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Boster Bio rabbit anti hcn2 primary antibody

HCND is required for the function of <t>HCN2</t> channels. A, ribbon representation of the cryo-EM structure of HCN1 (PDB code 5U6P; Ref. 17). Only two diagonal subunits are shown for clarity. The transmembrane segments (TM) are gray, the HCND is orange, the C-linker is red, the CNBD is blue, and the distal C terminus is green. cAMP is shown in yellow. B, amino acid sequence alignment of the HCND for all four mammalian HCN channel isoforms. Identical residues are shown on a yellow background, conserved residues are on a blue background, and similar residues are on a green background. Letters without a background indicate nonsimilar residues. C and D, representative currents recorded from the WT (C) and ΔHCND mutant (D) mHCN2 channels.

Rabbit Anti Hcn2 Primary Antibody, supplied by Boster Bio, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+hcn2+primary+antibody/Anti-HCN2+Antibody+Picoband/pmc07294080-343-7-11
Average 90 stars, based on 4 article reviews

rabbit anti hcn2 primary antibody - by Bioz Stars, 2026-09

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1) Product Images from "The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms"

Article Title: The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.RA120.013281

HCND is required for the function of HCN2 channels. A, ribbon representation of the cryo-EM structure of HCN1 (PDB code 5U6P; Ref. 17). Only two diagonal subunits are shown for clarity. The transmembrane segments (TM) are gray, the HCND is orange, the C-linker is red, the CNBD is blue, and the distal C terminus is green. cAMP is shown in yellow. B, amino acid sequence alignment of the HCND for all four mammalian HCN channel isoforms. Identical residues are shown on a yellow background, conserved residues are on a blue background, and similar residues are on a green background. Letters without a background indicate nonsimilar residues. C and D, representative currents recorded from the WT (C) and ΔHCND mutant (D) mHCN2 channels.

Figure Legend Snippet: HCND is required for the function of HCN2 channels. A, ribbon representation of the cryo-EM structure of HCN1 (PDB code 5U6P; Ref. 17). Only two diagonal subunits are shown for clarity. The transmembrane segments (TM) are gray, the HCND is orange, the C-linker is red, the CNBD is blue, and the distal C terminus is green. cAMP is shown in yellow. B, amino acid sequence alignment of the HCND for all four mammalian HCN channel isoforms. Identical residues are shown on a yellow background, conserved residues are on a blue background, and similar residues are on a green background. Letters without a background indicate nonsimilar residues. C and D, representative currents recorded from the WT (C) and ΔHCND mutant (D) mHCN2 channels.

Techniques Used: Cryo-EM Sample Prep, Sequencing, Mutagenesis

$HCND is essential for the surface expression of HCN2 channels. A, top panel, representative immunoblot of the biotinylated protein fraction for untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells probed with HCN2 specific antibody. Bottom panel, representative immunoblot of the whole-cell lysates from untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells probed with α-tubulin antibodies. B, quantification of unglycosylated channel expression in untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells. The means of the data are presented as black lines. n = 3. The data were compared using unpaired Student's t test. *, p < 0.0001. C, ribbon representation of the WT and ΔHCND mutant mHCN2 channels. The same color coding as in Fig. 1A, with the KYK ER retention signal residues shown in red spheres. D, representative currents from KYK_AAA/ΔHCND mutant channels.$
Figure Legend Snippet: HCND is essential for the surface expression of HCN2 channels. A, top panel, representative immunoblot of the biotinylated protein fraction for untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells probed with HCN2 specific antibody. Bottom panel, representative immunoblot of the whole-cell lysates from untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells probed with α-tubulin antibodies. B, quantification of unglycosylated channel expression in untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells. The means of the data are presented as black lines. n = 3. The data were compared using unpaired Student's t test. *, p < 0.0001. C, ribbon representation of the WT and ΔHCND mutant mHCN2 channels. The same color coding as in Fig. 1A, with the KYK ER retention signal residues shown in red spheres. D, representative currents from KYK_AAA/ΔHCND mutant channels.

Techniques Used: Expressing, Western Blot, Control, Transfection, Mutagenesis

Interactions between the HCND and S2 are required for the HCN2 channel function. A, enlarged view of the interaction interface between the HCND and the VSD in HCN1 channel structure. The interacting residues Gly197 and Arg195 on the S2 and Ile135 on the HCND are shown as sticks. Corresponding residues in HCN2 channels are shown in parentheses. B, representative currents from R237A/G239A mutant mHCN2 channels.

Figure Legend Snippet: Interactions between the HCND and S2 are required for the HCN2 channel function. A, enlarged view of the interaction interface between the HCND and the VSD in HCN1 channel structure. The interacting residues Gly197 and Arg195 on the S2 and Ile135 on the HCND are shown as sticks. Corresponding residues in HCN2 channels are shown in parentheses. B, representative currents from R237A/G239A mutant mHCN2 channels.

Techniques Used: Mutagenesis

Interactions between the HCND and C-linker–CNBD affect voltage-dependent gating of HCN2 channels. A, enlarged view of the interaction interface between the HCND and the C-linker–CNBD in HCN1 channels. The interacting residues Glu436 and Gln440 on the C-linker, His517 on the CNBD, and Arg112 on the HCND are shown as sticks. Corresponding residues in HCN2 channels are shown in parentheses. B, representative currents from E478A/Q482A/H559A (3M) mutant mHCN2 channels. C, averaged conductance–voltage relationship for the currents from WT (filled circles, n of 9) and 3M mutant (open circles, n of 10) mHCN2 channels. Lines correspond to the fits with the Boltzmann function with the V½ of −91.3 ± 0.3 mV for WT and −97.1 ± 0.3 mV for the 3M mutant, and s of 13.8 ± 0.2 for WT and 11.9 ± 0.3 for 3M mutant mHCN2 channels.

Figure Legend Snippet: Interactions between the HCND and C-linker–CNBD affect voltage-dependent gating of HCN2 channels. A, enlarged view of the interaction interface between the HCND and the C-linker–CNBD in HCN1 channels. The interacting residues Glu436 and Gln440 on the C-linker, His517 on the CNBD, and Arg112 on the HCND are shown as sticks. Corresponding residues in HCN2 channels are shown in parentheses. B, representative currents from E478A/Q482A/H559A (3M) mutant mHCN2 channels. C, averaged conductance–voltage relationship for the currents from WT (filled circles, n of 9) and 3M mutant (open circles, n of 10) mHCN2 channels. Lines correspond to the fits with the Boltzmann function with the V½ of −91.3 ± 0.3 mV for WT and −97.1 ± 0.3 mV for the 3M mutant, and s of 13.8 ± 0.2 for WT and 11.9 ± 0.3 for 3M mutant mHCN2 channels.

Techniques Used: Mutagenesis

Interactions between the HCND and C-linker–CNBD affect the cAMP-dependent gating of HCN2 channels. A and B, representative currents from WT (A) and 3M mutant (B) mHCN2 channels recorded at −90 mV in the absence (black) and presence (red) of 10 μm cAMP. C, plots of the percentage of increase in tail currents versus the cAMP concentration for WT (filled circles) and 3M (open circles) mutant mHCN2 channels. The tail currents were recorded at −40 mV after the test pulse to −90 mV. Lines correspond to the fits with the Hill equation with the Kd of 100 ± 40 nm for WT and 60 ± 20 nm for 3M mutant mHCN2 channels. n ≥ 5 for each condition. D, plots of deactivation time constants for tail currents recorded at −40 mV after the test pulse to −90 mV for WT and 3M mutant channels in the presence and absence of 10 μm cAMP, as indicated. The means of the data are presented as black lines. n = 6 for WT and n = 5 for 3M mutant channels. The data with and without cAMP for WT and 3M channels were compared using paired Student's t test. The data between WT and 3M mutant channels were compared using unpaired Student's t test. * p < 0.02.

Figure Legend Snippet: Interactions between the HCND and C-linker–CNBD affect the cAMP-dependent gating of HCN2 channels. A and B, representative currents from WT (A) and 3M mutant (B) mHCN2 channels recorded at −90 mV in the absence (black) and presence (red) of 10 μm cAMP. C, plots of the percentage of increase in tail currents versus the cAMP concentration for WT (filled circles) and 3M (open circles) mutant mHCN2 channels. The tail currents were recorded at −40 mV after the test pulse to −90 mV. Lines correspond to the fits with the Hill equation with the Kd of 100 ± 40 nm for WT and 60 ± 20 nm for 3M mutant mHCN2 channels. n ≥ 5 for each condition. D, plots of deactivation time constants for tail currents recorded at −40 mV after the test pulse to −90 mV for WT and 3M mutant channels in the presence and absence of 10 μm cAMP, as indicated. The means of the data are presented as black lines. n = 6 for WT and n = 5 for 3M mutant channels. The data with and without cAMP for WT and 3M channels were compared using paired Student's t test. The data between WT and 3M mutant channels were compared using unpaired Student's t test. * p < 0.02.

Techniques Used: Mutagenesis, Concentration Assay

Image Search Results

Journal: The Journal of Biological Chemistry

Article Title: The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms

doi: 10.1074/jbc.RA120.013281

Figure Lengend Snippet: HCND is required for the function of HCN2 channels. A, ribbon representation of the cryo-EM structure of HCN1 (PDB code 5U6P; Ref. 17). Only two diagonal subunits are shown for clarity. The transmembrane segments (TM) are gray, the HCND is orange, the C-linker is red, the CNBD is blue, and the distal C terminus is green. cAMP is shown in yellow. B, amino acid sequence alignment of the HCND for all four mammalian HCN channel isoforms. Identical residues are shown on a yellow background, conserved residues are on a blue background, and similar residues are on a green background. Letters without a background indicate nonsimilar residues. C and D, representative currents recorded from the WT (C) and ΔHCND mutant (D) mHCN2 channels.

Article Snippet: The HCN channels were detected using a rabbit anti-HCN2 primary antibody (Boster, A02804) that recognizes the C-terminal sequence of HCN2 channels and a goat anti-rabbit secondary antibody (Abcam, ab6721).

Techniques: Cryo-EM Sample Prep, Sequencing, Mutagenesis

Journal: The Journal of Biological Chemistry

Article Title: The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms

doi: 10.1074/jbc.RA120.013281

Figure Lengend Snippet: HCND is essential for the surface expression of HCN2 channels. A, top panel, representative immunoblot of the biotinylated protein fraction for untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells probed with HCN2 specific antibody. Bottom panel, representative immunoblot of the whole-cell lysates from untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells probed with α-tubulin antibodies. B, quantification of unglycosylated channel expression in untransfected (control), WT, and ΔHCND mHCN2 transfected HEK293 cells. The means of the data are presented as black lines. n = 3. The data were compared using unpaired Student's t test. *, p < 0.0001. C, ribbon representation of the WT and ΔHCND mutant mHCN2 channels. The same color coding as in Fig. 1A, with the KYK ER retention signal residues shown in red spheres. D, representative currents from KYK_AAA/ΔHCND mutant channels.

Techniques: Expressing, Western Blot, Control, Transfection, Mutagenesis

Journal: The Journal of Biological Chemistry

Article Title: The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms

doi: 10.1074/jbc.RA120.013281

Figure Lengend Snippet: Interactions between the HCND and S2 are required for the HCN2 channel function. A, enlarged view of the interaction interface between the HCND and the VSD in HCN1 channel structure. The interacting residues Gly197 and Arg195 on the S2 and Ile135 on the HCND are shown as sticks. Corresponding residues in HCN2 channels are shown in parentheses. B, representative currents from R237A/G239A mutant mHCN2 channels.

Techniques: Mutagenesis

Journal: The Journal of Biological Chemistry

Article Title: The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms

doi: 10.1074/jbc.RA120.013281

Figure Lengend Snippet: Interactions between the HCND and C-linker–CNBD affect voltage-dependent gating of HCN2 channels. A, enlarged view of the interaction interface between the HCND and the C-linker–CNBD in HCN1 channels. The interacting residues Glu436 and Gln440 on the C-linker, His517 on the CNBD, and Arg112 on the HCND are shown as sticks. Corresponding residues in HCN2 channels are shown in parentheses. B, representative currents from E478A/Q482A/H559A (3M) mutant mHCN2 channels. C, averaged conductance–voltage relationship for the currents from WT (filled circles, n of 9) and 3M mutant (open circles, n of 10) mHCN2 channels. Lines correspond to the fits with the Boltzmann function with the V½ of −91.3 ± 0.3 mV for WT and −97.1 ± 0.3 mV for the 3M mutant, and s of 13.8 ± 0.2 for WT and 11.9 ± 0.3 for 3M mutant mHCN2 channels.

Techniques: Mutagenesis

Journal: The Journal of Biological Chemistry

Article Title: The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms

doi: 10.1074/jbc.RA120.013281

Figure Lengend Snippet: Interactions between the HCND and C-linker–CNBD affect the cAMP-dependent gating of HCN2 channels. A and B, representative currents from WT (A) and 3M mutant (B) mHCN2 channels recorded at −90 mV in the absence (black) and presence (red) of 10 μm cAMP. C, plots of the percentage of increase in tail currents versus the cAMP concentration for WT (filled circles) and 3M (open circles) mutant mHCN2 channels. The tail currents were recorded at −40 mV after the test pulse to −90 mV. Lines correspond to the fits with the Hill equation with the Kd of 100 ± 40 nm for WT and 60 ± 20 nm for 3M mutant mHCN2 channels. n ≥ 5 for each condition. D, plots of deactivation time constants for tail currents recorded at −40 mV after the test pulse to −90 mV for WT and 3M mutant channels in the presence and absence of 10 μm cAMP, as indicated. The means of the data are presented as black lines. n = 6 for WT and n = 5 for 3M mutant channels. The data with and without cAMP for WT and 3M channels were compared using paired Student's t test. The data between WT and 3M mutant channels were compared using unpaired Student's t test. * p < 0.02.

Techniques: Mutagenesis, Concentration Assay

A specific band is shown in both hippocampal and total brain lysates, which is consistent with the predicted HCN2 molecular weight (95 kd).

Journal: bioRxiv

Article Title: Somatodendritic HCN channels in hippocampal OLM cells revealed by a convergence of computational models and experiments

doi: 10.1101/633941

Figure Lengend Snippet: A specific band is shown in both hippocampal and total brain lysates, which is consistent with the predicted HCN2 molecular weight (95 kd).

Article Snippet: Sections were then washed in PBS (3 × 10 min) and incubated with rabbit anti-HCN2 primary antibody (0.8 mg/ml in ADS, Alomone Labs, cat# APC-030) overnight at 4°C using an orbital shaker (Multi-Purpose Rotator, ThermoScientific).

Techniques: Molecular Weight

A. Neurotrace 435, B. endogenous tdTomato, and C. HCN2 immunofluorescence were imaged in hippocampal slices from Chrna2-CRE:tdTomato mice. D. Expanded view of two OLM cells illustrating E. HCN2 immunofluorescence on OLM cell proximal dendrites. F., H. tdTomato images of additional OLM cells with G., I. dendritic HCN2 immunofluorescence. Slices obtained from ventral hippocampal CA1. Scale bar in G. applies to zoomed out images in A., B., C., F., G. . Scale bar in I. applies to zoomed in images in D., E., H., I. .

Journal: bioRxiv

Article Title: Somatodendritic HCN channels in hippocampal OLM cells revealed by a convergence of computational models and experiments

doi: 10.1101/633941

Figure Lengend Snippet: A. Neurotrace 435, B. endogenous tdTomato, and C. HCN2 immunofluorescence were imaged in hippocampal slices from Chrna2-CRE:tdTomato mice. D. Expanded view of two OLM cells illustrating E. HCN2 immunofluorescence on OLM cell proximal dendrites. F., H. tdTomato images of additional OLM cells with G., I. dendritic HCN2 immunofluorescence. Slices obtained from ventral hippocampal CA1. Scale bar in G. applies to zoomed out images in A., B., C., F., G. . Scale bar in I. applies to zoomed in images in D., E., H., I. .

Techniques: Immunofluorescence

A. Endogenous td-Tomato and B. HCN2 immunofluorescence imaged in dorsal hippocampal slices from Chrna2-CRE:tdTomato mice. C., D. Expanded view of panels A., B. . Fewer tdTomato cells were found in dorsal compared to ventral slices.

Journal: bioRxiv

Article Title: Somatodendritic HCN channels in hippocampal OLM cells revealed by a convergence of computational models and experiments

doi: 10.1101/633941

Figure Lengend Snippet: A. Endogenous td-Tomato and B. HCN2 immunofluorescence imaged in dorsal hippocampal slices from Chrna2-CRE:tdTomato mice. C., D. Expanded view of panels A., B. . Fewer tdTomato cells were found in dorsal compared to ventral slices.

Techniques: Immunofluorescence

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1) Product Images from "The HCN domain is required for HCN channel cell-surface expression and couples voltage- and cAMP-dependent gating mechanisms"

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