Every lot is tried & tested in a relevant biological assay.
- King, J.V.L. et al. (2019) Cell 178, 1362.
- Alomone Labs Wasabi receptor toxin leads to Ca2+ signals in HEK 293 cells transfected with TRPA1.A. Upper, individual traces (grey) and mean trace (black) of changes in intracellular Ca2+ concentration with time (measured as a change in FURA-2AM fluorescent intensity) in HEK 293 cells transfected with human TRPA1, following application of 5 µM Wasabi receptor toxin (#STW-200) followed by 200 µM AITC. Bottom, Mean ± SEM of changes in intracellular Ca2+ in HEK 293 cells transfected with human TRPA1, following application of 5 µM Wasabi receptor toxin followed by 200 µM AITC. n = 42 cells, representative of 5 plates. B. Same as in A, but in untransfected HEK 293 cells. Ionomycin was added at the end of each experiment. n = 60 cells, representative of 3 plates.
Figure kindly provided by Prof. Alexander Binshtok, Dept. Medical Neurobiology, Institute for Medical Research, IMRIC, Hebrew University School of Medicine, Jerusalem.
Wasabi receptor toxin (WaTx) is a peptide toxin originally isolated from Urodacus manicatus (Australian Black Rock scorpion) venom. The peptide toxin activates TRPA1 channel by a novel mechanism: it penetrates the cell and stabilizes the channel’s open state, thereby causing pain1.
TRPA1 ion channel is a chemosensory receptor for a broad class of volatile environmental irritants. It is expressed in sensory neurons and activated by natural products from mustard and allium plants. This activation elicits the sinus clearing or eye stinging pain one experiences when eating wasabi or chopping an onion2.
TRPA1 is also a sensor for endogenous inflammatory agents that directly activate this channel to produce acute and persistent pain2. TRPA1 is considered a promising therapeutic target for treating chronic pain, itch, and neurogenic inflammatory syndromes3.
Wasabi Receptor Toxin (#STW-200) is a highly pure, synthetic, and biologically active peptide toxin.