TRP Channel Assays
TRP channel (transient receptor potential channel) is a family of ion channels found mostly on the plasma membrane of a variety of animal cell types. The permeability of these ion channels to cations such as sodium, calcium, and magnesium is relatively non-selective.
Creative Biolabs offers the design and validation of TRP channel assays allowing for a significant improvement in throughput to facilitate drug development. We prioritized potential candidates and reduced the number of molecules that needed to be tested in the final stages, which is still the gold standard technology for this difficult medicine.
| Family | Background | Sub-Family |
| TRPV Assays | TRPV is named for the vanilloid chemicals that activate some of these channels. The interaction of these channels with chemicals like capsaicin has made them renowned. |
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| TRPA Assays | TRPA is named for the huge number of ankyrin repeats near the N-terminus. TRPA is located largely in afferent nociceptive nerve fibers and is linked to pain signaling amplification as well as cold pain hypersensitivity. |
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| TRPC Assays | TRPC is named from the fact that it is the most closely linked to Drosophila TRP, the TRP channel's namesake. TRPC channel mutations have been linked to respiratory disorders as well as focal segmental glomerulosclerosis in the kidneys. |
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| TRPM Assays | TRPM was discovered through a genomic comparison between normal and malignant nevi. TRPM channel mutations have been linked to hypomagnesemia with subsequent hypocalcemia. |
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Pharmacology
TRP channels mediate a wide range of sensations, including pain, temperature, various tastes, pressure, and vision. Some TRP channels in the body are thought to act as miniscule thermometers and are used by animals to detect heat and cold. TRPs are osmotic pressure, volume, stretch, and vibration sensors. TRPs have been discovered to play a multifaceted role in sensory signaling.
Structure
The S1–S6 membrane-spanning helices that make up TRP channels have intracellular N- and C-termini. Numerous post-transcriptional processes, including phosphorylation, G-protein receptor coupling, ligand-gating, and ubiquitination, are used to activate and regulate mammalian TRP channels. The receptors, which control ion entry, are present in almost all cell types and are primarily localized in cell and organelle membranes. When fully functional, most TRP channels form homo- or heterotetramers. The intricate arrangement of p-loops in the tetrameric protein, which are found in the extracellular domain between the S5 and S6 transmembrane segments, creates the ion selectivity filter, or pore. TRP channels, like the majority of cation channels, have negatively charged residues inside the pore to draw in positively charged ions.
