TRPV1 Protein, Human (Cell-Free, His)

TRPV1 is a nociceptive and temperature-sensitive non-selective cation channel belonging to the transient receptor potential vanillic acid channel subfamily, and is a multimodal signal integrator. TRPV1 is mainly expressed in peripheral sensory neurons, and is also widely distributed in various neural and non-neuronal cells, including immune cells, pancreatic β cells, muscle cells, and adipocytes. The TRPV1 structure includes six transmembrane domains, an intracellular N-terminus with ankyrin repeat sequences, an intracellular C-terminus, and a central pore region mediating channel activation and ion selection. The functional activity of TRPV1 is regulated by phosphorylation, dephosphorylation, PI(4,5)P2 binding, kinases, and calmodulin. Upon activation, TRPV1 primarily mediates extracellular calcium ion influx, inducing sensory neuronal depolarization, action potential firing, and neurogenic inflammation, mediating the occurrence and amplification of pain. Sustained or repeated activation of TRPV1 produces a desensitization effect, preventing calcium ion overload from damaging neurons, thereby exerting an analgesic effect. TRPV1 is widely involved in physiological and pathological processes such as pain perception, thermoregulation, osmolarity regulation, coughing, and bladder overactivity. TRPV1 is a core pathway for temperature and pain perception in mammals, and its discovery was awarded the 2021 Nobel Prize in Physiology or Medicine ^[1][2][3][4].

TRPV1 Protein, Human can be activated by Capsaicin (HY-10448), olivani, resin toxin, and arachidonic acid ethanolamine in SH-SY5Y_hTRPV1 cells, increasing the intracellular calcium ion concentration, with corresponding EC₅₀ values of 2.9 nmol/L, 34.7 nmol/L, 0.9 nmol/L, and 4.6 μmol/L, respectively. Capsaicin and iodoresin toxin can inhibit TRPV1 Protein, Human, blocking the agonist-induced increase in calcium ions, with K_B values of approximately 70 nmol/L and 2 nmol/L, respectively^[3].
TRPV1 Protein, Human, after activation by Capsaicin (EC₅₀ = 0.6 nmol/L), can induce SH-SY5YhTRPV1 cells to release pre-labeled [³H] norepinephrine, and the increase in intracellular calcium ions precedes the release of neurotransmitters^[3].
Protein, Human, after activation by Capsaicin (EC₅₀ = 155 nmol/L; 24 h), causes delayed cytotoxicity in SH-SY5Y hTRPV1 cells. Capsazepine (HY-15640) and ruthenium chloride can eliminate this toxicity by inhibiting TRPV1^[3].
TRPV1 Protein, Human was heterologously expressed in HEK293 cells. Capsaicin (132-275 nM) and arachidonic acid ethanolamine (1.5-4.8 μM) could be activated at 22℃ and 37℃ and increase intracellular calcium ion levels. The corresponding pEC₅₀ of capsaicin were 6.88 and 6.77, respectively^[4].