anti kv1 3 antisera Search Results


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  • 93
    Millipore kv1 3 antisera
    Localization of <t>Kv1.3</t> channels after sequential mutation of the acidic ER export motif. The Kv1.3-eGFP and each of the mutated Kv1.3-eGFP proteins (see methods) were transiently expressed in BSC40 cells and the fluorescence was observed using confocal microscopy ( a - h ) in the presence of the membranous ER resident protein Sec61β and the Golgi resident protein Golgin97. The Kv1.3-eGFP co-localization with these organelle specific resident proteins and the resulting fluorescent trafficking profile ( a ) is similar in appearance with the Kv1.3-eGFP E443A ( b ), Kv1.3-eGFP E445A ( c ), Kv1.3-eGFP E443A-E445A ( e ), and Kv1.3-eGFP E445A-E447A ( f ) profiles indicating that there is no significant ER retention of any of these mutated proteins. A noticeable difference in the co-localization of Kv1.3-eGFP and Sec61β is observed in the Kv1.3-eGFP E447A ( d ), Kv1.3-eGFP E443A-E445A-E447A ( g ), and Kv1.3-eGFP ∆C ( h ) trafficking profiles where there is either a modest ( d and g ) or severe ( h ) retention within the ER network ( d , g , and h ; white arrows). Line scans of each fluorescent channel are shown. The white arrow in the merged image represents the placement and direction of the line scan. Scale bar = 10 μm
    Kv1 3 Antisera, supplied by Millipore, 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/kv1 3 antisera/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kv1 3 antisera - by Bioz Stars, 2022-08
    93/100 stars
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    93
    Alomone Labs anti kv1 3 antisera
    Recognition of <t>Kv1.3</t> 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.
    Anti Kv1 3 Antisera, 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/anti kv1 3 antisera/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti kv1 3 antisera - by Bioz Stars, 2022-08
    93/100 stars
      Buy from Supplier

    Image Search Results


    Localization of Kv1.3 channels after sequential mutation of the acidic ER export motif. The Kv1.3-eGFP and each of the mutated Kv1.3-eGFP proteins (see methods) were transiently expressed in BSC40 cells and the fluorescence was observed using confocal microscopy ( a - h ) in the presence of the membranous ER resident protein Sec61β and the Golgi resident protein Golgin97. The Kv1.3-eGFP co-localization with these organelle specific resident proteins and the resulting fluorescent trafficking profile ( a ) is similar in appearance with the Kv1.3-eGFP E443A ( b ), Kv1.3-eGFP E445A ( c ), Kv1.3-eGFP E443A-E445A ( e ), and Kv1.3-eGFP E445A-E447A ( f ) profiles indicating that there is no significant ER retention of any of these mutated proteins. A noticeable difference in the co-localization of Kv1.3-eGFP and Sec61β is observed in the Kv1.3-eGFP E447A ( d ), Kv1.3-eGFP E443A-E445A-E447A ( g ), and Kv1.3-eGFP ∆C ( h ) trafficking profiles where there is either a modest ( d and g ) or severe ( h ) retention within the ER network ( d , g , and h ; white arrows). Line scans of each fluorescent channel are shown. The white arrow in the merged image represents the placement and direction of the line scan. Scale bar = 10 μm

    Journal: BMC Biochemistry

    Article Title: Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a

    doi: 10.1186/s12858-015-0045-6

    Figure Lengend Snippet: Localization of Kv1.3 channels after sequential mutation of the acidic ER export motif. The Kv1.3-eGFP and each of the mutated Kv1.3-eGFP proteins (see methods) were transiently expressed in BSC40 cells and the fluorescence was observed using confocal microscopy ( a - h ) in the presence of the membranous ER resident protein Sec61β and the Golgi resident protein Golgin97. The Kv1.3-eGFP co-localization with these organelle specific resident proteins and the resulting fluorescent trafficking profile ( a ) is similar in appearance with the Kv1.3-eGFP E443A ( b ), Kv1.3-eGFP E445A ( c ), Kv1.3-eGFP E443A-E445A ( e ), and Kv1.3-eGFP E445A-E447A ( f ) profiles indicating that there is no significant ER retention of any of these mutated proteins. A noticeable difference in the co-localization of Kv1.3-eGFP and Sec61β is observed in the Kv1.3-eGFP E447A ( d ), Kv1.3-eGFP E443A-E445A-E447A ( g ), and Kv1.3-eGFP ∆C ( h ) trafficking profiles where there is either a modest ( d and g ) or severe ( h ) retention within the ER network ( d , g , and h ; white arrows). Line scans of each fluorescent channel are shown. The white arrow in the merged image represents the placement and direction of the line scan. Scale bar = 10 μm

    Article Snippet: Blocked membranes were incubated overnight at 4 °C with Kv1.3 antisera, FSU120, generated against the intracellular C-terminal domain [ ] and an anti-actin primary antibody (Millipore).

    Techniques: Mutagenesis, Fluorescence, Confocal Microscopy

    Kv1.3-eGFP trafficking after siRNA mediated knockdown of Sec24. Kv1.3-eGFP trafficking was examined after the knockdown of Sec24 isoforms (as indicated) in the presences of the membranous ER resident protein Sec61β tagged with the mCherry fluorophore (Sec61β-mCherry). Cellular nuclei were stained with DAPI. The wild-type (wt) trafficking profile is similar to the trafficking profile of Sec24c and Sec24cd knockdown conditions. An altered trafficking profile is seen in Sec24a, Sec24b, Sec24ab, and Sec24abcd conditions. Interestingly, there is also an altered trafficking profile in the Sec24d condition, but the Kv1.3-eGFP signal does not overlap well with the Sec61β protein. Line scans of each fluorescent channel are shown. The white arrow in the merged image represents the placement and direction of the line scan. Scale bar = 5 μm

    Journal: BMC Biochemistry

    Article Title: Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a

    doi: 10.1186/s12858-015-0045-6

    Figure Lengend Snippet: Kv1.3-eGFP trafficking after siRNA mediated knockdown of Sec24. Kv1.3-eGFP trafficking was examined after the knockdown of Sec24 isoforms (as indicated) in the presences of the membranous ER resident protein Sec61β tagged with the mCherry fluorophore (Sec61β-mCherry). Cellular nuclei were stained with DAPI. The wild-type (wt) trafficking profile is similar to the trafficking profile of Sec24c and Sec24cd knockdown conditions. An altered trafficking profile is seen in Sec24a, Sec24b, Sec24ab, and Sec24abcd conditions. Interestingly, there is also an altered trafficking profile in the Sec24d condition, but the Kv1.3-eGFP signal does not overlap well with the Sec61β protein. Line scans of each fluorescent channel are shown. The white arrow in the merged image represents the placement and direction of the line scan. Scale bar = 5 μm

    Article Snippet: Blocked membranes were incubated overnight at 4 °C with Kv1.3 antisera, FSU120, generated against the intracellular C-terminal domain [ ] and an anti-actin primary antibody (Millipore).

    Techniques: Staining

    Retention of Kv1.3-eGFP in the ER upon sequential mutation of the acidic motif. Bar graph depicting the amount of Kv1.3-eGFP or mutant proteins retained in the ER. Ratio of relative percent intensity is equal to the amount of protein retained in the ER microsome fractions divided by the total amount of protein from whole cell homogenates. Resulting values were plotted as the mean ± standard error of the mean of three replicates ( n = 3). The only statistically different mutant was the Kv1.3-eGFP E443A-E445A-E447A by one-way ANOVA, Bonferoni correction applied for Type-1 errors (p > 0.008)

    Journal: BMC Biochemistry

    Article Title: Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a

    doi: 10.1186/s12858-015-0045-6

    Figure Lengend Snippet: Retention of Kv1.3-eGFP in the ER upon sequential mutation of the acidic motif. Bar graph depicting the amount of Kv1.3-eGFP or mutant proteins retained in the ER. Ratio of relative percent intensity is equal to the amount of protein retained in the ER microsome fractions divided by the total amount of protein from whole cell homogenates. Resulting values were plotted as the mean ± standard error of the mean of three replicates ( n = 3). The only statistically different mutant was the Kv1.3-eGFP E443A-E445A-E447A by one-way ANOVA, Bonferoni correction applied for Type-1 errors (p > 0.008)

    Article Snippet: Blocked membranes were incubated overnight at 4 °C with Kv1.3 antisera, FSU120, generated against the intracellular C-terminal domain [ ] and an anti-actin primary antibody (Millipore).

    Techniques: Mutagenesis

    Biophysical properties of Kv1.3 channels following mutations of the acidic ER export motif. a Bar graph of the mean peak (left) or sustained (middle) current (± s.e.m.) for various voltage-clamped Kv1.3-eGFP or mutant channels as recorded in cell-attached patches using a single step depolarization of +40 mV (V c ) from a holding potential (V h ) of -80 mV. Representative current traces comparing Kv1.3-eGFP with that of Kv1.3-eGFP ∆C (right). b Same as in (A) but comparing inactivation (left) or deactivation (middle) kinetics of Kv1.3-eGFP. Significantly different by one-way ANOVA, Bonferoni’s post-hoc test, * = 0.001. c Line graph of the normalized tail currents is fit with a Boltzmann relation to calculate voltage at half-activation (V 1/2 ). Significantly different V 1/2 by one-way ANOVA, Bonferoni’s post-hoc test, *** = 0.0001, * = 0.001

    Journal: BMC Biochemistry

    Article Title: Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a

    doi: 10.1186/s12858-015-0045-6

    Figure Lengend Snippet: Biophysical properties of Kv1.3 channels following mutations of the acidic ER export motif. a Bar graph of the mean peak (left) or sustained (middle) current (± s.e.m.) for various voltage-clamped Kv1.3-eGFP or mutant channels as recorded in cell-attached patches using a single step depolarization of +40 mV (V c ) from a holding potential (V h ) of -80 mV. Representative current traces comparing Kv1.3-eGFP with that of Kv1.3-eGFP ∆C (right). b Same as in (A) but comparing inactivation (left) or deactivation (middle) kinetics of Kv1.3-eGFP. Significantly different by one-way ANOVA, Bonferoni’s post-hoc test, * = 0.001. c Line graph of the normalized tail currents is fit with a Boltzmann relation to calculate voltage at half-activation (V 1/2 ). Significantly different V 1/2 by one-way ANOVA, Bonferoni’s post-hoc test, *** = 0.0001, * = 0.001

    Article Snippet: Blocked membranes were incubated overnight at 4 °C with Kv1.3 antisera, FSU120, generated against the intracellular C-terminal domain [ ] and an anti-actin primary antibody (Millipore).

    Techniques: Mutagenesis, Activation Assay

    In vitro Kv1.3-Sec24a membrane floatation assay. Membrane floatation assay used to test for the association between Kv1.3 and Sec24a 341 . ( a ) Kv1.3 proteins reconstituted into synthetic lipid vesicles (proteoliposomes) and ( b ) control lipid vesicles (liposomes). ( c ) Schematic of the floatation assay. Proteoliposomes, drawn as small black circles, migrate through the three-step sucrose gradient (0 %, 25 %, and 30 % w/v sucrose; top (1), middle (2) and bottom (3), respectively) after incubation and centrifugation. ( d ) Kv1.3 proteoliposomes were found in the top fraction after centrifugation. ( e ) When Kv1.3 proteoliposomes (~65 kDa as a monomer) were incubated with Sec24a 341 (~80 kDa), both Kv1.3 and Sec24a 341 were detected in the top fraction. ( f ) Sec24a 341 alone was not detected in the top fraction. ( g ) When Kv1.3 proteins in detergent micelles were mixed with Sec24a 341 in the presence of control liposomes, both Kv1.3 and Sec24a 341 were found in the top fraction. ( h ) Sec24a 341 incubated with control liposomes was not found in the top fraction. ( i ) Kv1.3 micelles and Sec24a 341 do not float in the absence of membranes. ( j ) Kv1.3 was detected in the top fraction when Kv1.3 in detergent micelles were incubated with control liposomes. Scale bar = 100 nm

    Journal: BMC Biochemistry

    Article Title: Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a

    doi: 10.1186/s12858-015-0045-6

    Figure Lengend Snippet: In vitro Kv1.3-Sec24a membrane floatation assay. Membrane floatation assay used to test for the association between Kv1.3 and Sec24a 341 . ( a ) Kv1.3 proteins reconstituted into synthetic lipid vesicles (proteoliposomes) and ( b ) control lipid vesicles (liposomes). ( c ) Schematic of the floatation assay. Proteoliposomes, drawn as small black circles, migrate through the three-step sucrose gradient (0 %, 25 %, and 30 % w/v sucrose; top (1), middle (2) and bottom (3), respectively) after incubation and centrifugation. ( d ) Kv1.3 proteoliposomes were found in the top fraction after centrifugation. ( e ) When Kv1.3 proteoliposomes (~65 kDa as a monomer) were incubated with Sec24a 341 (~80 kDa), both Kv1.3 and Sec24a 341 were detected in the top fraction. ( f ) Sec24a 341 alone was not detected in the top fraction. ( g ) When Kv1.3 proteins in detergent micelles were mixed with Sec24a 341 in the presence of control liposomes, both Kv1.3 and Sec24a 341 were found in the top fraction. ( h ) Sec24a 341 incubated with control liposomes was not found in the top fraction. ( i ) Kv1.3 micelles and Sec24a 341 do not float in the absence of membranes. ( j ) Kv1.3 was detected in the top fraction when Kv1.3 in detergent micelles were incubated with control liposomes. Scale bar = 100 nm

    Article Snippet: Blocked membranes were incubated overnight at 4 °C with Kv1.3 antisera, FSU120, generated against the intracellular C-terminal domain [ ] and an anti-actin primary antibody (Millipore).

    Techniques: In Vitro, Incubation, Centrifugation

    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