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Validated All-in-One™ qPCR Primer for KCNA5(NM_002234.3) Search again
Product ID:
HQP009873
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ATFB7, HCK1, HK2, HPCN1, KV1.5, PCN1
Gene Description:
potassium voltage-gated channel subfamily A member 5
Target Gene Accession:
NM_002234.3(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:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
Potassium channels represent the most complex class of voltage-gated ino channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s).
Gene References into function
- characterization of a truncated form of Kv1.5
- Modulation by protein kinase C activation: role of the Kvbeta1.2 subunit.
- co-localization of Kv1.5 with PSD95 at the cell surface is similarly independent of the canonical PDZ-binding motif
- Reduction in the activation energy for the inactivation transition from the open state underlies the inhibition of hKv1.5 Na(+) current at low pH.
- Kv1.5 potassium channel mRNA expression correlates with glioma entities and malignancy grades; expression is high in astrocytomas, moderate in oligodendrogliomas, and low in glioblastomas.
- multiple isoforms of SAP97 were identifed in human heart atrium specimens; isoforms were found to co-immunoprecipiate with hKv1.5; isoforms were found to have distinct effect on hKv1.5 current and spatial channel organization
- the destabilization or bending of the S6 alpha-helix of KV1.5 caused by the PXP motif apparently creates a flexible "hinge" that allows movement of the lower S6 segment during channel gating and opening
- No electrical remodeling is evident in Kv1.5DN-expressing ventricular myocytes, and the (Kv1.5DN-induced) elimination of IK,slow1 does not result in spontaneous ventricular arrhythmias.
- an examination of the effect of K channel blocker S0100176) on the structure of the Kv1.5 channel
- Overexpression of the human KCNA5 gene increases K+ currents (i.e., K+ efflux or loss), accelerates apoptotic volume decrease (AVD), increases caspase-3 activity, and induces apoptosis
- Heterologously expressed human pulmonary arterial smooth muscle cells (PASMC) Kv1.5 generated an O2- and correolide-sensitive I(K) like that in resistance PASMCs.
- There is a central role for developmentally regulated ductus arteriosus SMC O2-sensitive Kv channels in the functional closure of the DA.
- This suggests that for Kv channels, the coupling between voltage sensing and gating reflects primarily an intrasubunit interaction.
- P. 142: "An aligment of KCNA5 among human, mouse, and rat shows 86% amino acid identity, and no monogenicc human arrhythmia syndrome has been linked to KCNA5"
- a pathway for Kv1.5 internalization from the cell surface involving early endosomes, followed by later trafficking by the dynein motor along microtubules.
- KCNA5 is an important Kv channel that regulates resting membrane potential and that acute hypoxia selectively reduces KCNA5 channel activity in pulmonary smooth muscle cells relative to mesenteric smooth muscle cells and other cell types.
- We found three heterozygous SNPs: R87Q, A251T, and P307S. Both R87Q and P307S diminished the inactivation amplitude.
- specific inhibition of kinase C by Calphostin C eliminated the increase in wild-type hKv1.5 currents associated with synapse-associated protein 97 overexpression suggesting a role for this kinase in the response
- functional role of K(v)1.5 and K(v)1.3 on activated human dendritic cells
- hKv1.5 channel is expressed in human alveolar macrophages and it plays a role in phagocytosis and migration of the human alveolar macrophage.
- Mg2+ block causes voltage-dependent inactivation of Kv1.5
- These results imply that protonation of residue 463 does not modulate inactivation solely by an electrostatic interaction with residues near the pore mouth.
- results suggest Kv1.5 channels are modulated by agonists; novel SNPs are present in idiopathic pulmonary arterial hypertension; SNPs may underlie altered expression and/or function of Kv1.5 channels in pulmonary artery smooth muscle cells in IPAH
- S-acylation can regulate steady-state expression of Kv1.5.
- Down-regulation of Kv1.5 enhanced the drug-resistant phenotype of gastric cancer cells.
- In conclusion, N-cadherin modifies Kv1.5 channel activity and is thus a novel candidate signaling molecule participating in the regulation of a variety of functions including cardiac action potential and vascular tone.
- mitochondrial abnormalities that disturb the reactive O(2) species HIF-1alpha-Kv1.5 O(2)-sensing pathway contribute to the pathogenesis of pulmonary arterial hypertension and cancer--REVIEW
- KCNA5 is involved K(+)-channel in regulatory volume decrease in human spermatozoa, and channel activity is regulated beyond the extent of protein expression.
- R87Q and P307S polymorphisms in hKv1.5, possibly in combination with other risk factors, may influencethe development of postoperative atrial fibrillation
- implicate the traffic and localization of Kv1.3/Kv1.5 heteromers in the complex regulation of immune system cells
- SAP97 regulates the K(+) current in cardiac myocytes by retaining and immobilizing Kv1.5 subunits in the plasma membrane.
- Results support a role of FHL1 as a key molecular component in the I(Kur) complex in human atrium, where it likely regulates functional expression of KCNA5.
- Report a Kv1.5 channel with an altered activation gate sequence that displays both "fast" and "slow" activation kinetics.
- Active site architecture, certain key residues and pharmacophore common-features responsible for substrate specificity are identified on Kv1.5 potassium channel that are very helpful in understanding the blockade mechanism of Kv1.5 potassium channel.
- The Rab GTPases thus constitute dynamic targets by which cells may modulate Kv1.5 functional expression.
- Double-mutant cycle analysis indicates that R5 of Kvbeta1.3 interacts with A501 and T480 of Kv1.5, residues located deep within the pore of the channel.
- Replacing L45 and S6(T) by corresponding hKv2.1 sequences, transfered the hKv2.1 kinetics but not the voltage dependence to hKv1.5. Point mutations in S6(T) show that it needs to be alpha-helical and forms a "crevice" for the L45 residues I422 and T426.