TRPM8 antibody

Background of TRPM8 antibody

Dorsal root ganglion (DRG) are receptive of environmental stimuli such as temperature and pressure by molecular markers, for temperature the DRG neurons have thermo transient potential receptors (TRPs) are members of the transient receptor potential family of ion channels and are gated by shifts in temperature. TRPM8 is activated by cooling, and TRPM8-deficient mice have severe deficits in cool thermosensation (1). The ion channels carrying the stimulus-activated receptor current in sensory neurons have been identified and the mechanism of their activation elucidated, for a variety of sensory systems and for species ranging from worms and flies to humans. In physiological terms the Transient Receptor channels should be a non-selective cation channel that is permeable to all the alkali cations and to many divalent cations. The channel has a particularly high calcium permeability, passing Ca2+ at least 10 times better than Na+ at the same time, Ca2+ in millimolar concentrations acts as a partial blocker, inhibiting current by monovalent ions. Most eukaryotic genomes include a substantial repeat-rich fraction termed heterochromatin, which is concentrated in centric and telomeric regions. The repetitive nature of heterochromatic sequence makes it difficult to assemble and analyze. To better understand the heterochromatic component of the Drosophila melanogaster genome, the entire transposable region was annotated for a whole-genome shotgun sequence assembly. The shot gun sequence assembly analyses predicted 297 protein-coding genes and six non-protein-coding genes, including known heterochromatic genes, and regions of similarity to known transposable elements (1). One of these genes code for a protein called transient receptor potential (Trp). The transient receptor potential gene is referred to in FlyBase by the symbol trp (CG7875, FBgn0003861). It has the cytological map location 99C6-99C7. Its sequence location is 3R:25740242: 25746011. There are at least one more subtype is known to exist as TrpA1.
Trpm8 is a 1104 amino acid protein, containing 8 TMDs and is a calcium ion channel component; its function is described in modulation of calcium channel activity. It also regulates calcium calmodulin and intracellular ligand-gated calcium channel and store-operated calcium channels. The physiological functions associated with Trp include modulation in the light activated voltage-gated channel activity, calcium ion transport in response to light stimulus and in light induced release of cytosolic sequestered calcium ion. Physiologically, trp involvement is also studied in calcium-mediated signaling; phototransduction; phospholipase C inhibition. There are 29 alleles are reported in literature, the phenotypes of these alleles are annotated with: photoreceptor; photoreceptor cell; antenna; rhabdomere; ommatidium; retina. It has one annotated transcript and one annotated polypeptide. Trp undergoes phosphorylation for activation at position. There are number of human homolog for the fly Trp channels including TRPN1, TRPV4, TRPML3 and TRPA1 (2).