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Validated All-in-One™ qPCR Primer for TRPM8(NM_024080.4) Search again
Product ID:
HQP018887
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
LTRPC6, LTrpC-6, TRPP8, trp-p8
Gene Description:
transient receptor potential cation channel subfamily M member 8
Target Gene Accession:
NM_024080.4(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
- temperature sensing is tightly linked to voltage-dependent gating in the cold-sensitive channel TRPM8 and the heat-sensitive channel TRPV1
- characterize the cold- and voltage-induced activation of TRPM8 channel in an attempt to identify the temperature- and voltage-dependent components involved in channel activation
- TRPM8 gene expression requires a functional androgen receptor.
- In conclusion, our results indicate that menthol induced steep outward rectification of TRPM8 results from the voltage-dependent open channel probability and the permeating ion-dependent modulation of the unitary channel conductance.
- results directly demonstrate that expression of TRPM8 in mammalian neurones induces cold sensing.
- TRPM8 may be an ER Ca(2+) release channel, involved in a number of Ca(2+)- and store-dependent processes in prostate cancer epithelial cells, including those that are important for prostate carcinogenesis, such as proliferation and apoptosis.
- investigated maturation of TRPM8 by identifying and mutating relevant N-linked glycosylation site and showing that glycosylation is neither essential for multimerization nor for transport to the plasma membrane
- TRPM8-independent menthol-induced Ca2+ release originates from both endoplasmic reticulum and Golgi compartments.
- TRPM8 is now best known as a cold- and menthol-activated channel implicated in thermosensation--{REVIEW}
- Expression TRPM8 in neuroendocrine tumor cells and its role in regulating [Ca(2+)](i) and NT secretion.
- The same regulatory events have opposing actions on TRPM8 and TRPV1 receptors. Anandamide and NADA are the first potential endogenous functional antagonists of TRPM8 channels.
- Prostate cancer (PCa) epithelial cells obtained from in situ PCa were characterized by a significantly stronger plasma membrane TRPM8-mediated current than that in normal cells.
- Study represent new tools to dissect TRPM8 functions and may serve as chemical leads for the development of additional TRPM8 agonists and novel antagonists.
- accumulation of TRPV1 and TRPV3 in peripheral nerves after injury, in spared axons, matches our previously reported changes in avulsed DRG.
- the transmembrane segment S6 has a role in determining cation versus anion selectivity of TRPM2 and TRPM8
- TRPM8 axons diffusely innervate the skin and oral cavity of TRPM8 transgenic mice, terminating in nerve endings mediating distinct perceptions of innocuous cool, noxious cold, and first- and second-cold pain.
- The expression of TRPM8 mRNA in the prostate was much higher than that in the bladder mucosa (3024:1), but was not found in the bladder muscle layer.
- activation of the TRPM8 variant in human lung epithelial cells leads to increased expression of IL-1alpha, -1beta, -4, -6, -8, and -13, granulocyte-macrophage colony-stimulating factor (GM-CSF), and TNF-alpha.
- TRPM8 variant receptor may function as a modulator of respiratory physiology caused by cold air, and may partially explain asthmatic respiratory hypersensitivity to cold air.
- TRPM8 plays a role in mechanisms that increase [Ca(2+)](i) needed for DBTRG cell migration.
- results reveal that a functional TRPM8 protein is expressed in human melanoma cells to involve the mechanism underlying tumor progression via the Ca(2+) handling pathway, providing us with a novel target of drug development for malignant melanoma
- Pore dilation occurs in TRPA1, but not in TRPM8 channels.
