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Validated All-in-One™ qPCR Primer for TRPC1(NM_001251845.2) Search again
Product ID:
HQP162353
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HTRP-1, TRP1
Gene Description:
transient receptor potential cation channel subfamily C member 1
Target Gene Accession:
NM_001251845.2(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.
Gene References into function
- Calmodulin regulates Ca(2+)-dependent feedback inhibition of store-operated Ca(2+) influx by interaction with a site in the C terminus of TrpC1.
- an examination of subunits in living cells
- Inhibition of endogenous TRP1 decreases capacitative Ca2+ entry and attenuates pulmonary artery smooth muscle cell proliferation.
- involved in the activation of store-mediated Ca(2+) entry by coupling to IP3R1 in normal human platelets
- may be candidate protein forming store-operated calcium entry channels in term pregnant human myometrium
- Caveolin-1 contributes to assembly of store-operated Ca2+ influx channels by regulating plasma membrane localization of TRPC1.
- Expression of the channel in human esophagogastric junction.
- TRPC1 interaction with IP3R is signaled by Rho activation at the plasma membrane of endothelial cells, and Ca2+ entry is triggered following store depletion
- TRPC1 store dependence is suppressed by I-mfa1
- TRPC1 is associated with cholesterol-rich lipid raft domains in human platelets; these domains are important for participation of TRPC1 in store-mediated Ca2+ entry in platelets.
- analysis of hydrophobic regions of transient receptor potential Ca2+ channel TRPC1
- Phosphorylation of TRPC1 and Ca2+ entry were essential for the increase in permeability induced by thrombin in confluent endothelial monolayers.
- Ca(2+) increase related to the incorporation of 7-ketocholesterol into lipid raft domains of the plasma membrane, followed by the translocation of transient receptor potential calcium channel 1
- hTRPC1 is an important Ca(2+)-permeable channel that mediates pulmonary vasoconstriction when pulmonary artery smooth muscle cell intracellular Ca2+ stores are depleted.
- Expression level of TRPC1 in endothelial cells is a critical determinant of Ca(2+) influx and signaling of the increase in endothelial permeability.
- role in inhibiting 1-methyl-4-phenylpyridinium ion neurotoxicity in human SH-SY5Y neuroblastoma 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]
- TRPC1, but not TRPC4, interacts with PLCgamma1 and the inositol 1,4,5-trisphosphate receptor (IP3R).
- TRPC1 and/or TRPC5 channels serve as store-operated Ca2+ channels in A431 cells, and may function as regulators for intracellular Ca2+ signaling.
- TRPC1 and TRPC3 co-assemble, via N-terminal interactions, to form a heteromeric store-operated non-selective cation channel in HSY cells
- endogenous TRPC1, TRPC3, and TRPC7 participate in forming heteromeric store-operated channels, whereas TRPC3 and TRPC7 can also participate in forming heteromeric receptor-operated channels.
- TRPC1 is involved in calcium-induced differentiation of human gingival keratinocytes likely by supporting a store-operated calcium ion influx.
- 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
- therefore suggesting that TRPC1 and/or TRPC3 proteins are responsible for the response to alpha-adrenergic stimulation but that TRPC1, TPRC3 and TRPV6 proteins, expressed alone or concomitantly, are not sufficient for SOC formation.
- results indicate that TRPC1 proteins function as Ca2+ permeable channels in intestinal epithelial cells and play a critical role in the regulation of apoptosis
- protease-activated receptor-1 has a role in calcium influx, which activates a feed-forward mechanism of TRPC1 expression via nuclear factor-kappaB activation in endothelial cells
- Thus, these results demonstrate a crucial role of caveolin-1 scaffolding domain interaction with TRPC1 in regulating Ca2+ influx via SOC.
- Interaction of STIM1 with endogenously expressed human canonical TRP1 (hTRPC1) upon depletion of intracellular Ca2+ stores.
- We suggest that the anti-apoptotic effect of TRPC1 could potentially contribute to abnormal keratosis in DD.
- activation of TRPC1 leads to the entry to the cytoplasmic space of substantial amounts of Na+ as well as Ca2+--{REVIEW}
- dynamic assembly of TRPC1-STIM1-Orai1 ternary complex is involved in activation of SOC channel in response to internal Ca2+ store depletion
- TRPC1 has an important role in store-operated calcium channels [review]
- Angiotensin II and subsequent NF-kappaB activation induce human coronary artery smooth muscle cell hypertrophy through an enhancement of transient receptor potential channel 1 (TRPC1) expression.
- In human salivary gland TRPC1 regulates calcium homeostasis and may have a role in cell differentiation.
- These results indicate that TRPC1 is a multifunctional protein able to form intracellular calcium release channels when expressed alone, and plasma membrane channels when co-expressed with TRPC4 or TRPC5, but not TRPC3 or TRPC6.
- TRPC1-associated alpha-actinin is tyrosine phosphorylated during platelet activation.
- TRPC1 channel expression was important for keratinocyte differentiation, as knocking out the channels (by siRNA strategy) prevented the induction of Ca(2+)-induced differentiation.
- functional expression of TRPC1 in mammalian stretch-activated mechano-sensitive Ca(2+) permeable cation channels remains problematic
- TRPC5 and TRPC1 are expressed in secretory fibroblast-like synoviocytes from patients with rheumatoid arthritis, and endogenous TRPC5-TRPC1 channels of the cells are activated by reduced thioredoxin
- Dyssregulation of HNF 4 alpha and TRPC1 may be a possible molecular rationale in diabetic nephropathy.
- Provide evidence for a functional role of the de novo coupling between hTRPC1 and IP3RII in the activation of store operated calcium entry in platelets.
- These findings shed new light on the constituents of the D2R signalplex, and support the involvement of D2Rs in cellular calcium signaling pathways via a novel link to TRPC channels.
- demonstrate a functional requirement for Orai1 in TRPC1+STIM1-dependent SOCE
- Data show that STIM1 and TRPC1 interact and insert TRPC1 into lipid rafts, where TRPC1 functions as a store-operated channel; in the absence of STIM1, TRPC1 associates with other members from the TRPC family of channels to form receptor-operated channels
- intact lipid raft domains determine targeting of STIM1 clusters to ER-plasma membrane junctions following store depletion which facilitates the functional interaction of STIM1 with TRPC1 and activation of store-operated Ca(2+) entry
- data show that calcium influx in HL-60 cells relies on TRPC channels 1,3, and 6, and Orai1 for allowing NADPH oxidase activation
- Huh-7 and HepG2 cells (hepatoma cell lines) express transient receptor potential canonical 1 (TRPC1) and TRPC6, as well as STIM1 and Orai1, and these 4 channels are the most likely candidates to account for the Store-operated calcium entry in these cells
- TRPC1 channels regulate directionality of migrating cells.
- Store-operated Ca(2+) entry in platelets occurs independently of transient receptor potential (TRP) C1.
- the STIM1-Orai1-hTRPC1 complex has a role in the activation of store-operated Ca(2+) entry
- Report interactions, functions, and independence of plasma membrane STIM1 and TRPC1 in vascular smooth muscle cells.
- thrombin-induced p65/RelA, AMPK, and PKCdelta activation were markedly reduced by knockdown of the TRPC isoform TRPC1 expressed in human endothelial cells and in endothelial cells obtained from Trpc4 knock-out mice.
- STIM1 gates TRPC1 by intermolecular electrostatic interaction.