guinea pig anti asic1  (Alomone Labs)


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    Name:
    Guinea pig Anti ASIC1 Antibody
    Description:
    Guinea pig Anti ASIC1 Antibody is directed against an epitope of rat ASIC1 Guinea pig Anti ASIC1 Antibody AGP 053 raised in guinea pig can be used in western blot immunohistochemistry and immunocytochemistry applications It has been designed to recognize ASIC1 from mouse rat and human samples The antigen used to immunize guinea pigs is the same as Anti ASIC1 Antibody ASC 014 raised in rabbit Our line of guinea pig antibodies enables more flexibility with our products such as multiplex staining studies immunoprecipitation etc
    Catalog Number:
    AGP-053
    Price:
    397.0
    Category:
    Primary Antibody
    Applications:
    Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Western Blot
    Purity:
    Affinity purified on immobilized antigen.
    Immunogen:
    Synthetic peptide
    Size:
    25 mcl
    Antibody Type:
    Polyclonal Primary Antibodies
    Format:
    Lyophilized Powder
    Host:
    Guinea pig
    Isotype:
    Guinea pig total IgG
    Buy from Supplier


    Structured Review

    Alomone Labs guinea pig anti asic1
    Guinea pig Anti ASIC1 Antibody
    Guinea pig Anti ASIC1 Antibody is directed against an epitope of rat ASIC1 Guinea pig Anti ASIC1 Antibody AGP 053 raised in guinea pig can be used in western blot immunohistochemistry and immunocytochemistry applications It has been designed to recognize ASIC1 from mouse rat and human samples The antigen used to immunize guinea pigs is the same as Anti ASIC1 Antibody ASC 014 raised in rabbit Our line of guinea pig antibodies enables more flexibility with our products such as multiplex staining studies immunoprecipitation etc
    https://www.bioz.com/result/guinea pig anti asic1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    guinea pig anti asic1 - by Bioz Stars, 2021-09
    93/100 stars

    Images

    1) Product Images from "Merkel Cell-Driven BDNF Signaling Specifies SAI Neuron Molecular and Electrophysiological Phenotypes"

    Article Title: Merkel Cell-Driven BDNF Signaling Specifies SAI Neuron Molecular and Electrophysiological Phenotypes

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.3781-15.2016

    Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, Asic1, and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p
    Figure Legend Snippet: Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, Asic1, and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Mouse Assay, Immunostaining

    2) Product Images from "Merkel Cell-Driven BDNF Signaling Specifies SAI Neuron Molecular and Electrophysiological Phenotypes"

    Article Title: Merkel Cell-Driven BDNF Signaling Specifies SAI Neuron Molecular and Electrophysiological Phenotypes

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.3781-15.2016

    Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, Asic1, and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p
    Figure Legend Snippet: Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, Asic1, and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Mouse Assay, Immunostaining

    3) Product Images from "ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway"

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms18102125

    Blockade of ASIC1a and Ca 2+ with PcTx1 and BAPTA-AM suppresses acid-induced articular chondrocytes autophagy. Rat articular chondrocytes were incubated with or without ASIC1a-specific blocker, PcTx1 (100 ng/mL) and calcium chelating agent, BAPTA-AM (10 μM) for 1 h, and then stimulated with extracellular acid (pH 6.0) for 3 h. ( A ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( B ) the autophagy markers, Beclin1 and LC3B-II protein expression were determined by Western blotting; ( C ) monodansylcadaverine (MDC) staining for acidic vacuoles was analyzed by fluorescence microscopy. Scale bar = 20 μm. Values were presented as mean ± SD of three separated experiments. ** p
    Figure Legend Snippet: Blockade of ASIC1a and Ca 2+ with PcTx1 and BAPTA-AM suppresses acid-induced articular chondrocytes autophagy. Rat articular chondrocytes were incubated with or without ASIC1a-specific blocker, PcTx1 (100 ng/mL) and calcium chelating agent, BAPTA-AM (10 μM) for 1 h, and then stimulated with extracellular acid (pH 6.0) for 3 h. ( A ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( B ) the autophagy markers, Beclin1 and LC3B-II protein expression were determined by Western blotting; ( C ) monodansylcadaverine (MDC) staining for acidic vacuoles was analyzed by fluorescence microscopy. Scale bar = 20 μm. Values were presented as mean ± SD of three separated experiments. ** p

    Techniques Used: Incubation, Isolation, Quantitative RT-PCR, Expressing, Western Blot, Staining, Fluorescence, Microscopy

    FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were incubated with extracellular acid (pH 6.0) for the indicated time periods. The protein expression of FoxO3a was assessed by Western blot; ( B ) nuclear and cytoplasmic FoxO3a proteins were isolated as described in materials and methods and expression level of FoxO3a in nuclear fraction was determined by Western blot analysis; histone H3 was used as normalized control in nuclear protein; ( C ) representative immunofluorescence analysis was performed on articular chondrocytes using anti-FoxO3a (green) antibody after acid treatment for 30 min. Nuclei were counterstained with DAPI (blue). Merge contains the combined image of FoxO3a immunostaining and DAPI staining. Scale bar = 100 μm. DAPI: 4′,6-diamidino-2-phenylindole, a fluorescent stain that binds strongly to A-T rich regions in DNA. ( D ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The FoxO3a protein expression was determined by Western blotting; ( E , F ) rat articular chondrocytes were transfected with siRNA targeting FoxO3a or scrambled control siRNA. After transfection, articular chondrocytes were treated with extracellular acid; ( E ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( F ) the protein expression of Beclin1, LC3B-II were determined by Western blot analysis; ( G ) rat articular chondrocytes were transfected with a mCherry-EGFP-LC3B plasmid and FoxO3a-siRNA or control-siRNA and then treated with extracellular acid, the GFP-LC3 puncta (green dots) and autophagosomes (yellow dots) and autolysosomes (red dots) were analyzed by fluorescence microscopy. Scale bar = 20 μm; ( H ) rat articular chondrocytes were transfected with FoxO3a-siRNA or control-siRNA and then treated with extracellular acid. The ultrastructure of the chondrocytes was imaged using transmission electron microscopy. N: nucleus; White arrows: autophagosomes. All images were shown at 20,000× magnification. Data were presented as mean ± SD of three independent experiments. * p
    Figure Legend Snippet: FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were incubated with extracellular acid (pH 6.0) for the indicated time periods. The protein expression of FoxO3a was assessed by Western blot; ( B ) nuclear and cytoplasmic FoxO3a proteins were isolated as described in materials and methods and expression level of FoxO3a in nuclear fraction was determined by Western blot analysis; histone H3 was used as normalized control in nuclear protein; ( C ) representative immunofluorescence analysis was performed on articular chondrocytes using anti-FoxO3a (green) antibody after acid treatment for 30 min. Nuclei were counterstained with DAPI (blue). Merge contains the combined image of FoxO3a immunostaining and DAPI staining. Scale bar = 100 μm. DAPI: 4′,6-diamidino-2-phenylindole, a fluorescent stain that binds strongly to A-T rich regions in DNA. ( D ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The FoxO3a protein expression was determined by Western blotting; ( E , F ) rat articular chondrocytes were transfected with siRNA targeting FoxO3a or scrambled control siRNA. After transfection, articular chondrocytes were treated with extracellular acid; ( E ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( F ) the protein expression of Beclin1, LC3B-II were determined by Western blot analysis; ( G ) rat articular chondrocytes were transfected with a mCherry-EGFP-LC3B plasmid and FoxO3a-siRNA or control-siRNA and then treated with extracellular acid, the GFP-LC3 puncta (green dots) and autophagosomes (yellow dots) and autolysosomes (red dots) were analyzed by fluorescence microscopy. Scale bar = 20 μm; ( H ) rat articular chondrocytes were transfected with FoxO3a-siRNA or control-siRNA and then treated with extracellular acid. The ultrastructure of the chondrocytes was imaged using transmission electron microscopy. N: nucleus; White arrows: autophagosomes. All images were shown at 20,000× magnification. Data were presented as mean ± SD of three independent experiments. * p

    Techniques Used: Incubation, Expressing, Western Blot, Isolation, Immunofluorescence, Immunostaining, Staining, Transfection, Quantitative RT-PCR, Plasmid Preparation, Fluorescence, Microscopy, Transmission Assay, Electron Microscopy

    AMPK/FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for the indicated time periods. Cells were then lysed to determine the expression level of phosphorylated AMPKα (Thr172) by Western blot analysis; ( B ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The level of p-AMPK/AMPK was determined by Western blotting; ( C ) rat articular chondrocytes were transfected with siRNA specific for AMPKα or scrambled control and then treated with extracellular acid (pH 6.0). After 30 min incubation, cells were then lysed to determine the expression level of FoxO3a by Western blot analysis; ( D ) rat articular chondrocytes transfected with siRNA for AMPKα or scrambled control were treated with extracellular acid. The levels of Beclin1, LC3B-II protein expression were determined by Western blot followed by densitometry analysis; ( E , F ) rat articular chondrocytes were pretreated with Compound C (10 µM) followed by treatment with extracellular acid (pH 6.0) for 30 min. The protein expression levels of total and nuclear FoxO3a were examined by Western blotting; ( G , H ) rat articular chondrocytes were incubated with or without 10 μM Compound C for 1 h and then stimulated with extracellular acid (pH 6.0) for 3 h. The mRNA and protein expression of Beclin1, LC3B-II were determined by qRT-PCR and Western blotting; ( I ) articular chondrocytes were transfected with EGFP-LC3 plasmid and then treated as for ( H ) followed by examining with fluorescence microscopy. Scale bar = 20 μm. GFP-LC3 puncta were quantified for each experiment, with at least 30 cells counted in each experiment. Data were presented as mean ± SD of three independent experiments. * p
    Figure Legend Snippet: AMPK/FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for the indicated time periods. Cells were then lysed to determine the expression level of phosphorylated AMPKα (Thr172) by Western blot analysis; ( B ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The level of p-AMPK/AMPK was determined by Western blotting; ( C ) rat articular chondrocytes were transfected with siRNA specific for AMPKα or scrambled control and then treated with extracellular acid (pH 6.0). After 30 min incubation, cells were then lysed to determine the expression level of FoxO3a by Western blot analysis; ( D ) rat articular chondrocytes transfected with siRNA for AMPKα or scrambled control were treated with extracellular acid. The levels of Beclin1, LC3B-II protein expression were determined by Western blot followed by densitometry analysis; ( E , F ) rat articular chondrocytes were pretreated with Compound C (10 µM) followed by treatment with extracellular acid (pH 6.0) for 30 min. The protein expression levels of total and nuclear FoxO3a were examined by Western blotting; ( G , H ) rat articular chondrocytes were incubated with or without 10 μM Compound C for 1 h and then stimulated with extracellular acid (pH 6.0) for 3 h. The mRNA and protein expression of Beclin1, LC3B-II were determined by qRT-PCR and Western blotting; ( I ) articular chondrocytes were transfected with EGFP-LC3 plasmid and then treated as for ( H ) followed by examining with fluorescence microscopy. Scale bar = 20 μm. GFP-LC3 puncta were quantified for each experiment, with at least 30 cells counted in each experiment. Data were presented as mean ± SD of three independent experiments. * p

    Techniques Used: Expressing, Western Blot, Transfection, Incubation, Quantitative RT-PCR, Plasmid Preparation, Fluorescence, Microscopy

    Blockade of ASIC1a with PcTx1 reduces acid-induced elevation of (Ca 2+ ) i level in articular chondrocytes. Cellular confocal micrographs of the same scale showing the changes in the (Ca 2+ ) i concentration, as visualized by Fluo-3-AM in articular chondrocytes. ( A , a ) acid-induced increase of (Ca 2+ ) i in Ca 2+ -free extracellular solution; ( B , b ) acid-induced increase of (Ca 2+ ) i in extracellular Ca 2+ solution; ( C , c ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with ASIC1a-specific blocker, PcTx1; ( D , d ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with calcium chelating agent, BAPTA-AM. The amplitude of (Ca 2+ ) i intensity in articular chondrocytes induced by acid treatment was quantified as the maximal rise of (Ca 2+ ) i above basal levels. ( i ) before exposure to acid solution; ( ii ) increased Ca 2+ intensity when pH was decreased to 6.0; ( iii ) after exposure to the acid solution for three minutes ( n = 8 for each).
    Figure Legend Snippet: Blockade of ASIC1a with PcTx1 reduces acid-induced elevation of (Ca 2+ ) i level in articular chondrocytes. Cellular confocal micrographs of the same scale showing the changes in the (Ca 2+ ) i concentration, as visualized by Fluo-3-AM in articular chondrocytes. ( A , a ) acid-induced increase of (Ca 2+ ) i in Ca 2+ -free extracellular solution; ( B , b ) acid-induced increase of (Ca 2+ ) i in extracellular Ca 2+ solution; ( C , c ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with ASIC1a-specific blocker, PcTx1; ( D , d ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with calcium chelating agent, BAPTA-AM. The amplitude of (Ca 2+ ) i intensity in articular chondrocytes induced by acid treatment was quantified as the maximal rise of (Ca 2+ ) i above basal levels. ( i ) before exposure to acid solution; ( ii ) increased Ca 2+ intensity when pH was decreased to 6.0; ( iii ) after exposure to the acid solution for three minutes ( n = 8 for each).

    Techniques Used: Concentration Assay

    Expression of acid-sensing ion channel 1a (ASIC1a) on rat articular chondrocytes. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for different time periods. Cells were then lysed to determine the expression level of ASIC1a by Western blot analysis. Values are presented as mean ± SD of three independent experiments. ** p
    Figure Legend Snippet: Expression of acid-sensing ion channel 1a (ASIC1a) on rat articular chondrocytes. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for different time periods. Cells were then lysed to determine the expression level of ASIC1a by Western blot analysis. Values are presented as mean ± SD of three independent experiments. ** p

    Techniques Used: Expressing, Western Blot

    Proposed model for the role of AMPK/FoxO3a signaling in the ASIC1a-mediated autophagy in rat articular chondrocytes.
    Figure Legend Snippet: Proposed model for the role of AMPK/FoxO3a signaling in the ASIC1a-mediated autophagy in rat articular chondrocytes.

    Techniques Used:

    4) Product Images from "Acid-Sensitive Ion Channels Are Expressed in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes"

    Article Title: Acid-Sensitive Ion Channels Are Expressed in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes

    Journal: Stem Cells and Development

    doi: 10.1089/scd.2018.0234

    mRNA expression of ASIC family in hiPSC differentiated cardiomyocytes. (A) Expression of ASIC1 and ASIC2 transcripts in human iPSC-derived cardiac clusters (IMR-90 line) and control cell lines. Beating hiPSC-derived cardiac clusters were collected on days 30 and 100 of differentiation using END2 protocol. hASIC1 mRNA was detected in undifferentiated hiPSCs and hiPSC-CMs (day 30), but was very low in day 100 hiPSC-CM. hiPSC-derived NPCs and hiPSC-NPC-derived neurons were used as positive controls. Human ASIC2 transcripts were detected only in hiPSC-NPC-derived neurons but not in any stage of hiPSC-CMs. (B) ASIC1a , ASIC2a , and ASIC2b section) in 55 days old hiPSC-CMs derived from iPSC-K3 line. (C, D) Quantitative polymerase chain reaction data confirmed the expression of ASIC1a , ASIC2a , and ASIC3 mRNA in hiPSC-CMs derived from both K3 and IMR-90 iPSC lines, n = 3 and n = 4, respectively. The ** p
    Figure Legend Snippet: mRNA expression of ASIC family in hiPSC differentiated cardiomyocytes. (A) Expression of ASIC1 and ASIC2 transcripts in human iPSC-derived cardiac clusters (IMR-90 line) and control cell lines. Beating hiPSC-derived cardiac clusters were collected on days 30 and 100 of differentiation using END2 protocol. hASIC1 mRNA was detected in undifferentiated hiPSCs and hiPSC-CMs (day 30), but was very low in day 100 hiPSC-CM. hiPSC-derived NPCs and hiPSC-NPC-derived neurons were used as positive controls. Human ASIC2 transcripts were detected only in hiPSC-NPC-derived neurons but not in any stage of hiPSC-CMs. (B) ASIC1a , ASIC2a , and ASIC2b section) in 55 days old hiPSC-CMs derived from iPSC-K3 line. (C, D) Quantitative polymerase chain reaction data confirmed the expression of ASIC1a , ASIC2a , and ASIC3 mRNA in hiPSC-CMs derived from both K3 and IMR-90 iPSC lines, n = 3 and n = 4, respectively. The ** p

    Techniques Used: Expressing, Derivative Assay, Real-time Polymerase Chain Reaction

    Assessment of ASIC1 expression in human iPSC-CMs using immunocytochemistry. Representative immunofluorescence panels show colocalization of ASIC1 ( red ) with the cardiomyocyte marker a-actinin ( green ) in human iPSC-derived cardiomyocytes both at day 20 and at day 62 of directed differentiation. The neuroblastoma SH-SY5Y cells were used as positive control and exhibit more intense ASIC1 signal than CMs. Cells incubated only with fluorescently labeled secondary antibodies did not produce any specific signals. Nuclei were counterstained with DAPI ( blue ). CMs were differentiated from NP0040 iPSC line. Scale bars: 50 μm. Color images are available online.
    Figure Legend Snippet: Assessment of ASIC1 expression in human iPSC-CMs using immunocytochemistry. Representative immunofluorescence panels show colocalization of ASIC1 ( red ) with the cardiomyocyte marker a-actinin ( green ) in human iPSC-derived cardiomyocytes both at day 20 and at day 62 of directed differentiation. The neuroblastoma SH-SY5Y cells were used as positive control and exhibit more intense ASIC1 signal than CMs. Cells incubated only with fluorescently labeled secondary antibodies did not produce any specific signals. Nuclei were counterstained with DAPI ( blue ). CMs were differentiated from NP0040 iPSC line. Scale bars: 50 μm. Color images are available online.

    Techniques Used: Expressing, Immunocytochemistry, Immunofluorescence, Marker, Derivative Assay, Positive Control, Incubation, Labeling

    Immunohistochemical detection of ASIC1 in adult rat brain and heart tissue cryoslices. Representative immunofluorescence panels show colocalization of ASIC1 with the neuronal marker microtubule-associated protein 2 (Map2) in the adult rat brain but no ASIC1 expression in the adult rat heart muscle cells, which stained positive for the cardiomyocyte marker sarcomeric α-actinin (Actn2). Tissue specimens incubated only with fluorescently labeled secondary antibodies gave no specific signals. Nuclei were counterstained with Hoechst 33342. Scale bars: 100 μm. Color images are available online.
    Figure Legend Snippet: Immunohistochemical detection of ASIC1 in adult rat brain and heart tissue cryoslices. Representative immunofluorescence panels show colocalization of ASIC1 with the neuronal marker microtubule-associated protein 2 (Map2) in the adult rat brain but no ASIC1 expression in the adult rat heart muscle cells, which stained positive for the cardiomyocyte marker sarcomeric α-actinin (Actn2). Tissue specimens incubated only with fluorescently labeled secondary antibodies gave no specific signals. Nuclei were counterstained with Hoechst 33342. Scale bars: 100 μm. Color images are available online.

    Techniques Used: Immunohistochemistry, Immunofluorescence, Marker, Expressing, Staining, Incubation, Labeling

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  • 93
    Alomone Labs guinea pig anti asic1
    Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, <t>Asic1,</t> and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p
    Guinea Pig Anti Asic1, 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/guinea pig anti asic1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    guinea pig anti asic1 - by Bioz Stars, 2021-09
    93/100 stars
      Buy from Supplier

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    Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, Asic1, and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p

    Journal: The Journal of Neuroscience

    Article Title: Merkel Cell-Driven BDNF Signaling Specifies SAI Neuron Molecular and Electrophysiological Phenotypes

    doi: 10.1523/JNEUROSCI.3781-15.2016

    Figure Lengend Snippet: Merkel cell deletion alters the expression of SAI ion channel components. A , qPCR analysis of ion channels in P21 thoracic DRGs ( n ≥ 8 mice/genotype at each age). B–G , Immunostaining for NF200, γENaC, Asic1, and DOR in T7 DRG sections from P21 control littermate and K14; Atoh1 CKO mice. Asterisks indicate double-positive cells. H , Percentages of Islet1/2 + T7 DRG neurons that were NF200 + γENaC + , NF200 + Asic1, and NF200 + DOR + in P21 control and K14; Atoh1 CKO mice ( n ≥ 3 mice/genotype). Error bars in graphs represent the SEM, and asterisks indicate statistically significant differences between genotypes. * p

    Article Snippet: The primary antibodies used were mouse anti-Islet1/2 (1:50; catalog #39.4D5, Developmental Studies Hybridoma Bank), rabbit anti-NF200 (1:1000; N4142, Sigma-Aldrich), goat anti-TrkB (1:200; AF1494, R & D Systems), goat anti-TrkC [AF1404 (1:100) and BAF1404 (1:20), R & D Systems], rabbit anti-Ret (1:50; catalog #18121, Immuno-Biological Laboratories), rabbit anti-parvalbumin (PV; 1:1000; PV25, Swant), rabbit anti-CGRP (1:1000; T-4032, Peninsula Laboratories), rabbit anti-phospho-SMAD1/5/8 (1:250; catalog 9511, Cell Signaling Technology), goat anti-TBX3 (1:100; sc-31656, Santa Cruz Biotechnology), rat anti-Keratin8 (1:20, TROMA-1, Developmental Studies Hybridoma Bank), guinea pig anti-Asic1 (1:250; Alomone Labs), rabbit anti-δ opioid receptor (DOR; 1:500; Alomone Labs), and rabbit anti-γENaC (1:500; StressMarq Biosciences).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Mouse Assay, Immunostaining

    Blockade of ASIC1a and Ca 2+ with PcTx1 and BAPTA-AM suppresses acid-induced articular chondrocytes autophagy. Rat articular chondrocytes were incubated with or without ASIC1a-specific blocker, PcTx1 (100 ng/mL) and calcium chelating agent, BAPTA-AM (10 μM) for 1 h, and then stimulated with extracellular acid (pH 6.0) for 3 h. ( A ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( B ) the autophagy markers, Beclin1 and LC3B-II protein expression were determined by Western blotting; ( C ) monodansylcadaverine (MDC) staining for acidic vacuoles was analyzed by fluorescence microscopy. Scale bar = 20 μm. Values were presented as mean ± SD of three separated experiments. ** p

    Journal: International Journal of Molecular Sciences

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    doi: 10.3390/ijms18102125

    Figure Lengend Snippet: Blockade of ASIC1a and Ca 2+ with PcTx1 and BAPTA-AM suppresses acid-induced articular chondrocytes autophagy. Rat articular chondrocytes were incubated with or without ASIC1a-specific blocker, PcTx1 (100 ng/mL) and calcium chelating agent, BAPTA-AM (10 μM) for 1 h, and then stimulated with extracellular acid (pH 6.0) for 3 h. ( A ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( B ) the autophagy markers, Beclin1 and LC3B-II protein expression were determined by Western blotting; ( C ) monodansylcadaverine (MDC) staining for acidic vacuoles was analyzed by fluorescence microscopy. Scale bar = 20 μm. Values were presented as mean ± SD of three separated experiments. ** p

    Article Snippet: Guinea pig polyclonal anti-ASIC1a (Alomone Labs, Jerusalem, Israel) was applied at a dilution of 1:600, rabbit monoclonal antibodies against LC3B, Beclin1, FoxO3a, AMPKα, phospho-AMPKα (Cell Signaling Technology, Danvers, MA, USA) were used at dilution of 1:1000, mouse monoclonal anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used at a dilution of 1:500.

    Techniques: Incubation, Isolation, Quantitative RT-PCR, Expressing, Western Blot, Staining, Fluorescence, Microscopy

    FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were incubated with extracellular acid (pH 6.0) for the indicated time periods. The protein expression of FoxO3a was assessed by Western blot; ( B ) nuclear and cytoplasmic FoxO3a proteins were isolated as described in materials and methods and expression level of FoxO3a in nuclear fraction was determined by Western blot analysis; histone H3 was used as normalized control in nuclear protein; ( C ) representative immunofluorescence analysis was performed on articular chondrocytes using anti-FoxO3a (green) antibody after acid treatment for 30 min. Nuclei were counterstained with DAPI (blue). Merge contains the combined image of FoxO3a immunostaining and DAPI staining. Scale bar = 100 μm. DAPI: 4′,6-diamidino-2-phenylindole, a fluorescent stain that binds strongly to A-T rich regions in DNA. ( D ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The FoxO3a protein expression was determined by Western blotting; ( E , F ) rat articular chondrocytes were transfected with siRNA targeting FoxO3a or scrambled control siRNA. After transfection, articular chondrocytes were treated with extracellular acid; ( E ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( F ) the protein expression of Beclin1, LC3B-II were determined by Western blot analysis; ( G ) rat articular chondrocytes were transfected with a mCherry-EGFP-LC3B plasmid and FoxO3a-siRNA or control-siRNA and then treated with extracellular acid, the GFP-LC3 puncta (green dots) and autophagosomes (yellow dots) and autolysosomes (red dots) were analyzed by fluorescence microscopy. Scale bar = 20 μm; ( H ) rat articular chondrocytes were transfected with FoxO3a-siRNA or control-siRNA and then treated with extracellular acid. The ultrastructure of the chondrocytes was imaged using transmission electron microscopy. N: nucleus; White arrows: autophagosomes. All images were shown at 20,000× magnification. Data were presented as mean ± SD of three independent experiments. * p

    Journal: International Journal of Molecular Sciences

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    doi: 10.3390/ijms18102125

    Figure Lengend Snippet: FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were incubated with extracellular acid (pH 6.0) for the indicated time periods. The protein expression of FoxO3a was assessed by Western blot; ( B ) nuclear and cytoplasmic FoxO3a proteins were isolated as described in materials and methods and expression level of FoxO3a in nuclear fraction was determined by Western blot analysis; histone H3 was used as normalized control in nuclear protein; ( C ) representative immunofluorescence analysis was performed on articular chondrocytes using anti-FoxO3a (green) antibody after acid treatment for 30 min. Nuclei were counterstained with DAPI (blue). Merge contains the combined image of FoxO3a immunostaining and DAPI staining. Scale bar = 100 μm. DAPI: 4′,6-diamidino-2-phenylindole, a fluorescent stain that binds strongly to A-T rich regions in DNA. ( D ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The FoxO3a protein expression was determined by Western blotting; ( E , F ) rat articular chondrocytes were transfected with siRNA targeting FoxO3a or scrambled control siRNA. After transfection, articular chondrocytes were treated with extracellular acid; ( E ) mRNAs were isolated from articular chondrocytes and qRT-PCR was performed; ( F ) the protein expression of Beclin1, LC3B-II were determined by Western blot analysis; ( G ) rat articular chondrocytes were transfected with a mCherry-EGFP-LC3B plasmid and FoxO3a-siRNA or control-siRNA and then treated with extracellular acid, the GFP-LC3 puncta (green dots) and autophagosomes (yellow dots) and autolysosomes (red dots) were analyzed by fluorescence microscopy. Scale bar = 20 μm; ( H ) rat articular chondrocytes were transfected with FoxO3a-siRNA or control-siRNA and then treated with extracellular acid. The ultrastructure of the chondrocytes was imaged using transmission electron microscopy. N: nucleus; White arrows: autophagosomes. All images were shown at 20,000× magnification. Data were presented as mean ± SD of three independent experiments. * p

    Article Snippet: Guinea pig polyclonal anti-ASIC1a (Alomone Labs, Jerusalem, Israel) was applied at a dilution of 1:600, rabbit monoclonal antibodies against LC3B, Beclin1, FoxO3a, AMPKα, phospho-AMPKα (Cell Signaling Technology, Danvers, MA, USA) were used at dilution of 1:1000, mouse monoclonal anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used at a dilution of 1:500.

    Techniques: Incubation, Expressing, Western Blot, Isolation, Immunofluorescence, Immunostaining, Staining, Transfection, Quantitative RT-PCR, Plasmid Preparation, Fluorescence, Microscopy, Transmission Assay, Electron Microscopy

    AMPK/FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for the indicated time periods. Cells were then lysed to determine the expression level of phosphorylated AMPKα (Thr172) by Western blot analysis; ( B ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The level of p-AMPK/AMPK was determined by Western blotting; ( C ) rat articular chondrocytes were transfected with siRNA specific for AMPKα or scrambled control and then treated with extracellular acid (pH 6.0). After 30 min incubation, cells were then lysed to determine the expression level of FoxO3a by Western blot analysis; ( D ) rat articular chondrocytes transfected with siRNA for AMPKα or scrambled control were treated with extracellular acid. The levels of Beclin1, LC3B-II protein expression were determined by Western blot followed by densitometry analysis; ( E , F ) rat articular chondrocytes were pretreated with Compound C (10 µM) followed by treatment with extracellular acid (pH 6.0) for 30 min. The protein expression levels of total and nuclear FoxO3a were examined by Western blotting; ( G , H ) rat articular chondrocytes were incubated with or without 10 μM Compound C for 1 h and then stimulated with extracellular acid (pH 6.0) for 3 h. The mRNA and protein expression of Beclin1, LC3B-II were determined by qRT-PCR and Western blotting; ( I ) articular chondrocytes were transfected with EGFP-LC3 plasmid and then treated as for ( H ) followed by examining with fluorescence microscopy. Scale bar = 20 μm. GFP-LC3 puncta were quantified for each experiment, with at least 30 cells counted in each experiment. Data were presented as mean ± SD of three independent experiments. * p

    Journal: International Journal of Molecular Sciences

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    doi: 10.3390/ijms18102125

    Figure Lengend Snippet: AMPK/FoxO3a signaling is involved in ASIC1a-mediated articular chondrocytes autophagy. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for the indicated time periods. Cells were then lysed to determine the expression level of phosphorylated AMPKα (Thr172) by Western blot analysis; ( B ) pretreatment with ASIC1a-specific blocker, PcTx1 and calcium chelating agent, BAPTA-AM for 1 h, articular chondrocytes were stimulated with extracellular acid (pH 6.0) for 30 min. The level of p-AMPK/AMPK was determined by Western blotting; ( C ) rat articular chondrocytes were transfected with siRNA specific for AMPKα or scrambled control and then treated with extracellular acid (pH 6.0). After 30 min incubation, cells were then lysed to determine the expression level of FoxO3a by Western blot analysis; ( D ) rat articular chondrocytes transfected with siRNA for AMPKα or scrambled control were treated with extracellular acid. The levels of Beclin1, LC3B-II protein expression were determined by Western blot followed by densitometry analysis; ( E , F ) rat articular chondrocytes were pretreated with Compound C (10 µM) followed by treatment with extracellular acid (pH 6.0) for 30 min. The protein expression levels of total and nuclear FoxO3a were examined by Western blotting; ( G , H ) rat articular chondrocytes were incubated with or without 10 μM Compound C for 1 h and then stimulated with extracellular acid (pH 6.0) for 3 h. The mRNA and protein expression of Beclin1, LC3B-II were determined by qRT-PCR and Western blotting; ( I ) articular chondrocytes were transfected with EGFP-LC3 plasmid and then treated as for ( H ) followed by examining with fluorescence microscopy. Scale bar = 20 μm. GFP-LC3 puncta were quantified for each experiment, with at least 30 cells counted in each experiment. Data were presented as mean ± SD of three independent experiments. * p

    Article Snippet: Guinea pig polyclonal anti-ASIC1a (Alomone Labs, Jerusalem, Israel) was applied at a dilution of 1:600, rabbit monoclonal antibodies against LC3B, Beclin1, FoxO3a, AMPKα, phospho-AMPKα (Cell Signaling Technology, Danvers, MA, USA) were used at dilution of 1:1000, mouse monoclonal anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used at a dilution of 1:500.

    Techniques: Expressing, Western Blot, Transfection, Incubation, Quantitative RT-PCR, Plasmid Preparation, Fluorescence, Microscopy

    Blockade of ASIC1a with PcTx1 reduces acid-induced elevation of (Ca 2+ ) i level in articular chondrocytes. Cellular confocal micrographs of the same scale showing the changes in the (Ca 2+ ) i concentration, as visualized by Fluo-3-AM in articular chondrocytes. ( A , a ) acid-induced increase of (Ca 2+ ) i in Ca 2+ -free extracellular solution; ( B , b ) acid-induced increase of (Ca 2+ ) i in extracellular Ca 2+ solution; ( C , c ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with ASIC1a-specific blocker, PcTx1; ( D , d ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with calcium chelating agent, BAPTA-AM. The amplitude of (Ca 2+ ) i intensity in articular chondrocytes induced by acid treatment was quantified as the maximal rise of (Ca 2+ ) i above basal levels. ( i ) before exposure to acid solution; ( ii ) increased Ca 2+ intensity when pH was decreased to 6.0; ( iii ) after exposure to the acid solution for three minutes ( n = 8 for each).

    Journal: International Journal of Molecular Sciences

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    doi: 10.3390/ijms18102125

    Figure Lengend Snippet: Blockade of ASIC1a with PcTx1 reduces acid-induced elevation of (Ca 2+ ) i level in articular chondrocytes. Cellular confocal micrographs of the same scale showing the changes in the (Ca 2+ ) i concentration, as visualized by Fluo-3-AM in articular chondrocytes. ( A , a ) acid-induced increase of (Ca 2+ ) i in Ca 2+ -free extracellular solution; ( B , b ) acid-induced increase of (Ca 2+ ) i in extracellular Ca 2+ solution; ( C , c ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with ASIC1a-specific blocker, PcTx1; ( D , d ) acid-induced increase of (Ca 2+ ) i in articular chondrocytes pretreated with calcium chelating agent, BAPTA-AM. The amplitude of (Ca 2+ ) i intensity in articular chondrocytes induced by acid treatment was quantified as the maximal rise of (Ca 2+ ) i above basal levels. ( i ) before exposure to acid solution; ( ii ) increased Ca 2+ intensity when pH was decreased to 6.0; ( iii ) after exposure to the acid solution for three minutes ( n = 8 for each).

    Article Snippet: Guinea pig polyclonal anti-ASIC1a (Alomone Labs, Jerusalem, Israel) was applied at a dilution of 1:600, rabbit monoclonal antibodies against LC3B, Beclin1, FoxO3a, AMPKα, phospho-AMPKα (Cell Signaling Technology, Danvers, MA, USA) were used at dilution of 1:1000, mouse monoclonal anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used at a dilution of 1:500.

    Techniques: Concentration Assay

    Expression of acid-sensing ion channel 1a (ASIC1a) on rat articular chondrocytes. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for different time periods. Cells were then lysed to determine the expression level of ASIC1a by Western blot analysis. Values are presented as mean ± SD of three independent experiments. ** p

    Journal: International Journal of Molecular Sciences

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    doi: 10.3390/ijms18102125

    Figure Lengend Snippet: Expression of acid-sensing ion channel 1a (ASIC1a) on rat articular chondrocytes. ( A ) rat articular chondrocytes were treated with extracellular acid (pH 6.0) for different time periods. Cells were then lysed to determine the expression level of ASIC1a by Western blot analysis. Values are presented as mean ± SD of three independent experiments. ** p

    Article Snippet: Guinea pig polyclonal anti-ASIC1a (Alomone Labs, Jerusalem, Israel) was applied at a dilution of 1:600, rabbit monoclonal antibodies against LC3B, Beclin1, FoxO3a, AMPKα, phospho-AMPKα (Cell Signaling Technology, Danvers, MA, USA) were used at dilution of 1:1000, mouse monoclonal anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used at a dilution of 1:500.

    Techniques: Expressing, Western Blot

    Proposed model for the role of AMPK/FoxO3a signaling in the ASIC1a-mediated autophagy in rat articular chondrocytes.

    Journal: International Journal of Molecular Sciences

    Article Title: ASIC1a Promotes Acid-Induced Autophagy in Rat Articular Chondrocytes through the AMPK/FoxO3a Pathway

    doi: 10.3390/ijms18102125

    Figure Lengend Snippet: Proposed model for the role of AMPK/FoxO3a signaling in the ASIC1a-mediated autophagy in rat articular chondrocytes.

    Article Snippet: Guinea pig polyclonal anti-ASIC1a (Alomone Labs, Jerusalem, Israel) was applied at a dilution of 1:600, rabbit monoclonal antibodies against LC3B, Beclin1, FoxO3a, AMPKα, phospho-AMPKα (Cell Signaling Technology, Danvers, MA, USA) were used at dilution of 1:1000, mouse monoclonal anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used at a dilution of 1:500.

    Techniques:

    mRNA expression of ASIC family in hiPSC differentiated cardiomyocytes. (A) Expression of ASIC1 and ASIC2 transcripts in human iPSC-derived cardiac clusters (IMR-90 line) and control cell lines. Beating hiPSC-derived cardiac clusters were collected on days 30 and 100 of differentiation using END2 protocol. hASIC1 mRNA was detected in undifferentiated hiPSCs and hiPSC-CMs (day 30), but was very low in day 100 hiPSC-CM. hiPSC-derived NPCs and hiPSC-NPC-derived neurons were used as positive controls. Human ASIC2 transcripts were detected only in hiPSC-NPC-derived neurons but not in any stage of hiPSC-CMs. (B) ASIC1a , ASIC2a , and ASIC2b section) in 55 days old hiPSC-CMs derived from iPSC-K3 line. (C, D) Quantitative polymerase chain reaction data confirmed the expression of ASIC1a , ASIC2a , and ASIC3 mRNA in hiPSC-CMs derived from both K3 and IMR-90 iPSC lines, n = 3 and n = 4, respectively. The ** p

    Journal: Stem Cells and Development

    Article Title: Acid-Sensitive Ion Channels Are Expressed in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes

    doi: 10.1089/scd.2018.0234

    Figure Lengend Snippet: mRNA expression of ASIC family in hiPSC differentiated cardiomyocytes. (A) Expression of ASIC1 and ASIC2 transcripts in human iPSC-derived cardiac clusters (IMR-90 line) and control cell lines. Beating hiPSC-derived cardiac clusters were collected on days 30 and 100 of differentiation using END2 protocol. hASIC1 mRNA was detected in undifferentiated hiPSCs and hiPSC-CMs (day 30), but was very low in day 100 hiPSC-CM. hiPSC-derived NPCs and hiPSC-NPC-derived neurons were used as positive controls. Human ASIC2 transcripts were detected only in hiPSC-NPC-derived neurons but not in any stage of hiPSC-CMs. (B) ASIC1a , ASIC2a , and ASIC2b section) in 55 days old hiPSC-CMs derived from iPSC-K3 line. (C, D) Quantitative polymerase chain reaction data confirmed the expression of ASIC1a , ASIC2a , and ASIC3 mRNA in hiPSC-CMs derived from both K3 and IMR-90 iPSC lines, n = 3 and n = 4, respectively. The ** p

    Article Snippet: The following primary antibodies were used: guinea pig polyclonal anti-ASIC1 (1:200, Cat. No. AGP-053; Alomone Labs), mouse monoclonal anti-α-actinin (1:800, Cat. No. A-7811, Clone: EA-53; Sigma), and rabbit polyclonal anti-MAP2 (1:200, Cat. No. ab32454; Abcam).

    Techniques: Expressing, Derivative Assay, Real-time Polymerase Chain Reaction

    Assessment of ASIC1 expression in human iPSC-CMs using immunocytochemistry. Representative immunofluorescence panels show colocalization of ASIC1 ( red ) with the cardiomyocyte marker a-actinin ( green ) in human iPSC-derived cardiomyocytes both at day 20 and at day 62 of directed differentiation. The neuroblastoma SH-SY5Y cells were used as positive control and exhibit more intense ASIC1 signal than CMs. Cells incubated only with fluorescently labeled secondary antibodies did not produce any specific signals. Nuclei were counterstained with DAPI ( blue ). CMs were differentiated from NP0040 iPSC line. Scale bars: 50 μm. Color images are available online.

    Journal: Stem Cells and Development

    Article Title: Acid-Sensitive Ion Channels Are Expressed in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes

    doi: 10.1089/scd.2018.0234

    Figure Lengend Snippet: Assessment of ASIC1 expression in human iPSC-CMs using immunocytochemistry. Representative immunofluorescence panels show colocalization of ASIC1 ( red ) with the cardiomyocyte marker a-actinin ( green ) in human iPSC-derived cardiomyocytes both at day 20 and at day 62 of directed differentiation. The neuroblastoma SH-SY5Y cells were used as positive control and exhibit more intense ASIC1 signal than CMs. Cells incubated only with fluorescently labeled secondary antibodies did not produce any specific signals. Nuclei were counterstained with DAPI ( blue ). CMs were differentiated from NP0040 iPSC line. Scale bars: 50 μm. Color images are available online.

    Article Snippet: The following primary antibodies were used: guinea pig polyclonal anti-ASIC1 (1:200, Cat. No. AGP-053; Alomone Labs), mouse monoclonal anti-α-actinin (1:800, Cat. No. A-7811, Clone: EA-53; Sigma), and rabbit polyclonal anti-MAP2 (1:200, Cat. No. ab32454; Abcam).

    Techniques: Expressing, Immunocytochemistry, Immunofluorescence, Marker, Derivative Assay, Positive Control, Incubation, Labeling

    Immunohistochemical detection of ASIC1 in adult rat brain and heart tissue cryoslices. Representative immunofluorescence panels show colocalization of ASIC1 with the neuronal marker microtubule-associated protein 2 (Map2) in the adult rat brain but no ASIC1 expression in the adult rat heart muscle cells, which stained positive for the cardiomyocyte marker sarcomeric α-actinin (Actn2). Tissue specimens incubated only with fluorescently labeled secondary antibodies gave no specific signals. Nuclei were counterstained with Hoechst 33342. Scale bars: 100 μm. Color images are available online.

    Journal: Stem Cells and Development

    Article Title: Acid-Sensitive Ion Channels Are Expressed in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes

    doi: 10.1089/scd.2018.0234

    Figure Lengend Snippet: Immunohistochemical detection of ASIC1 in adult rat brain and heart tissue cryoslices. Representative immunofluorescence panels show colocalization of ASIC1 with the neuronal marker microtubule-associated protein 2 (Map2) in the adult rat brain but no ASIC1 expression in the adult rat heart muscle cells, which stained positive for the cardiomyocyte marker sarcomeric α-actinin (Actn2). Tissue specimens incubated only with fluorescently labeled secondary antibodies gave no specific signals. Nuclei were counterstained with Hoechst 33342. Scale bars: 100 μm. Color images are available online.

    Article Snippet: The following primary antibodies were used: guinea pig polyclonal anti-ASIC1 (1:200, Cat. No. AGP-053; Alomone Labs), mouse monoclonal anti-α-actinin (1:800, Cat. No. A-7811, Clone: EA-53; Sigma), and rabbit polyclonal anti-MAP2 (1:200, Cat. No. ab32454; Abcam).

    Techniques: Immunohistochemistry, Immunofluorescence, Marker, Expressing, Staining, Incubation, Labeling