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Validated All-in-One™ qPCR Primer for HCN2(NM_001194.3) Search again
Product ID:
HQP016388
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
BCNG-2, BCNG2, EIG17, FEB2, GEFSP11, HAC-1
Gene Description:
hyperpolarization activated cyclic nucleotide gated potassium and sodium channel 2
Target Gene Accession:
NM_001194.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Gene References into function
- HCN4 activates substantially slower than HCN2 and with a half-maximum activation voltage approximately equal 10 mV less negative, both isoforms activate more positively in myocytes suggesting cell-type specificity
- activation of the fast channel HCN2 is dependent on the S1 segment
- HCN1 and HCN2 expression were measured using in situ hybridization and immunocytochemistry in hippocampi; the expression of HCN isoforms is dynamically regulated in human as well as in experimental hippocampal epilepsy
- Native I(f) channels in atrial myocardium are heteromeric complexes composed of HCN4 and/or HCN2.
- Mutations of a putative cyclic-nucleotide-binding domain (CNBD) can disrupt the function of the hyperpolarization-activated cyclic-nucleotide-gated channel (HCN2).
- an intact F-actin cytoskeleton is a prerequisite for the swelling-induced HCN2 current
- With computer modelling, we show that in channels with relatively slow opening kinetics and fast mode-shift transitions, such as HCN2 and HCN4 channels, the mode shift effects are not readily observable, except in the tail kinetics.
- Noise analysis on macroscopic currents revealed fluctuations whose magnitudes were systematically larger than predicted from the actual single channel current size, consistent with cooperativity between single HCN channels.
- Several functional variants were identified including the amino acid substitution R527Q in HCN2 exon 5. HCN2 channels containing the R527Q variant demonstrated a trend towards a decreased slope of the conductance-voltage relation.
- down-regulation of miR-1 and miR-133 expression contributes to re-expression of HCN2/HCN4 and thereby the electrical remodeling process in hypertrophic hearts
- RPTPalpha plays a critical role in HCN channel function via tyrosine dephosphorylation
