cardiotrophin 1  (Alomone Labs)


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    Alomone Labs cardiotrophin 1
    Cardiotrophin 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 1 article reviews
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    cardiotrophin 1 - by Bioz Stars, 2022-05
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    Alomone Labs antibody against aqp3
    A549 cell aggregation is an active process. ( A ) The effect of ROCK on A549 cell aggregation. The phase-contrast micrographs show the morphologies of the A549 cells following treatment with a ROCK inhibitor, Y-27632, and the Rho activator Ⅱ. ( B ) The effects of <t>AQP3</t> knockdown with siRNA on actomyosin cytoskeleton remodeling. A549 cells were stained with anti-AQP3 antibody, followed by Fluorescein-conjugated antibody (green). The actin microfilaments were stained with rhodamine-conjugated phalloidin (red), and the nuclei were stained with DAPI (blue). ( C ) The effects of AQP3 knockdown with siRNA on the apoptosis signaling pathway. Twenty-four h following siRNA transfection in 2D culture condition, the cells were further incubated in the 2D or 3D culture condition. Then, cells were harvested to confirm the effect of AQP3 knockdown on the apoptotic molecular signatures using Western blotting. α-tubulin was used as an internal control.
    Antibody Against Aqp3, 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/antibody against aqp3/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody against aqp3 - by Bioz Stars, 2022-05
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    95
    Alomone Labs anti trpa1 antibodies
    Oxaliplatin increases <t>TRPA1</t> protein expression as seen with immunohistochemistry in the DRG. a Effect of oxaliplatin (6 mg/kg, i.p.) on co-localization of TRPA1 protein expression with isolectin B4 binding in rat DRG (L 4–6 ) neurons. The photomicrographs show representative data. Co-localization of TRPA1 expression ( red ) and isolectin B4 binding ( green ) is shown. Double-labeled neurons ( arrowheads ) are stained yellow in the merged panel. b Histogram shows the percent of TRPA1-positive neurons relative to isolectin B4-binding neurons. TRPA1 and isolectin B4 co-localization was significantly higher on day 2 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose treatment. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration (6 mg/kg, i.p.). *P
    Anti Trpa1 Antibodies, 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
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    A549 cell aggregation is an active process. ( A ) The effect of ROCK on A549 cell aggregation. The phase-contrast micrographs show the morphologies of the A549 cells following treatment with a ROCK inhibitor, Y-27632, and the Rho activator Ⅱ. ( B ) The effects of AQP3 knockdown with siRNA on actomyosin cytoskeleton remodeling. A549 cells were stained with anti-AQP3 antibody, followed by Fluorescein-conjugated antibody (green). The actin microfilaments were stained with rhodamine-conjugated phalloidin (red), and the nuclei were stained with DAPI (blue). ( C ) The effects of AQP3 knockdown with siRNA on the apoptosis signaling pathway. Twenty-four h following siRNA transfection in 2D culture condition, the cells were further incubated in the 2D or 3D culture condition. Then, cells were harvested to confirm the effect of AQP3 knockdown on the apoptotic molecular signatures using Western blotting. α-tubulin was used as an internal control.

    Journal: International Journal of Molecular Sciences

    Article Title: AQP3 Increases Intercellular Cohesion in NSCLC A549 Cell Spheroids through Exploratory Cell Protrusions

    doi: 10.3390/ijms22084287

    Figure Lengend Snippet: A549 cell aggregation is an active process. ( A ) The effect of ROCK on A549 cell aggregation. The phase-contrast micrographs show the morphologies of the A549 cells following treatment with a ROCK inhibitor, Y-27632, and the Rho activator Ⅱ. ( B ) The effects of AQP3 knockdown with siRNA on actomyosin cytoskeleton remodeling. A549 cells were stained with anti-AQP3 antibody, followed by Fluorescein-conjugated antibody (green). The actin microfilaments were stained with rhodamine-conjugated phalloidin (red), and the nuclei were stained with DAPI (blue). ( C ) The effects of AQP3 knockdown with siRNA on the apoptosis signaling pathway. Twenty-four h following siRNA transfection in 2D culture condition, the cells were further incubated in the 2D or 3D culture condition. Then, cells were harvested to confirm the effect of AQP3 knockdown on the apoptotic molecular signatures using Western blotting. α-tubulin was used as an internal control.

    Article Snippet: The samples were then separated with SDS-PAGE gel and immunoblotted with the antibody against AQP3 (Alomone Labs Ltd., Jerusalem, Israel, 1/200), GAPDH (BioLegend, San Diego, CA, USA), or β-actin (Santa Cruz Biotechnology) or α-tubulin (Santa Cruz Biotechnology). β-actin, GAPDH, and α-tubulin were used as loading controls.

    Techniques: Staining, Transfection, Incubation, Western Blot

    The effect of AQP3 on spatiotemporal dynamics of protrusions. ( A ) Polymerase chain reaction and ( B ) Quantitative real-time reverse transcription-polymerase chain reaction of the transcript levels of the organic hydroxyl transport genes. The data shown here represent three independent experiments, and the values represent the mean ± SEM of triplicate samples. The level of each mRNA was normalized to that of the GAPDH mRNA in the same sample and presented as the fold-change over that of the 2D culture control cells. The differences in expression levels were evaluated for significance using two-tailed t-tests with unequal variance. * p

    Journal: International Journal of Molecular Sciences

    Article Title: AQP3 Increases Intercellular Cohesion in NSCLC A549 Cell Spheroids through Exploratory Cell Protrusions

    doi: 10.3390/ijms22084287

    Figure Lengend Snippet: The effect of AQP3 on spatiotemporal dynamics of protrusions. ( A ) Polymerase chain reaction and ( B ) Quantitative real-time reverse transcription-polymerase chain reaction of the transcript levels of the organic hydroxyl transport genes. The data shown here represent three independent experiments, and the values represent the mean ± SEM of triplicate samples. The level of each mRNA was normalized to that of the GAPDH mRNA in the same sample and presented as the fold-change over that of the 2D culture control cells. The differences in expression levels were evaluated for significance using two-tailed t-tests with unequal variance. * p

    Article Snippet: The samples were then separated with SDS-PAGE gel and immunoblotted with the antibody against AQP3 (Alomone Labs Ltd., Jerusalem, Israel, 1/200), GAPDH (BioLegend, San Diego, CA, USA), or β-actin (Santa Cruz Biotechnology) or α-tubulin (Santa Cruz Biotechnology). β-actin, GAPDH, and α-tubulin were used as loading controls.

    Techniques: Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Expressing, Two Tailed Test

    Expression of SK3 channels, Abi-1 and nWASP in neuronal stem cells (NSCs) and in primary hippocampal neurons (HNs). (A) Western Blot analysis of SK3 channel transfected NSCs (SK3 pIRES) indicates that the SK3 channel antibody readily recognizes the overexpressed protein. NSCs transfected with the RNAi construct show a decrease of SK3 protein compared to NSCs transfected with a scrambled RNAi construct and untransfected cells. The SK3 channel protein can also be detected in hippocampal neurons. Subfractionation of brain tissue reveals that the protein is enriched towards the postsynaptic density fraction (PSD). (B) nWASP and Abi-1 are detectable in NSCs as well as in hippocampal neurons. (C) Light cycler analysis of SK3 channel mRNA in NSCs and hippocampal neurons reveals that SK3 transcript levels are downregulated after induction of differentiation in NSCs but show a steep increase in later steps of hippocampal neuron maturation. P -values from ANOVA for multiple-group comparison are 0.0011 for NSCs and

    Journal: PLoS ONE

    Article Title: An SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis

    doi: 10.1371/journal.pone.0018148

    Figure Lengend Snippet: Expression of SK3 channels, Abi-1 and nWASP in neuronal stem cells (NSCs) and in primary hippocampal neurons (HNs). (A) Western Blot analysis of SK3 channel transfected NSCs (SK3 pIRES) indicates that the SK3 channel antibody readily recognizes the overexpressed protein. NSCs transfected with the RNAi construct show a decrease of SK3 protein compared to NSCs transfected with a scrambled RNAi construct and untransfected cells. The SK3 channel protein can also be detected in hippocampal neurons. Subfractionation of brain tissue reveals that the protein is enriched towards the postsynaptic density fraction (PSD). (B) nWASP and Abi-1 are detectable in NSCs as well as in hippocampal neurons. (C) Light cycler analysis of SK3 channel mRNA in NSCs and hippocampal neurons reveals that SK3 transcript levels are downregulated after induction of differentiation in NSCs but show a steep increase in later steps of hippocampal neuron maturation. P -values from ANOVA for multiple-group comparison are 0.0011 for NSCs and

    Article Snippet: The following primary antibodies were used: rabbit anti-SK3 diluted 1∶200, rabbit (Alomone Labs), mouse anti-Nestin monoclonal diluted 1∶500 (BD Biosciences), mouse anti-Abi-1 diluted 1∶250 (MBL), mouse anti-myc antibody diluted 1∶500 (Invitrogen), rabbit anti-PSD95 diluted 1∶1000, rabbit anti-SV2 diluted 1∶300 (both abcam, Cambridge, USA) and rabbit anti-nWASP diluted 1∶500 (Santa Cruz) or chicken anti-nWASP diluted 1∶500 (abcam); fluorescence labeled secondary antibodies were Alexa Fluor® 488 (green, used filter set: excitation BP 450 – 490, FT 510, emission BP 515 - 565), Alexa Fluor® 568 (red, used filter set: excitation BP 534 nm–558 nm, FT 560, emission BP 575 - 640) and Alexa Fluor® 647 (magenta used filter set: excitation BP 610 nm–670 nm, FT 660, emission BP 640–740 (all from Invitrogen) all diluted 1∶500.

    Techniques: Expressing, Western Blot, Transfection, Construct

    Pharmacological treatment of NSCs with 1-EBIO, wiskostatin and apamin. Application of the SK3 channel opening substance 1-EBIO shows the rapid outgrowth and enlargement of filopodia with a translocation of the channel into the newly build processes in SK3 channel overexpressing NSCs. Apamin treatment that leads to a blockage of SK3 channels as well as the application of wiskostatin drastically reduces filopodia formation. (B) Double transfection of NSCs with SK3 channels and Abi-1 results in the co-localization of both proteins in the cell cytoplasm. The application of wiskostatin and apamin to the cells induced the translocation of the proteins to small microcompartments. In contrast, the SK3 channel activator 1-EBIO induced the rapid outgrowth of numerous large lamellipodia that show a netlike arrangement of SK3 channel immunoreactivity. (C) The double transfection of SK3 channels and nWASP resulted in a morphology of NSCs that was characterized by larger filopodial extensions that were lost after application of wiskostatin, enhanced and more elaborated under the influence of 1-EBIO and altered towards lamellipodia after apamin application. Scale bars as indicated.

    Journal: PLoS ONE

    Article Title: An SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis

    doi: 10.1371/journal.pone.0018148

    Figure Lengend Snippet: Pharmacological treatment of NSCs with 1-EBIO, wiskostatin and apamin. Application of the SK3 channel opening substance 1-EBIO shows the rapid outgrowth and enlargement of filopodia with a translocation of the channel into the newly build processes in SK3 channel overexpressing NSCs. Apamin treatment that leads to a blockage of SK3 channels as well as the application of wiskostatin drastically reduces filopodia formation. (B) Double transfection of NSCs with SK3 channels and Abi-1 results in the co-localization of both proteins in the cell cytoplasm. The application of wiskostatin and apamin to the cells induced the translocation of the proteins to small microcompartments. In contrast, the SK3 channel activator 1-EBIO induced the rapid outgrowth of numerous large lamellipodia that show a netlike arrangement of SK3 channel immunoreactivity. (C) The double transfection of SK3 channels and nWASP resulted in a morphology of NSCs that was characterized by larger filopodial extensions that were lost after application of wiskostatin, enhanced and more elaborated under the influence of 1-EBIO and altered towards lamellipodia after apamin application. Scale bars as indicated.

    Article Snippet: The following primary antibodies were used: rabbit anti-SK3 diluted 1∶200, rabbit (Alomone Labs), mouse anti-Nestin monoclonal diluted 1∶500 (BD Biosciences), mouse anti-Abi-1 diluted 1∶250 (MBL), mouse anti-myc antibody diluted 1∶500 (Invitrogen), rabbit anti-PSD95 diluted 1∶1000, rabbit anti-SV2 diluted 1∶300 (both abcam, Cambridge, USA) and rabbit anti-nWASP diluted 1∶500 (Santa Cruz) or chicken anti-nWASP diluted 1∶500 (abcam); fluorescence labeled secondary antibodies were Alexa Fluor® 488 (green, used filter set: excitation BP 450 – 490, FT 510, emission BP 515 - 565), Alexa Fluor® 568 (red, used filter set: excitation BP 534 nm–558 nm, FT 560, emission BP 575 - 640) and Alexa Fluor® 647 (magenta used filter set: excitation BP 610 nm–670 nm, FT 660, emission BP 640–740 (all from Invitrogen) all diluted 1∶500.

    Techniques: Translocation Assay, Transfection

    Structure and expression of the SK3 channel. (A,B) Domain structure and amino acid sequence of the rat SK3 channel. An N-terminal proline rich region (green) is indicated that harbors the interaction domain with the SH3 domain of Abi-1 (red). Bold letters indicate the transmembrane domains that are organized around the pore region (yellow). At the C-terminus the calmodulin binding site (light blue) as well as a coiled coil domain (purple) with a leucine zipper motif (purple in black frame) is located. (C) In situ hybridization experiments of a whole body embryo section at developmental stage day 20 and during rat brain development show that the SK3 channel transcripts are nearly exclusively expressed in brain. In embryonic tissue the mRNA is especially found in the subventricular zone, during brain development the transcripts are densely expressed in the dentate gyrus, the olfactory bulb, caudate putamen and in thalamic nuclei. (D) This schematic drawing illustrates the intramembranous localization of the protein showing that both the C- and the N-terminus are intracellular.

    Journal: PLoS ONE

    Article Title: An SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis

    doi: 10.1371/journal.pone.0018148

    Figure Lengend Snippet: Structure and expression of the SK3 channel. (A,B) Domain structure and amino acid sequence of the rat SK3 channel. An N-terminal proline rich region (green) is indicated that harbors the interaction domain with the SH3 domain of Abi-1 (red). Bold letters indicate the transmembrane domains that are organized around the pore region (yellow). At the C-terminus the calmodulin binding site (light blue) as well as a coiled coil domain (purple) with a leucine zipper motif (purple in black frame) is located. (C) In situ hybridization experiments of a whole body embryo section at developmental stage day 20 and during rat brain development show that the SK3 channel transcripts are nearly exclusively expressed in brain. In embryonic tissue the mRNA is especially found in the subventricular zone, during brain development the transcripts are densely expressed in the dentate gyrus, the olfactory bulb, caudate putamen and in thalamic nuclei. (D) This schematic drawing illustrates the intramembranous localization of the protein showing that both the C- and the N-terminus are intracellular.

    Article Snippet: The following primary antibodies were used: rabbit anti-SK3 diluted 1∶200, rabbit (Alomone Labs), mouse anti-Nestin monoclonal diluted 1∶500 (BD Biosciences), mouse anti-Abi-1 diluted 1∶250 (MBL), mouse anti-myc antibody diluted 1∶500 (Invitrogen), rabbit anti-PSD95 diluted 1∶1000, rabbit anti-SV2 diluted 1∶300 (both abcam, Cambridge, USA) and rabbit anti-nWASP diluted 1∶500 (Santa Cruz) or chicken anti-nWASP diluted 1∶500 (abcam); fluorescence labeled secondary antibodies were Alexa Fluor® 488 (green, used filter set: excitation BP 450 – 490, FT 510, emission BP 515 - 565), Alexa Fluor® 568 (red, used filter set: excitation BP 534 nm–558 nm, FT 560, emission BP 575 - 640) and Alexa Fluor® 647 (magenta used filter set: excitation BP 610 nm–670 nm, FT 660, emission BP 640–740 (all from Invitrogen) all diluted 1∶500.

    Techniques: Expressing, Sequencing, Binding Assay, In Situ Hybridization

    SK3 channel, nWASP and Abi-1 protein levels also alter hippocampal neuron morphology. (A) In close homology to the observation in NSCs we found that the overexpression of SK3 channels as well as of nWASP in developing hippocampal neurons is leading to a very complex dendritic tree with numerous secondary and tertiary dendrites. In contrast the Abi-1-GFP fusion protein extremely simplifies the dendritic arbor. (B-C) Overexpression of SK3 channels and Abi-1, nWASP respectively, resulted in a perfect co-localization of both fusion proteins especially in outgrowing neurites. Co-expression of SK3 channels and Abi-1 abolishes the SK3 channel overexpression phenotype while the addition of nWASP to SK3 channel transfected neurons is leading to a multidendritic neuron that is characterized by numerous primary, secondary and tertiary neurites. Nuclei are stained with DAPI (blue). Scale bars as indicated.

    Journal: PLoS ONE

    Article Title: An SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis

    doi: 10.1371/journal.pone.0018148

    Figure Lengend Snippet: SK3 channel, nWASP and Abi-1 protein levels also alter hippocampal neuron morphology. (A) In close homology to the observation in NSCs we found that the overexpression of SK3 channels as well as of nWASP in developing hippocampal neurons is leading to a very complex dendritic tree with numerous secondary and tertiary dendrites. In contrast the Abi-1-GFP fusion protein extremely simplifies the dendritic arbor. (B-C) Overexpression of SK3 channels and Abi-1, nWASP respectively, resulted in a perfect co-localization of both fusion proteins especially in outgrowing neurites. Co-expression of SK3 channels and Abi-1 abolishes the SK3 channel overexpression phenotype while the addition of nWASP to SK3 channel transfected neurons is leading to a multidendritic neuron that is characterized by numerous primary, secondary and tertiary neurites. Nuclei are stained with DAPI (blue). Scale bars as indicated.

    Article Snippet: The following primary antibodies were used: rabbit anti-SK3 diluted 1∶200, rabbit (Alomone Labs), mouse anti-Nestin monoclonal diluted 1∶500 (BD Biosciences), mouse anti-Abi-1 diluted 1∶250 (MBL), mouse anti-myc antibody diluted 1∶500 (Invitrogen), rabbit anti-PSD95 diluted 1∶1000, rabbit anti-SV2 diluted 1∶300 (both abcam, Cambridge, USA) and rabbit anti-nWASP diluted 1∶500 (Santa Cruz) or chicken anti-nWASP diluted 1∶500 (abcam); fluorescence labeled secondary antibodies were Alexa Fluor® 488 (green, used filter set: excitation BP 450 – 490, FT 510, emission BP 515 - 565), Alexa Fluor® 568 (red, used filter set: excitation BP 534 nm–558 nm, FT 560, emission BP 575 - 640) and Alexa Fluor® 647 (magenta used filter set: excitation BP 610 nm–670 nm, FT 660, emission BP 640–740 (all from Invitrogen) all diluted 1∶500.

    Techniques: Over Expression, Expressing, Transfection, Staining

    SK3 channels, Abi-1 and nWASP are found in neuronal complexes and colocalize in defined subcompartments of NSCs and hippocampal neurons (HNs). (A-B)Triple staining experiments show that Abi-1 as well as nWASP (red) colocalize with the SK3 channel (green) in distinct lamellipodia like structures of NSCs that are also rich of actin fibers stained by phalloidin (magenta), DAPI (blue) is used to label nuclei. (C–D) In hippocampal neurons SK3 channels are densely targeted to dendritic spines/PSDs and co-localize with nWASP as well as with Abi-1 (see arrows in insets). To visualize the cytoskeleton tubulin antibodies (Tubb, magenta) are used, DAPI staining (blue) show neuronal nuclei. (E) Co-immunoprecipitation experiments show the presence of all three molecules in one neuronal complex also in vivo . Magnetic beads loaded with SK3 channels antibodies were employed to precipitate the SK3 channel complex from rat brain. Within this precipitate Abi-1 as well as nWASP can be detected. (F) Schematic drawing of the fusions proteins and Abi-1 deletion constructs used for transfection experiments with their respective domain regions. The SK3 channel codes for a conserved N-terminal proline rich stretch that mediates the interaction with the Abi-1 SH3 domain. (G) Co-transfection of the nWASP with the SK3 channel results in a complete colocalization in NSCs. This is also observed when full length Abi-1-myc is co-transfected with the SK3 channel GFP fusion protein. The co-expression of SK3 channels with an Abi-1 SH3 domain deletion construct (Abi-1 ΔSH3-RFP) results in no co-localization of the proteins while the SK3 channel perfectly co-localizes with the Abi-1-SH3 domain fusion protein. Moreover, the full length SK3 channel protein can co-precipitate the GFP-SH3 domain from the co-transfected cell lysate but fails to bind to the Abi-1 protein that is not expressing the SH3 domain. Scale bars as indicated.

    Journal: PLoS ONE

    Article Title: An SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis

    doi: 10.1371/journal.pone.0018148

    Figure Lengend Snippet: SK3 channels, Abi-1 and nWASP are found in neuronal complexes and colocalize in defined subcompartments of NSCs and hippocampal neurons (HNs). (A-B)Triple staining experiments show that Abi-1 as well as nWASP (red) colocalize with the SK3 channel (green) in distinct lamellipodia like structures of NSCs that are also rich of actin fibers stained by phalloidin (magenta), DAPI (blue) is used to label nuclei. (C–D) In hippocampal neurons SK3 channels are densely targeted to dendritic spines/PSDs and co-localize with nWASP as well as with Abi-1 (see arrows in insets). To visualize the cytoskeleton tubulin antibodies (Tubb, magenta) are used, DAPI staining (blue) show neuronal nuclei. (E) Co-immunoprecipitation experiments show the presence of all three molecules in one neuronal complex also in vivo . Magnetic beads loaded with SK3 channels antibodies were employed to precipitate the SK3 channel complex from rat brain. Within this precipitate Abi-1 as well as nWASP can be detected. (F) Schematic drawing of the fusions proteins and Abi-1 deletion constructs used for transfection experiments with their respective domain regions. The SK3 channel codes for a conserved N-terminal proline rich stretch that mediates the interaction with the Abi-1 SH3 domain. (G) Co-transfection of the nWASP with the SK3 channel results in a complete colocalization in NSCs. This is also observed when full length Abi-1-myc is co-transfected with the SK3 channel GFP fusion protein. The co-expression of SK3 channels with an Abi-1 SH3 domain deletion construct (Abi-1 ΔSH3-RFP) results in no co-localization of the proteins while the SK3 channel perfectly co-localizes with the Abi-1-SH3 domain fusion protein. Moreover, the full length SK3 channel protein can co-precipitate the GFP-SH3 domain from the co-transfected cell lysate but fails to bind to the Abi-1 protein that is not expressing the SH3 domain. Scale bars as indicated.

    Article Snippet: The following primary antibodies were used: rabbit anti-SK3 diluted 1∶200, rabbit (Alomone Labs), mouse anti-Nestin monoclonal diluted 1∶500 (BD Biosciences), mouse anti-Abi-1 diluted 1∶250 (MBL), mouse anti-myc antibody diluted 1∶500 (Invitrogen), rabbit anti-PSD95 diluted 1∶1000, rabbit anti-SV2 diluted 1∶300 (both abcam, Cambridge, USA) and rabbit anti-nWASP diluted 1∶500 (Santa Cruz) or chicken anti-nWASP diluted 1∶500 (abcam); fluorescence labeled secondary antibodies were Alexa Fluor® 488 (green, used filter set: excitation BP 450 – 490, FT 510, emission BP 515 - 565), Alexa Fluor® 568 (red, used filter set: excitation BP 534 nm–558 nm, FT 560, emission BP 575 - 640) and Alexa Fluor® 647 (magenta used filter set: excitation BP 610 nm–670 nm, FT 660, emission BP 640–740 (all from Invitrogen) all diluted 1∶500.

    Techniques: Staining, Immunoprecipitation, In Vivo, Magnetic Beads, Construct, Transfection, Cotransfection, Expressing

    SK3 channel, nWASP and Abi-1 protein levels alter NSC morphology. (A–G) Overexpression of SK3 channels in NSCs significantly triggers long filopodia formation in NSCs while Abi-1 overexpression downregulates filopodia number and length (B). (C) Co-expression of SK3 channels and Abi-1 results in an NSC morphology that is identical to Abi-1 overexpression alone. (D) nWASP transfection strongly induces filopodia formation and this effect can be even enhanced by double transfection of nWASP together with SK3 channels (E). Downregulation of SK3 channels in NSCs by an RNAi construct that efficiently diminishes SK3 channel protein concentrations (F) does not significantly influence filopodia number and/or length of filopodia (G). Scale bars as indicated. (H–I) Statistical analysis of NSC morphology (number of filopodia per 1 µm/length of filopodia) after the above described transfection experiments. P -values from ANOVA for multiple-group comparison are

    Journal: PLoS ONE

    Article Title: An SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis

    doi: 10.1371/journal.pone.0018148

    Figure Lengend Snippet: SK3 channel, nWASP and Abi-1 protein levels alter NSC morphology. (A–G) Overexpression of SK3 channels in NSCs significantly triggers long filopodia formation in NSCs while Abi-1 overexpression downregulates filopodia number and length (B). (C) Co-expression of SK3 channels and Abi-1 results in an NSC morphology that is identical to Abi-1 overexpression alone. (D) nWASP transfection strongly induces filopodia formation and this effect can be even enhanced by double transfection of nWASP together with SK3 channels (E). Downregulation of SK3 channels in NSCs by an RNAi construct that efficiently diminishes SK3 channel protein concentrations (F) does not significantly influence filopodia number and/or length of filopodia (G). Scale bars as indicated. (H–I) Statistical analysis of NSC morphology (number of filopodia per 1 µm/length of filopodia) after the above described transfection experiments. P -values from ANOVA for multiple-group comparison are

    Article Snippet: The following primary antibodies were used: rabbit anti-SK3 diluted 1∶200, rabbit (Alomone Labs), mouse anti-Nestin monoclonal diluted 1∶500 (BD Biosciences), mouse anti-Abi-1 diluted 1∶250 (MBL), mouse anti-myc antibody diluted 1∶500 (Invitrogen), rabbit anti-PSD95 diluted 1∶1000, rabbit anti-SV2 diluted 1∶300 (both abcam, Cambridge, USA) and rabbit anti-nWASP diluted 1∶500 (Santa Cruz) or chicken anti-nWASP diluted 1∶500 (abcam); fluorescence labeled secondary antibodies were Alexa Fluor® 488 (green, used filter set: excitation BP 450 – 490, FT 510, emission BP 515 - 565), Alexa Fluor® 568 (red, used filter set: excitation BP 534 nm–558 nm, FT 560, emission BP 575 - 640) and Alexa Fluor® 647 (magenta used filter set: excitation BP 610 nm–670 nm, FT 660, emission BP 640–740 (all from Invitrogen) all diluted 1∶500.

    Techniques: Over Expression, Expressing, Transfection, Construct

    IAN transection both in NP and non-NP groups changes the expression profile of TRPV1 to myelinated neurons of a larger diameter. The total number of TG cells labeled for the fluoro-gold (FG + ) (A: NP group, B: Non-NP group); TG cells that labeled for TRPV1 and FG (TRPV1 + +FG + ) in 2-; 3-and 4-week NP groups and in sham-operated group (C: NP group, D: Non-NP group). The ratio of TRPV1 + +FG + to all FG+ positive cells (E: NP group, F: Non-NP group). n = 5 for each group, (ANOVA followed by the Student–Newman–Keuls test, *p

    Journal: PLoS ONE

    Article Title: Expression of TRPV1 Channels after Nerve Injury Provides an Essential Delivery Tool for Neuropathic Pain Attenuation

    doi: 10.1371/journal.pone.0044023

    Figure Lengend Snippet: IAN transection both in NP and non-NP groups changes the expression profile of TRPV1 to myelinated neurons of a larger diameter. The total number of TG cells labeled for the fluoro-gold (FG + ) (A: NP group, B: Non-NP group); TG cells that labeled for TRPV1 and FG (TRPV1 + +FG + ) in 2-; 3-and 4-week NP groups and in sham-operated group (C: NP group, D: Non-NP group). The ratio of TRPV1 + +FG + to all FG+ positive cells (E: NP group, F: Non-NP group). n = 5 for each group, (ANOVA followed by the Student–Newman–Keuls test, *p

    Article Snippet: They were then coincubated overnight at 4°C with a combination of rabbit anti-TRPV1 antibody (1∶200; Alomone Labs Ltd., Israel), which was diluted with 3% NGS in 0.01 M PBS with 0.3% Triton X-100, and mouse monoclonal anti-neurofilament 200 (NF200) antibody (1∶1000; Sigma-Aldrich), which was diluted with 3% NGS in 0.01 M PBS with 0.3% Triton X-100.

    Techniques: Expressing, Labeling

    Photomicrographs of immunohistochemistry of TG cells labeled for TRPV1, NF200 and FG in sham-operated group and in 2-; 3-and 4-week NP groups and in 2-; 3- and 4 weeks non-NP groups. Expanded view of TG in the sham-operated group (D1–D4). Arrow points on an example of TRPV1 + +FG + +NF - cell. Arrowhead points on an example of TRPV1 + +FG + +NF + cell. Note that TRPV1-positive cells increased with time after transection. Scale bar: 50 µm.

    Journal: PLoS ONE

    Article Title: Expression of TRPV1 Channels after Nerve Injury Provides an Essential Delivery Tool for Neuropathic Pain Attenuation

    doi: 10.1371/journal.pone.0044023

    Figure Lengend Snippet: Photomicrographs of immunohistochemistry of TG cells labeled for TRPV1, NF200 and FG in sham-operated group and in 2-; 3-and 4-week NP groups and in 2-; 3- and 4 weeks non-NP groups. Expanded view of TG in the sham-operated group (D1–D4). Arrow points on an example of TRPV1 + +FG + +NF - cell. Arrowhead points on an example of TRPV1 + +FG + +NF + cell. Note that TRPV1-positive cells increased with time after transection. Scale bar: 50 µm.

    Article Snippet: They were then coincubated overnight at 4°C with a combination of rabbit anti-TRPV1 antibody (1∶200; Alomone Labs Ltd., Israel), which was diluted with 3% NGS in 0.01 M PBS with 0.3% Triton X-100, and mouse monoclonal anti-neurofilament 200 (NF200) antibody (1∶1000; Sigma-Aldrich), which was diluted with 3% NGS in 0.01 M PBS with 0.3% Triton X-100.

    Techniques: Immunohistochemistry, Labeling

    The pattern of distribution of TRPV1 was altered in non-NP groups. The distribution area of TRPV1 + +FG + +NF + positive cells for all experimental groups. A cell area > 1000 µm 2 was considered large, while that

    Journal: PLoS ONE

    Article Title: Expression of TRPV1 Channels after Nerve Injury Provides an Essential Delivery Tool for Neuropathic Pain Attenuation

    doi: 10.1371/journal.pone.0044023

    Figure Lengend Snippet: The pattern of distribution of TRPV1 was altered in non-NP groups. The distribution area of TRPV1 + +FG + +NF + positive cells for all experimental groups. A cell area > 1000 µm 2 was considered large, while that

    Article Snippet: They were then coincubated overnight at 4°C with a combination of rabbit anti-TRPV1 antibody (1∶200; Alomone Labs Ltd., Israel), which was diluted with 3% NGS in 0.01 M PBS with 0.3% Triton X-100, and mouse monoclonal anti-neurofilament 200 (NF200) antibody (1∶1000; Sigma-Aldrich), which was diluted with 3% NGS in 0.01 M PBS with 0.3% Triton X-100.

    Techniques:

    Oxaliplatin increases TRPA1 protein expression as seen with immunohistochemistry in the DRG. a Effect of oxaliplatin (6 mg/kg, i.p.) on co-localization of TRPA1 protein expression with isolectin B4 binding in rat DRG (L 4–6 ) neurons. The photomicrographs show representative data. Co-localization of TRPA1 expression ( red ) and isolectin B4 binding ( green ) is shown. Double-labeled neurons ( arrowheads ) are stained yellow in the merged panel. b Histogram shows the percent of TRPA1-positive neurons relative to isolectin B4-binding neurons. TRPA1 and isolectin B4 co-localization was significantly higher on day 2 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose treatment. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration (6 mg/kg, i.p.). *P

    Journal: Molecular Pain

    Article Title: Transient receptor potential ankyrin 1 that is induced in dorsal root ganglion neurons contributes to acute cold hypersensitivity after oxaliplatin administration

    doi: 10.1186/s12990-015-0072-8

    Figure Lengend Snippet: Oxaliplatin increases TRPA1 protein expression as seen with immunohistochemistry in the DRG. a Effect of oxaliplatin (6 mg/kg, i.p.) on co-localization of TRPA1 protein expression with isolectin B4 binding in rat DRG (L 4–6 ) neurons. The photomicrographs show representative data. Co-localization of TRPA1 expression ( red ) and isolectin B4 binding ( green ) is shown. Double-labeled neurons ( arrowheads ) are stained yellow in the merged panel. b Histogram shows the percent of TRPA1-positive neurons relative to isolectin B4-binding neurons. TRPA1 and isolectin B4 co-localization was significantly higher on day 2 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose treatment. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration (6 mg/kg, i.p.). *P

    Article Snippet: DRG sections were incubated with excess blocking buffer containing 2 % skim milk in 0.1 % Triton X-100 in K+ -free PBS and subsequently reacted overnight at 4 °C with anti-TRPA1 antibodies (Alomone Labs, 1:200) in 2 % bovine serum albumin/0.1 % Triton X-100 in K+ -free PBS.

    Techniques: Expressing, Immunohistochemistry, Binding Assay, Labeling, Staining

    Effect of oxaliplatin on TRPA1 mRNA as seen with in situ hybridization histochemistry in rat DRG (L 4–6 ) neurons. a Oxaliplatin (6 mg/kg, i.p.) increases the co-localization between TRPA1 and p-p38 MAP kinase in rat DRG (L 4–6 ) neurons. The photomicrographs show representative data. Co-localization of TRPA1 mRNA ( green ) and p-p38 MAPK ( red ) is shown. Double-labeled neurons ( arrowheads ) appear yellow in the merged panel. b Histogram shows the percent of TRPA1 mRNA-positive neurons relative to p-p38-positive neurons. TRPA1 mRNA and p-p38 co-localization was significantly higher on day 2 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose treatment. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration. *P

    Journal: Molecular Pain

    Article Title: Transient receptor potential ankyrin 1 that is induced in dorsal root ganglion neurons contributes to acute cold hypersensitivity after oxaliplatin administration

    doi: 10.1186/s12990-015-0072-8

    Figure Lengend Snippet: Effect of oxaliplatin on TRPA1 mRNA as seen with in situ hybridization histochemistry in rat DRG (L 4–6 ) neurons. a Oxaliplatin (6 mg/kg, i.p.) increases the co-localization between TRPA1 and p-p38 MAP kinase in rat DRG (L 4–6 ) neurons. The photomicrographs show representative data. Co-localization of TRPA1 mRNA ( green ) and p-p38 MAPK ( red ) is shown. Double-labeled neurons ( arrowheads ) appear yellow in the merged panel. b Histogram shows the percent of TRPA1 mRNA-positive neurons relative to p-p38-positive neurons. TRPA1 mRNA and p-p38 co-localization was significantly higher on day 2 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose treatment. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration. *P

    Article Snippet: DRG sections were incubated with excess blocking buffer containing 2 % skim milk in 0.1 % Triton X-100 in K+ -free PBS and subsequently reacted overnight at 4 °C with anti-TRPA1 antibodies (Alomone Labs, 1:200) in 2 % bovine serum albumin/0.1 % Triton X-100 in K+ -free PBS.

    Techniques: In Situ Hybridization, Labeling

    Oxaliplatin administration increases TRPA1 mRNA and protein in DRGs. a Effect of oxaliplatin (6 mg/kg, i.p.) on TRPA1 mRNA expression in rat DRGs (L 4–6 ) at days 0 (before administration), 1, 2, 4, and 7 was measured. TRPA1 expression was normalized to β-actin expression. Histograms show the relative amount of TRPA1 mRNA in oxaliplatin-treated rats compared with day 0. Data are the mean ± SEM. n = 4 for oxaliplatin administration. *P

    Journal: Molecular Pain

    Article Title: Transient receptor potential ankyrin 1 that is induced in dorsal root ganglion neurons contributes to acute cold hypersensitivity after oxaliplatin administration

    doi: 10.1186/s12990-015-0072-8

    Figure Lengend Snippet: Oxaliplatin administration increases TRPA1 mRNA and protein in DRGs. a Effect of oxaliplatin (6 mg/kg, i.p.) on TRPA1 mRNA expression in rat DRGs (L 4–6 ) at days 0 (before administration), 1, 2, 4, and 7 was measured. TRPA1 expression was normalized to β-actin expression. Histograms show the relative amount of TRPA1 mRNA in oxaliplatin-treated rats compared with day 0. Data are the mean ± SEM. n = 4 for oxaliplatin administration. *P

    Article Snippet: DRG sections were incubated with excess blocking buffer containing 2 % skim milk in 0.1 % Triton X-100 in K+ -free PBS and subsequently reacted overnight at 4 °C with anti-TRPA1 antibodies (Alomone Labs, 1:200) in 2 % bovine serum albumin/0.1 % Triton X-100 in K+ -free PBS.

    Techniques: Expressing

    Effect of oxaliplatin on cold hypersensitivity after TRPA1 knockdown in the acetone spray test and water spray test. Intrathecal administration of TRPA1 AS-ODN prevents cold hypersensitivity induced by oxaliplatin (6 mg/kg, i.p.) as seen with the acetone spray test, but not the water spray test. The water spray test (22 °C) and acetone spray test at days 1, 2, 4, and 7 after oxaliplatin were measured in TRPA1 AS-ODN and TRPA1 MM-ODN treatment groups. a Histograms show the mean ± SEM of cold hypersensitivity at days 0 (before administration), 1, 2, 4, and 7 after oxaliplatin administration in the water spray test (22 °C). b Histograms show cold hypersensitivity at days 0 (before administration), 1, 2, 4, and 7 after oxaliplatin administration in the acetone spray test. Data are the mean ± SEM. n = 4 for oxaliplatin administration. *P

    Journal: Molecular Pain

    Article Title: Transient receptor potential ankyrin 1 that is induced in dorsal root ganglion neurons contributes to acute cold hypersensitivity after oxaliplatin administration

    doi: 10.1186/s12990-015-0072-8

    Figure Lengend Snippet: Effect of oxaliplatin on cold hypersensitivity after TRPA1 knockdown in the acetone spray test and water spray test. Intrathecal administration of TRPA1 AS-ODN prevents cold hypersensitivity induced by oxaliplatin (6 mg/kg, i.p.) as seen with the acetone spray test, but not the water spray test. The water spray test (22 °C) and acetone spray test at days 1, 2, 4, and 7 after oxaliplatin were measured in TRPA1 AS-ODN and TRPA1 MM-ODN treatment groups. a Histograms show the mean ± SEM of cold hypersensitivity at days 0 (before administration), 1, 2, 4, and 7 after oxaliplatin administration in the water spray test (22 °C). b Histograms show cold hypersensitivity at days 0 (before administration), 1, 2, 4, and 7 after oxaliplatin administration in the acetone spray test. Data are the mean ± SEM. n = 4 for oxaliplatin administration. *P

    Article Snippet: DRG sections were incubated with excess blocking buffer containing 2 % skim milk in 0.1 % Triton X-100 in K+ -free PBS and subsequently reacted overnight at 4 °C with anti-TRPA1 antibodies (Alomone Labs, 1:200) in 2 % bovine serum albumin/0.1 % Triton X-100 in K+ -free PBS.

    Techniques:

    Oxaliplatin increases TRPA1 mRNA as seen with in situ hybridization histochemistry in the DRG. Effect of oxaliplatin (6 mg/kg, i.p.) on TRPA1 mRNA expression in rat DRG (L 4–6 ) neurons. a Photomicrographs showing in situ hybridization for TRPA1 mRNA at day 2 after oxaliplatin (6 mg/kg, i.p.). TRPA1 mRNA-expressing small-sized neurons were more frequently observed after oxaliplatin treatment. b Size distribution of TRPA1-expressing neurons in DRGs in 5 % glucose- and oxaliplatin-treated rats. TRPA1 expression was distributed in all sizes of neurons, but most TRPA1 expression was found in small DRG neurons. c Histogram shows the percent of TRPA1-positive neurons relative to the total neurons. TRPA1 mRNA-expressing neurons were more frequently observed at days 1, 2, 4, and 7 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose-treated animals. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration. *P

    Journal: Molecular Pain

    Article Title: Transient receptor potential ankyrin 1 that is induced in dorsal root ganglion neurons contributes to acute cold hypersensitivity after oxaliplatin administration

    doi: 10.1186/s12990-015-0072-8

    Figure Lengend Snippet: Oxaliplatin increases TRPA1 mRNA as seen with in situ hybridization histochemistry in the DRG. Effect of oxaliplatin (6 mg/kg, i.p.) on TRPA1 mRNA expression in rat DRG (L 4–6 ) neurons. a Photomicrographs showing in situ hybridization for TRPA1 mRNA at day 2 after oxaliplatin (6 mg/kg, i.p.). TRPA1 mRNA-expressing small-sized neurons were more frequently observed after oxaliplatin treatment. b Size distribution of TRPA1-expressing neurons in DRGs in 5 % glucose- and oxaliplatin-treated rats. TRPA1 expression was distributed in all sizes of neurons, but most TRPA1 expression was found in small DRG neurons. c Histogram shows the percent of TRPA1-positive neurons relative to the total neurons. TRPA1 mRNA-expressing neurons were more frequently observed at days 1, 2, 4, and 7 after oxaliplatin administration (6 mg/kg, i.p.) compared to 5 % glucose-treated animals. Data are the mean ± SEM. n = 4 each for 5 % glucose and oxaliplatin administration. *P

    Article Snippet: DRG sections were incubated with excess blocking buffer containing 2 % skim milk in 0.1 % Triton X-100 in K+ -free PBS and subsequently reacted overnight at 4 °C with anti-TRPA1 antibodies (Alomone Labs, 1:200) in 2 % bovine serum albumin/0.1 % Triton X-100 in K+ -free PBS.

    Techniques: In Situ Hybridization, Expressing