouse secondary antibody (GenDEPOT, Barker, TX, USA) for 1 h and visualized using a WesternBrightTM QuantumTM (Advansta, Menlo Park, CA, USA).

    Article Title: Pharmacological inhibition of Kv3 on oxidative stress-induced cataract progression.
    Article Snippet: Oxidative stress is one of the most important risk factors for cataractogenesis.. Previous studies have indicated that BDS-II, a Kv3 channel blocker, plays pivotal roles in oxidative stress-related diseases.. This study demonstrates that BDS-II exerts a protective effect on cataractogenesis.

    Article Title: Kv3 channels contribute to cancer cell migration via vimentin regulation.
    Article Snippet: Cell migration is a complex and important process in cancer progression.. Vimentin has pivotal roles in cancer cell migration, and various signaling pathways including the AKT pathway are involved in cancer cell migration via vimentin regulation.. Recent studies have revealed that voltage-gated potassium (Kv) channels have important functions in cancer cell migration; however, the exact mechanism is still unclear.

    Expressing:

    Article Title: Reducing voltage-dependent potassium channel Kv3.4 levels ameliorates synapse loss in a mouse model of Alzheimer's disease.
    Article Snippet: .. For measurement of Kv3.4 expression within injection sites, 50 μm floating slices were stained with an antibody specific to Kv3.4 (Alomone Labs, APC-019) and an anti-rabbit Alexa Fluor Plus 647-conjugated secondary antibody (Invitrogen, Wlatham MA USA, A32795). ..

    Article Title: Reducing voltage-dependent potassium channel Kv3.4 levels ameliorates synapse loss in a mouse model of Alzheimer’s disease
    Article Snippet: .. For measurement of Kv3.4 expression within injection sites, 50 μm floating slices were stained with an antibody specific to Kv3.4 (Alomone Labs, APC-019) and an anti-rabbit Alexa Fluor Plus 647-conjugated secondary antibody (Invitrogen, Wlatham MA USA, A32795). ..

    Injection:

    Article Title: Reducing voltage-dependent potassium channel Kv3.4 levels ameliorates synapse loss in a mouse model of Alzheimer's disease.
    Article Snippet: .. For measurement of Kv3.4 expression within injection sites, 50 μm floating slices were stained with an antibody specific to Kv3.4 (Alomone Labs, APC-019) and an anti-rabbit Alexa Fluor Plus 647-conjugated secondary antibody (Invitrogen, Wlatham MA USA, A32795). ..

    Article Title: Reducing voltage-dependent potassium channel Kv3.4 levels ameliorates synapse loss in a mouse model of Alzheimer’s disease
    Article Snippet: .. For measurement of Kv3.4 expression within injection sites, 50 μm floating slices were stained with an antibody specific to Kv3.4 (Alomone Labs, APC-019) and an anti-rabbit Alexa Fluor Plus 647-conjugated secondary antibody (Invitrogen, Wlatham MA USA, A32795). ..

    Staining:

    Article Title: Reducing voltage-dependent potassium channel Kv3.4 levels ameliorates synapse loss in a mouse model of Alzheimer's disease.
    Article Snippet: .. For measurement of Kv3.4 expression within injection sites, 50 μm floating slices were stained with an antibody specific to Kv3.4 (Alomone Labs, APC-019) and an anti-rabbit Alexa Fluor Plus 647-conjugated secondary antibody (Invitrogen, Wlatham MA USA, A32795). ..

    Article Title: Reducing voltage-dependent potassium channel Kv3.4 levels ameliorates synapse loss in a mouse model of Alzheimer’s disease
    Article Snippet: .. For measurement of Kv3.4 expression within injection sites, 50 μm floating slices were stained with an antibody specific to Kv3.4 (Alomone Labs, APC-019) and an anti-rabbit Alexa Fluor Plus 647-conjugated secondary antibody (Invitrogen, Wlatham MA USA, A32795). ..

    Incubation:

    Article Title: Neural Inflammation in Thoracic Dorsal Root Ganglia Mediates Cardiopulmonary Spinal Afferent Sensitization in Chronic Heart Failure
    Article Snippet: For triple-immunostaining of potassium channels, sections were stained with the isolectin B4 (a C-fiber neuronal marker, Invitrogen, I21411) and NF200 (an A-fiber neuronal marker, Sigma- Aldrich, N5389). .. After washing with PBS, sections were incubated in blocking serum (10% donkey serum in PBS) for 1 h and further incubated overnight with rabbit antibodies of Kv1.4, Kv4.2, Kv4.3, and Kv3.4 (1:100, Alomone labs) and mouse anti-NF200 antibody (1:200, Sigma- Aldrich, N5389) overnight at 4°C. .. After being washed in PBS, the sections were treated with PBS and sections were incubated with fluorescence-conjugated secondary antibody (Alexa 568- conjugated goat anti-rabbit IgG and pacific blue-conjugated goat anti-mouse IgG, 1:200, Invitrogen) and Alexa FluorR 488 conjugated isolectin-B4 (1:200, Invitrogen) for 60 min at room temperature.

    Migration:

    Article Title: Kv3 channels contribute to cancer cell migration via vimentin regulation.
    Article Snippet: Cell migration is a complex and important process in cancer progression.. Vimentin has pivotal roles in cancer cell migration, and various signaling pathways including the AKT pathway are involved in cancer cell migration via vimentin regulation.. Recent studies have revealed that voltage-gated potassium (Kv) channels have important functions in cancer cell migration; however, the exact mechanism is still unclear.

    Western Blot:

    Article Title: Kv3 channels contribute to cancer cell migration via vimentin regulation.
    Article Snippet: Cell migration is a complex and important process in cancer progression.. Vimentin has pivotal roles in cancer cell migration, and various signaling pathways including the AKT pathway are involved in cancer cell migration via vimentin regulation.. Recent studies have revealed that voltage-gated potassium (Kv) channels have important functions in cancer cell migration; however, the exact mechanism is still unclear.



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    Western blots of wild type (Wt), N220Q, N229Q, and N220Q/N229Q <t>Kv3.1</t> proteins. Kv3.1 proteins were detected when heterologously expressed in B35 cells (A). Arrows and lines denote the type of N -glycan attached to the Kv3.1 protein. Assignments of the various glycosylated and unglycosylated Kv3.1 proteins were based on immunoband shifts produced by glycosidase treatment. N220Q and N229Q proteins were digested (+) and undigested (−) with neuraminidase (B), PNGase F (C) and Endo H (D). A solid line on image indicates that samples were run on a different blot (B). The numbers adjacent to the Western blots represent the Kaleidoscope markers (in KDa). Similar migration patterns were observed on at least three separate Western blots.
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    Image Search Results


    Antibody information.

    Journal: Scientific Reports

    Article Title: Kv3.4 regulates cell migration and invasion through TGF-β-induced epithelial–mesenchymal transition in A549 cells

    doi: 10.1038/s41598-024-52739-4

    Figure Lengend Snippet: Antibody information.

    Article Snippet: Kv3.4 , Alomone Labs , APC-019 , 1:500.

    Techniques:

    Activation of TAAR1 decreases I A by targeting Kv1.4 channels. a The expression of Kv1.4, Kv3.4, Kv4.1, Kv4.2 and Kv4.3 transcripts in mouse TGs. Samples without reverse transcriptase (-RT) were used as negative controls. b through d The time course curves of I A changes induced by 0.1 µM tyramine in the presence of AmmTX3 (2 µM, n = 11 cells, b ), CP339818 (1 µM, n = 9 cells, c ) or UK78282 (1 µM, n = 10 cells, d ). Inset s in each panel indicate the representative traces. The letters indicate the points used for sample traces. e Summary data indicating the effect of tyramine on I A in the presence of AmmTX3, CP339818 or UK78282. ** p < 0.01 vs. control, paired t test. f Western blot analysis demonstrating the protein abundance of Kv1.4, Kv3.4 or Kv4.3 in the control siRNA (NC-siRNA) and Kv1.4-siRNA-treated (Kv1.4-siRNA) groups. β-actin served as a loading control. The immunoblots are representative of the results of at least three independent experiments. ** p < 0.01 vs. NC-siRNA, unpaired t test. g Representative traces ( left panel ) and bar graph ( right panel ) demonstrating that Kv1.4-siRNA treatment abrogated the tyramine-mediated I A reduction ( n = 14 cells). Tyramine at 0.1 µM significantly decreased I A in cells transduced with NC-siRNA ( n = 15 cells). * p < 0.05 vs. control + NC-siRNA, unpaired t test

    Journal: The Journal of Headache and Pain

    Article Title: Trace amine-associated receptor 1 regulation of Kv1.4 channels in trigeminal ganglion neurons contributes to nociceptive behaviors

    doi: 10.1186/s10194-023-01582-5

    Figure Lengend Snippet: Activation of TAAR1 decreases I A by targeting Kv1.4 channels. a The expression of Kv1.4, Kv3.4, Kv4.1, Kv4.2 and Kv4.3 transcripts in mouse TGs. Samples without reverse transcriptase (-RT) were used as negative controls. b through d The time course curves of I A changes induced by 0.1 µM tyramine in the presence of AmmTX3 (2 µM, n = 11 cells, b ), CP339818 (1 µM, n = 9 cells, c ) or UK78282 (1 µM, n = 10 cells, d ). Inset s in each panel indicate the representative traces. The letters indicate the points used for sample traces. e Summary data indicating the effect of tyramine on I A in the presence of AmmTX3, CP339818 or UK78282. ** p < 0.01 vs. control, paired t test. f Western blot analysis demonstrating the protein abundance of Kv1.4, Kv3.4 or Kv4.3 in the control siRNA (NC-siRNA) and Kv1.4-siRNA-treated (Kv1.4-siRNA) groups. β-actin served as a loading control. The immunoblots are representative of the results of at least three independent experiments. ** p < 0.01 vs. NC-siRNA, unpaired t test. g Representative traces ( left panel ) and bar graph ( right panel ) demonstrating that Kv1.4-siRNA treatment abrogated the tyramine-mediated I A reduction ( n = 14 cells). Tyramine at 0.1 µM significantly decreased I A in cells transduced with NC-siRNA ( n = 15 cells). * p < 0.05 vs. control + NC-siRNA, unpaired t test

    Article Snippet: Blotted proteins were probed with the following primary antibodies: anti-TAAR1 (rabbit, 1:1000, Thermo Fisher Scientific, catalog no. PA5-95704), anti-TAAR4 (rabbit, 1:1000, Novus Biologicals, catalog no. NBP3-10140), anti-Gαo (rabbit, 1:1000, Cell Signaling Technology, catalog no. #3975S), anti-Gαi (rabbit, 1:600, Cell Signaling Technology, catalog no. #5290S), anti-PKC θ (rabbit, 1:500, Cell Signaling Technology, catalog no. #13,643), anti-Kv1.4 (rabbit, 1:800, Thermo Fisher Scientific, catalog no. PA5-85937), anti-Kv4.3 (rabbit, 1:600, Thermo Fisher Scientific, catalog no. PA5-95211) and anti-Kv3.4 (rabbit, 1:500, Thermo Fisher Scientific, catalog no. PA5-106236).

    Techniques: Activation Assay, Expressing, Western Blot, Transduction

    Western blots of wild type (Wt), N220Q, N229Q, and N220Q/N229Q Kv3.1 proteins. Kv3.1 proteins were detected when heterologously expressed in B35 cells (A). Arrows and lines denote the type of N -glycan attached to the Kv3.1 protein. Assignments of the various glycosylated and unglycosylated Kv3.1 proteins were based on immunoband shifts produced by glycosidase treatment. N220Q and N229Q proteins were digested (+) and undigested (−) with neuraminidase (B), PNGase F (C) and Endo H (D). A solid line on image indicates that samples were run on a different blot (B). The numbers adjacent to the Western blots represent the Kaleidoscope markers (in KDa). Similar migration patterns were observed on at least three separate Western blots.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: Western blots of wild type (Wt), N220Q, N229Q, and N220Q/N229Q Kv3.1 proteins. Kv3.1 proteins were detected when heterologously expressed in B35 cells (A). Arrows and lines denote the type of N -glycan attached to the Kv3.1 protein. Assignments of the various glycosylated and unglycosylated Kv3.1 proteins were based on immunoband shifts produced by glycosidase treatment. N220Q and N229Q proteins were digested (+) and undigested (−) with neuraminidase (B), PNGase F (C) and Endo H (D). A solid line on image indicates that samples were run on a different blot (B). The numbers adjacent to the Western blots represent the Kaleidoscope markers (in KDa). Similar migration patterns were observed on at least three separate Western blots.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques: Western Blot, Produced, Migration

    Whole cell currents for glycosylated (A, middle panel; B, top panel) and unglycosylated (A and B, bottom panels) Kv3.1 proteins were elicited from the indicated voltage protocol (A, top panel). Whole cell currents were scaled for inactivating (A) and non-inactivating (B) current types from B35 cells expressing glycosylated and unglycosylated Kv3.1 proteins. Right panels show traces at expanded time scales and grey lines denote currents at +40 and +60 mV. Traces were scaled to show differences in activation kinetics. Conductance-voltage (g/gmax) curves of both inactivating (C) and non-inactivating (D) current types for glycosylated and unglycosylated Kv3.1 channels. Rise times of inactivating (E) and non-inactivating (F) currents types. n represents number of cells.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: Whole cell currents for glycosylated (A, middle panel; B, top panel) and unglycosylated (A and B, bottom panels) Kv3.1 proteins were elicited from the indicated voltage protocol (A, top panel). Whole cell currents were scaled for inactivating (A) and non-inactivating (B) current types from B35 cells expressing glycosylated and unglycosylated Kv3.1 proteins. Right panels show traces at expanded time scales and grey lines denote currents at +40 and +60 mV. Traces were scaled to show differences in activation kinetics. Conductance-voltage (g/gmax) curves of both inactivating (C) and non-inactivating (D) current types for glycosylated and unglycosylated Kv3.1 channels. Rise times of inactivating (E) and non-inactivating (F) currents types. n represents number of cells.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques: Expressing, Activation Assay

    Electrophysiological parameters of glycosylated, unglycosylated, and partially glycosylated forms of the  Kv3.1  channel in B35 cells.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: Electrophysiological parameters of glycosylated, unglycosylated, and partially glycosylated forms of the Kv3.1 channel in B35 cells.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques:

    A deactivation voltage protocol (A, left panel) was utilized to obtain deactivation currents for B35 cells expressing the glycosylated (A, right panel) and unglycosylated. Scaled deactivation currents from transfected B35 cells expressing either inactivating (B) or non-inactivating (D) current types. Grey lines denote currents at −30 and −50 mV. Traces were scaled to show differences in deactivation kinetics. Deactivation time constant vs. voltage plot of B35 cells expressing glycosylated and unglycosylated Kv3.1 channels for inactivating (C) and non-inactivating (E) currents types.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: A deactivation voltage protocol (A, left panel) was utilized to obtain deactivation currents for B35 cells expressing the glycosylated (A, right panel) and unglycosylated. Scaled deactivation currents from transfected B35 cells expressing either inactivating (B) or non-inactivating (D) current types. Grey lines denote currents at −30 and −50 mV. Traces were scaled to show differences in deactivation kinetics. Deactivation time constant vs. voltage plot of B35 cells expressing glycosylated and unglycosylated Kv3.1 channels for inactivating (C) and non-inactivating (E) currents types.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques: Expressing, Transfection

    Whole cell currents were elicited from the shown voltage protocol (A, left panel) for B35 cells expressing glycosylated (A, right panel) and unglycosylated (B) Kv3.1 proteins. Traces were scaled to show differences in inactivation kinetics. Grey lines denote currents at +40 mV.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: Whole cell currents were elicited from the shown voltage protocol (A, left panel) for B35 cells expressing glycosylated (A, right panel) and unglycosylated (B) Kv3.1 proteins. Traces were scaled to show differences in inactivation kinetics. Grey lines denote currents at +40 mV.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques: Expressing

    Currents were elicited by a train of five depolarizing voltage steps to +40 mV once every 525 ms, from a holding potential of −50 mV (A, top panel) for B35 cells expressing glycosylated (A, bottom-left panel) and unglycosylated (A, bottom-right panel) Kv3.1 channels. A bar graph representing the percent of peak current amplitude remaining after the fifth pulse relative to peak current amplitude of initial pulse for the various Kv3.1 channels (B). Asterisks indicate significant differences in mean values at a probability of P <0.01 from that of glycosylated Kv3.1.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: Currents were elicited by a train of five depolarizing voltage steps to +40 mV once every 525 ms, from a holding potential of −50 mV (A, top panel) for B35 cells expressing glycosylated (A, bottom-left panel) and unglycosylated (A, bottom-right panel) Kv3.1 channels. A bar graph representing the percent of peak current amplitude remaining after the fifth pulse relative to peak current amplitude of initial pulse for the various Kv3.1 channels (B). Asterisks indicate significant differences in mean values at a probability of P <0.01 from that of glycosylated Kv3.1.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques: Expressing

    Wound width was determined and then normalized at 0, 6, 11 and 23 h for glycosylated and unglycosylated Kv3.1 transfected and non-transfected B35 cells (A). Similar experiments were also performed for glycosylated, and partially glycosylated Kv3.1 glycoproteins (N220Q, and N229Q) transfected B35 cells (B). Data were expressed as the mean +/− SEM. Asterisks indicate significant differences in mean values at a probability of P <0.01 from that of glycosylated Kv3.1. Images were obtained at 0 h, 6 h, 11 h and 23 h of the generated wound for group I: wild type Kv3.1 (row I), N220Q/N229Q (row II) transfected B35 cells and non-transfected B35 cells (row III); and group II: wild type Kv3.1 (row IV), N220Q (row V) and N229Q (row VI) (C). The distance between the two white dashed lines represents wound width for each image. This distance becomes smaller as time increases, representing the rate of cell migration. n represents number of cell wounds. The experiments were conducted on three separate occasions. The solid black line represents a 25 µM scale bar.

    Journal: PLoS ONE

    Article Title: Importance of Glycosylation on Function of a Potassium Channel in Neuroblastoma Cells

    doi: 10.1371/journal.pone.0019317

    Figure Lengend Snippet: Wound width was determined and then normalized at 0, 6, 11 and 23 h for glycosylated and unglycosylated Kv3.1 transfected and non-transfected B35 cells (A). Similar experiments were also performed for glycosylated, and partially glycosylated Kv3.1 glycoproteins (N220Q, and N229Q) transfected B35 cells (B). Data were expressed as the mean +/− SEM. Asterisks indicate significant differences in mean values at a probability of P <0.01 from that of glycosylated Kv3.1. Images were obtained at 0 h, 6 h, 11 h and 23 h of the generated wound for group I: wild type Kv3.1 (row I), N220Q/N229Q (row II) transfected B35 cells and non-transfected B35 cells (row III); and group II: wild type Kv3.1 (row IV), N220Q (row V) and N229Q (row VI) (C). The distance between the two white dashed lines represents wound width for each image. This distance becomes smaller as time increases, representing the rate of cell migration. n represents number of cell wounds. The experiments were conducted on three separate occasions. The solid black line represents a 25 µM scale bar.

    Article Snippet: Electrophoresed proteins were transferred to Immobilon-P PVDF membranes (Millipore, Billercia, MA, USA) at 175 mAmps for 90–240 min. Blots were then incubated at room temperature for 20 min in blocking buffer (PBS, 3% BSA with 0.1% Tween 20) followed by incubation for 2 h with polyclonal rabbit anti-Kv3.1, anti-Kv3.3, or anti-Kv3.4 antibodies (Alamone Labs, Jerusalem, Israel) or overnight with mouse anti-Kv3.1 antibody (NeuroMab).

    Techniques: Transfection, Generated, Migration