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Validated All-in-One™ qPCR Primer for TRPC6(NM_004621.5) Search again
Product ID:
HQP088426
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
FSGS2, TRP6
Gene Description:
transient receptor potential cation channel subfamily C member 6
Target Gene Accession:
NM_004621.5(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:
Summary
The protein encoded by this gene forms a receptor-activated calcium channel in the cell membrane. The channel is activated by diacylglycerol and is thought to be under the control of a phosphatidylinositol second messenger system.
Gene References into function
- T-cells express a diacylglycerol-activated cation channel, unrelated to the channel involved in capacitative Ca(2+) entry, and associated with the expression of TRP6 protein
- an examination of subunits in living cells
- expresssed in platelets: forms the store-independent calcium entry channel
- may be candidate protein forming store-operated calcium entry channels in term pregnant human myometrium
- Expression of the channel in human esophagogastric junction.
- Data demonstrate the expression of transient receptor potential channel 6 (TRPC6) and a range of homologs in the airway and the presence of a functional Ca(2+) entry pathway with characteristics typical of TRPC family members.
- the pattern of TRPC3 and TRPC6 glycosylation determines regulation of their activity
- an exocytotic mechanism is involved in the activation of TRPC6
- TRPC6 channels are activated by receptor stimulation
- TRPC channel overexpression may be partially responsible for the increased pulmonary artert smooth muscle cell proliferation and pulmonary vascular medial hypertrophy in pulmonary hypertension patients.
- Data suggest that the link between transient receptor potential channel 6 and phosphatidylinositol 3,4,5-trisphosphate-mediated calcium entry may be involved in initiating calcium response to agonist stimulation in T cells.
- TRPC3/TRPC6 channels are localized to the apical region of polarized epithelial cells, which in salivary gland ducts could contribute to the regulation of salivary [Ca2+] and secretion [TRPC6]
- a family with familial focal segmental glomerulosclerosis carries a missense mutation in TRPC6; the proline-to-glutamine substitution enhances TRPC6-mediated calcium signals in response to agonists & appears to alter intracellular distribution of TRPC6
- the canonical transient receptor potential 6 (TRPC6) ion channel is expressed in podocytes and is a component of the glomerular slit diaphragm.
- Mutation on chromosome 11 may be involved in focal sclerosing glomerulonephritis.
- study suggests that the lysophosphatidylcholine increases calcium in corporal smooth muscle cells probably through activation of a transcript of transient receptor potential channel 6 (TRPC6) channel
- in cells exhibiting a high input resistance, the primary effect of activating TRPC6 will be membrane depolarization
- demonstrates that hTrpC1 and hTrpC4 are the most abundant TrpC mRNAs in human myometrium, with TrpC6 being the next most abundant; these isoforms may play significant roles in signal regulated calcium entry in human myometrium
- Biochemical and functional evidence supporting the view that heteromultimeric TRPC6-TRPC7 channels contribute to receptor-activated, nonselective cation channels of A7r5 vascular smooth muscle cells. (TRPC6 and TRPC7 channels)
- In this review, the known roles of TRPC6 in the kidney and other organ systems are used as a framework to discuss possible signaling pathways that TRPC6 may modulate during normal glomerular function and in disease states.
- Galphaq activation of TRPC6 signals the activation of PKCalpha, and thereby induces RhoA activity and endothelial cell contraction
- TRPC6 was identified as an essential component of the slit diaphragm architecture of kidney podocytes--{review}
- TRPC6 bound directly to phosphoinositides, and with highest potency to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)). PIP(3) binding disrupted the association of calmodulin (CaM) with TRPC6.
- Orai1 physically interacts with the N and C termini of TRPC3 and TRPC6
- Snapin links the alpha(1A)-AR to TRPC6, augmenting Ca(2+) influx via ROC channels
- TRPC6 protein expression in glomerular mesangial cells (MCs) was downregulated by high glucose and the deficiency of TRPC6 protein might contribute to the impaired Ca(2+) signaling of MCs seen in diabetes.
- Phosphatidylinositol 4,5-bisphosphate enhances store-operated Ca2+ entry in human platelets, most probably by stimulation of hTRPC6 channels
- mitochondria limit the cytosolic diffusion of localized Na+ transients generated by agonist-mediated activation of transient receptor potential channel 6-containing channels
- functional expression of TRPC6 in mammalian stretch-activated mechano-sensitive Ca(2+) permeable cation channels remains problematic
- Human and mouse erythrocytes express TRPC6 cation channels which participate in cation leak and Ca(2+)-induced suicidal death.
- tested the hypothesis that hyperglycemia increases the expression of TRPC6 channels
- data show that calcium influx in HL-60 cells relies on TRPC channels 1,3, and 6, and Orai1 for allowing NADPH oxidase activation
- analysis of a TRPC6-TRPC5 channel cascade that restricts endothelial cell movement
- TRPC6 was very weakly expressed in isolated hepatocytes from healthy patients and expressed more strongly in tumoral samples from the liver of a cancer patient, strongly supporting a role for these calcium channels in liver oncogenesis.
- These results strongly suggest that TRPC6 channels can be negatively regulated by the nitric oxide-cyclic GMP-protein kinase G pathway, probably via T69 phosphorylation of the N-terminal.
- TRPC6 is an obligatory component of cation channels required for the VEGF-mediated increase in cytosolic calcium and subsequent downstream signaling that leads to processes associated with angiogenesis
- TRPC6 activation is sufficient to induce keratinocyte differentiation similar to the physiological stimulus [Ca(2+)](o)
- Two calcium2+-permeable members of the TRPC family of cation channels, TRPC3 and TRPC6, can interact with the pore-forming subunits of BKCa channels in podocytes and in heterologous systems in which both classes of channels are transiently expressed.
