| Post Translational Modifications | N-glycosylation is not essential for but facilitates cell surface expression, multimerization, association with lipid rafts and ion channel activity. |
| Function | Non-selective ion channel permeable to monovalent and divalent cations, including Na(+), K(+), and Ca(2+), with higher permeability for Ca(2+). Activated by multiple factors, such as temperature, voltage, pressure, and changes in osmolality. Activated by cool temperatures (<23-28 degrees Celsius) and by chemical ligands evoking a sensation of coolness, such as menthol and icilin, therefore plays a central role in the detection of environmental cold temperatures. TRPM8 is a voltage-dependent channel.its activation by cold or chemical ligands shifts its voltage thresholds towards physiological membrane potentials, leading to the opening of the channel. In addition to its critical role in temperature sensing, regulates basal tear secretion by sensing evaporation-induced cooling and changes in osmolality. |
| Protein Name | Transient Receptor Potential Cation Channel Subfamily M Member 8Long Transient Receptor Potential Channel 6Ltrpc-6Ltrpc6Transient Receptor Potential P8Trp-P8 |
| Database Links | Reactome: R-MMU-3295583 |
| Cellular Localisation | Cell MembraneMulti-Pass Membrane ProteinMembrane RaftLipid Raft Association Modulates Trpm8 Channel Activity |
| Alternative Antibody Names | Anti-Transient Receptor Potential Cation Channel Subfamily M Member 8 antibodyAnti-Long Transient Receptor Potential Channel 6 antibodyAnti-Ltrpc-6 antibodyAnti-Ltrpc6 antibodyAnti-Transient Receptor Potential P8 antibodyAnti-Trp-P8 antibodyAnti-Trpm8 antibodyAnti-Ltrpc6 antibodyAnti-Trpp8 antibody |
Information sourced from Uniprot.org
