hcn1  (Alomone Labs)


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    Structured Review

    Alomone Labs hcn1
    HCN immunoreactivity in club endings of myelinated fibers accompanied by fine unmyelinated fibers. Left, <t>HCN1</t> (FITC) colocalized (yellow) with peripherin (Rhodamine Red-X) in a club ending but not with fine unmyelinated fiber (arrowhead). Center, HCN2 (Rhodamine Red-X) appeared in both the fine unmyelinated fibers and in a club ending of a myelinated fiber (yellow). Right, Both club endings and fine fibers (arrowhead) labeled with FITC-NF mixture also expressed HCN4 (Rhodamine Red-X). HCN2 and HCN4 (Rhodamine Red-X) are also found in cells surrounding the fibers.
    Hcn1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hcn1/product/Alomone Labs
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hcn1 - by Bioz Stars, 2022-06
    90/100 stars

    Images

    1) Product Images from "Differential Distribution and Function of Hyperpolarization-Activated Channels in Sensory Neurons and Mechanosensitive Fibers"

    Article Title: Differential Distribution and Function of Hyperpolarization-Activated Channels in Sensory Neurons and Mechanosensitive Fibers

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.5156-03.2004

    HCN immunoreactivity in club endings of myelinated fibers accompanied by fine unmyelinated fibers. Left, HCN1 (FITC) colocalized (yellow) with peripherin (Rhodamine Red-X) in a club ending but not with fine unmyelinated fiber (arrowhead). Center, HCN2 (Rhodamine Red-X) appeared in both the fine unmyelinated fibers and in a club ending of a myelinated fiber (yellow). Right, Both club endings and fine fibers (arrowhead) labeled with FITC-NF mixture also expressed HCN4 (Rhodamine Red-X). HCN2 and HCN4 (Rhodamine Red-X) are also found in cells surrounding the fibers.
    Figure Legend Snippet: HCN immunoreactivity in club endings of myelinated fibers accompanied by fine unmyelinated fibers. Left, HCN1 (FITC) colocalized (yellow) with peripherin (Rhodamine Red-X) in a club ending but not with fine unmyelinated fiber (arrowhead). Center, HCN2 (Rhodamine Red-X) appeared in both the fine unmyelinated fibers and in a club ending of a myelinated fiber (yellow). Right, Both club endings and fine fibers (arrowhead) labeled with FITC-NF mixture also expressed HCN4 (Rhodamine Red-X). HCN2 and HCN4 (Rhodamine Red-X) are also found in cells surrounding the fibers.

    Techniques Used: Labeling

    HCN1, HCN2, and HCN4 immunoreactivity in nodose neurons. A–C , HCN immunoreactivity identified in 6–10 μm sections of nodose ganglion. HCN1 immunoreactivity was localized to a small subpopulation of neurons and, in most of these cells, was heavily localized at the plasma membrane ( A ). HCN2 ( B ) and HCN4 ( C ) immunoreactivity was present in all neurons in the ganglion. D–F , Single confocal sections through cultured nodose neurons selected for expression of HCN1 ( D ), HCN2 ( E ), and HCN4 ( F ). Heavy labeling at the membrane is again shown for HCN1 ( D ). Patches of HCN2 and HCN4 immunoreactivity were located at the cell perimeter; examples are indicated by the arrows ( E, F ). The light microscopic differential interference contrast image is also shown for each neuron. The calibration bar in C also applies to A and B , whereas calibration in F applies to E . The antibodies were preabsorbed with the immunizing peptide as shown in the figure. A control for nonspecific staining omitted the primary Ab (data not shown).
    Figure Legend Snippet: HCN1, HCN2, and HCN4 immunoreactivity in nodose neurons. A–C , HCN immunoreactivity identified in 6–10 μm sections of nodose ganglion. HCN1 immunoreactivity was localized to a small subpopulation of neurons and, in most of these cells, was heavily localized at the plasma membrane ( A ). HCN2 ( B ) and HCN4 ( C ) immunoreactivity was present in all neurons in the ganglion. D–F , Single confocal sections through cultured nodose neurons selected for expression of HCN1 ( D ), HCN2 ( E ), and HCN4 ( F ). Heavy labeling at the membrane is again shown for HCN1 ( D ). Patches of HCN2 and HCN4 immunoreactivity were located at the cell perimeter; examples are indicated by the arrows ( E, F ). The light microscopic differential interference contrast image is also shown for each neuron. The calibration bar in C also applies to A and B , whereas calibration in F applies to E . The antibodies were preabsorbed with the immunizing peptide as shown in the figure. A control for nonspecific staining omitted the primary Ab (data not shown).

    Techniques Used: Cell Culture, Expressing, Labeling, Staining

    Colocalization of HCN1 and IB4 or VR1. A , No dose ganglion section immunolabeled with rabbit HCN1 Ab (left) and IB4 lectin (right). HCN1 neurons do not contain IB4. Three of the HCN1-labeled neurons are identified by an asterisk. B , Nodose section labeled with anti-HCN1 Ab (left) and anti-VR1 Ab (center) is shown overlaid on the right. The neurons with strong labeling for HCN1 did not coexpress VR1, but weaker HCN1 staining is seen on two VR1(*)-immunoreactive neurons. The arrow indicates an example of HCN1 axonal labeling.
    Figure Legend Snippet: Colocalization of HCN1 and IB4 or VR1. A , No dose ganglion section immunolabeled with rabbit HCN1 Ab (left) and IB4 lectin (right). HCN1 neurons do not contain IB4. Three of the HCN1-labeled neurons are identified by an asterisk. B , Nodose section labeled with anti-HCN1 Ab (left) and anti-VR1 Ab (center) is shown overlaid on the right. The neurons with strong labeling for HCN1 did not coexpress VR1, but weaker HCN1 staining is seen on two VR1(*)-immunoreactive neurons. The arrow indicates an example of HCN1 axonal labeling.

    Techniques Used: Immunolabeling, Labeling, Staining

    HCN1, HCN2, HCN3, and HCN4 mRNA is expressed in nodose ganglia. PCR products resulting from the amplification of first-strand cDNA prepared with (+) or without (–) RT from nodose ganglia or brain poly A+ RNA with HCN1-, HCN2-, HCN3-, and HCN4-specific oligonucleotides were separated by electrophoresis and transferred to nylon membranes (Ambion). After Southern hybridization with 32 P-labeled specific internal oligomers, the autoradiogram showed a positive signal for all four channels from nodose and rat brain in the (+) RT lanes and no signals in the control (–) RT. The oligonucleotide probes amplify cDNA of 641 bp for HCN1, 638 bp for HCN2, 509 bp for HCN3, and 635 bp for HCN4.
    Figure Legend Snippet: HCN1, HCN2, HCN3, and HCN4 mRNA is expressed in nodose ganglia. PCR products resulting from the amplification of first-strand cDNA prepared with (+) or without (–) RT from nodose ganglia or brain poly A+ RNA with HCN1-, HCN2-, HCN3-, and HCN4-specific oligonucleotides were separated by electrophoresis and transferred to nylon membranes (Ambion). After Southern hybridization with 32 P-labeled specific internal oligomers, the autoradiogram showed a positive signal for all four channels from nodose and rat brain in the (+) RT lanes and no signals in the control (–) RT. The oligonucleotide probes amplify cDNA of 641 bp for HCN1, 638 bp for HCN2, 509 bp for HCN3, and 635 bp for HCN4.

    Techniques Used: Polymerase Chain Reaction, Amplification, Electrophoresis, Hybridization, Labeling

    HCN immunoreactivity in aortic baroreceptor terminals of myelinated fibers. Top, A collapsed Z-series stack of 0.4 μm confocal sections through a bush baroreceptor terminal shows localization of HCN1 (left) and PGP9.5 (right). PGP9.5 is a ubiquitin hydrolase expressed in neuronal–neuroendocrine cells. Middle, Bush ending is colabeled with HCN2 on the left and the neurofilament mixture on the right. Bottom, HCN4 immunoreactivity on the left is localized to the bush ending identified using the neurofilament mixture (right).
    Figure Legend Snippet: HCN immunoreactivity in aortic baroreceptor terminals of myelinated fibers. Top, A collapsed Z-series stack of 0.4 μm confocal sections through a bush baroreceptor terminal shows localization of HCN1 (left) and PGP9.5 (right). PGP9.5 is a ubiquitin hydrolase expressed in neuronal–neuroendocrine cells. Middle, Bush ending is colabeled with HCN2 on the left and the neurofilament mixture on the right. Bottom, HCN4 immunoreactivity on the left is localized to the bush ending identified using the neurofilament mixture (right).

    Techniques Used:

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    Alomone Labs hcn1
    TRIP8b interaction with <t>HCN1</t> is independent of TRIP8b alternative splicing and is bipartite
    Hcn1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hcn1/product/Alomone Labs
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hcn1 - by Bioz Stars, 2022-06
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    Image Search Results


    TRIP8b interaction with HCN1 is independent of TRIP8b alternative splicing and is bipartite

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Alternatively spliced isoforms of TRIP8b differentially control h channel trafficking and function

    doi: 10.1523/JNEUROSCI.0856-09.2009

    Figure Lengend Snippet: TRIP8b interaction with HCN1 is independent of TRIP8b alternative splicing and is bipartite

    Article Snippet: The following primary antibodies were used: mouse (ms) monoclonal antibodies to α-tubulin (DM1A, Upstate Biotechnology, Lake Placid, NY); rabbit (rab) polyclonal antibodies to HCN1 (Alomone Labs, Jerusalem); ms monoclonal to HA epitope (F-7, Santa Cruz Biotechnology, Santa Cruz, CA); Guinea pig (gp) polyclonal antibodies to HCN1 ( ); gp polyclonal antibodies to HCN2 ( ); rab and gp polyclonal antibodies to green fluorescent protein (see antibody generation and , available at as ); rab polyclonal antibodies to TRIP8b ( ); gp polyclonal antibodies to TRIP8b (see antibody generation and , available at as ); gp polyclonal antibodies to HCN4 ( ); gp polyclonal antibodies to TRIP8b exon 1a-5, exon 2, and exon 4 (see antibody generation and ); ms monoclonal to MAP-2 (Sigma, St. Louis, MO).

    Techniques:

    TRIP8b isoforms increase or decrease I h peak current in HCN1 cotransfected HEK293T cells depending on isoform identity

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Alternatively spliced isoforms of TRIP8b differentially control h channel trafficking and function

    doi: 10.1523/JNEUROSCI.0856-09.2009

    Figure Lengend Snippet: TRIP8b isoforms increase or decrease I h peak current in HCN1 cotransfected HEK293T cells depending on isoform identity

    Article Snippet: The following primary antibodies were used: mouse (ms) monoclonal antibodies to α-tubulin (DM1A, Upstate Biotechnology, Lake Placid, NY); rabbit (rab) polyclonal antibodies to HCN1 (Alomone Labs, Jerusalem); ms monoclonal to HA epitope (F-7, Santa Cruz Biotechnology, Santa Cruz, CA); Guinea pig (gp) polyclonal antibodies to HCN1 ( ); gp polyclonal antibodies to HCN2 ( ); rab and gp polyclonal antibodies to green fluorescent protein (see antibody generation and , available at as ); rab polyclonal antibodies to TRIP8b ( ); gp polyclonal antibodies to TRIP8b (see antibody generation and , available at as ); gp polyclonal antibodies to HCN4 ( ); gp polyclonal antibodies to TRIP8b exon 1a-5, exon 2, and exon 4 (see antibody generation and ); ms monoclonal to MAP-2 (Sigma, St. Louis, MO).

    Techniques:

    TRIP8b isoforms bidirectionally modify HCN1 protein surface expression as determined by flow cytometry

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Alternatively spliced isoforms of TRIP8b differentially control h channel trafficking and function

    doi: 10.1523/JNEUROSCI.0856-09.2009

    Figure Lengend Snippet: TRIP8b isoforms bidirectionally modify HCN1 protein surface expression as determined by flow cytometry

    Article Snippet: The following primary antibodies were used: mouse (ms) monoclonal antibodies to α-tubulin (DM1A, Upstate Biotechnology, Lake Placid, NY); rabbit (rab) polyclonal antibodies to HCN1 (Alomone Labs, Jerusalem); ms monoclonal to HA epitope (F-7, Santa Cruz Biotechnology, Santa Cruz, CA); Guinea pig (gp) polyclonal antibodies to HCN1 ( ); gp polyclonal antibodies to HCN2 ( ); rab and gp polyclonal antibodies to green fluorescent protein (see antibody generation and , available at as ); rab polyclonal antibodies to TRIP8b ( ); gp polyclonal antibodies to TRIP8b (see antibody generation and , available at as ); gp polyclonal antibodies to HCN4 ( ); gp polyclonal antibodies to TRIP8b exon 1a-5, exon 2, and exon 4 (see antibody generation and ); ms monoclonal to MAP-2 (Sigma, St. Louis, MO).

    Techniques: Expressing, Flow Cytometry

    TRIP8b isoforms A4, B2, and B3 alter amount of surface HCN1 protein

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Alternatively spliced isoforms of TRIP8b differentially control h channel trafficking and function

    doi: 10.1523/JNEUROSCI.0856-09.2009

    Figure Lengend Snippet: TRIP8b isoforms A4, B2, and B3 alter amount of surface HCN1 protein

    Article Snippet: The following primary antibodies were used: mouse (ms) monoclonal antibodies to α-tubulin (DM1A, Upstate Biotechnology, Lake Placid, NY); rabbit (rab) polyclonal antibodies to HCN1 (Alomone Labs, Jerusalem); ms monoclonal to HA epitope (F-7, Santa Cruz Biotechnology, Santa Cruz, CA); Guinea pig (gp) polyclonal antibodies to HCN1 ( ); gp polyclonal antibodies to HCN2 ( ); rab and gp polyclonal antibodies to green fluorescent protein (see antibody generation and , available at as ); rab polyclonal antibodies to TRIP8b ( ); gp polyclonal antibodies to TRIP8b (see antibody generation and , available at as ); gp polyclonal antibodies to HCN4 ( ); gp polyclonal antibodies to TRIP8b exon 1a-5, exon 2, and exon 4 (see antibody generation and ); ms monoclonal to MAP-2 (Sigma, St. Louis, MO).

    Techniques:

    Isoforms of TRIP8b alter the trafficking of HCN1 in cultured hippocampal neurons

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Alternatively spliced isoforms of TRIP8b differentially control h channel trafficking and function

    doi: 10.1523/JNEUROSCI.0856-09.2009

    Figure Lengend Snippet: Isoforms of TRIP8b alter the trafficking of HCN1 in cultured hippocampal neurons

    Article Snippet: The following primary antibodies were used: mouse (ms) monoclonal antibodies to α-tubulin (DM1A, Upstate Biotechnology, Lake Placid, NY); rabbit (rab) polyclonal antibodies to HCN1 (Alomone Labs, Jerusalem); ms monoclonal to HA epitope (F-7, Santa Cruz Biotechnology, Santa Cruz, CA); Guinea pig (gp) polyclonal antibodies to HCN1 ( ); gp polyclonal antibodies to HCN2 ( ); rab and gp polyclonal antibodies to green fluorescent protein (see antibody generation and , available at as ); rab polyclonal antibodies to TRIP8b ( ); gp polyclonal antibodies to TRIP8b (see antibody generation and , available at as ); gp polyclonal antibodies to HCN4 ( ); gp polyclonal antibodies to TRIP8b exon 1a-5, exon 2, and exon 4 (see antibody generation and ); ms monoclonal to MAP-2 (Sigma, St. Louis, MO).

    Techniques: Cell Culture

    Analyses of expression of the Cav2.3 protein in neuronal and nonneuronal cells or in cell membrane of the cells in dorsal root ganglia in vivo. Representative images to demonstrate expression of Cav2.3 in mouse DRG and colabeling with PGP9.5-positive neuronal cells (A), GFAP-positive satellite cells (B) and with HCN1 (hyperpolarization-activated cyclic nucleotide-gated) channel in the cell membrane (C). Observed colocalization is highlighted with white arrows. Quantification of coexpression of each neuronal subtype with the Cav2.3 expressing neurons is shown in panel D. Scale bars represent 50 µm in all panels. Tissue samples from 3 independent mice were analyzed.

    Journal: Pain

    Article Title: miR-34c-5p functions as pronociceptive microRNA in cancer pain by targeting Cav2.3 containing calcium channels

    doi: 10.1097/j.pain.0000000000000971

    Figure Lengend Snippet: Analyses of expression of the Cav2.3 protein in neuronal and nonneuronal cells or in cell membrane of the cells in dorsal root ganglia in vivo. Representative images to demonstrate expression of Cav2.3 in mouse DRG and colabeling with PGP9.5-positive neuronal cells (A), GFAP-positive satellite cells (B) and with HCN1 (hyperpolarization-activated cyclic nucleotide-gated) channel in the cell membrane (C). Observed colocalization is highlighted with white arrows. Quantification of coexpression of each neuronal subtype with the Cav2.3 expressing neurons is shown in panel D. Scale bars represent 50 µm in all panels. Tissue samples from 3 independent mice were analyzed.

    Article Snippet: Primary antibodies used for IF are Guinea pig anti-PGP9.5 (1:100 dilution, 14104, Neuromics, Edina, MN), Guinea pig anti-HCN1 (1:100, Alomone Labs, AGP203) rabbit anti-Cav2.3 antibody (1:80, Alomone Labs, ACC-006), Biotinylated-Isolectin B4 (1:100; B-1205, Vector, Burlingame, CA), Guinea pig Substance P (1:150; Neuromics GP14103), Anti-GFAP (1:500; NeuroMab clone N206A/8, UC Davis, Davis, CA) and Chicken anti-NF200 (1:500; Neuromics CH23015).

    Techniques: Expressing, In Vivo, Mouse Assay