P3495
Phrixotoxin-2
>98% (HPLC), lyophilized powder
Synonym(s):
κ-TRTX-Ps1b, PaTX2
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About This Item
Recommended Products
Amino Acid Sequence
Tyr-Cys-Gln-Lys-Trp-Met-Trp-Thr-Cys-Asp-Glu-Glu-Arg-Lys-Cys-Cys-Glu-Gly-Leu-Val-Cys-Arg-Leu-Trp-Cys-Lys-Arg-Ile-Ile-Asn-Met
Features and Benefits
This compound is featured on the Potassium Channels page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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S Diochot et al.
British journal of pharmacology, 126(1), 251-263 (1999-03-02)
1. In the present study, two new peptides, phrixotoxins PaTx1 and PaTx2 (29-31 amino acids), which potently block A-type potassium currents, have been purified from the venom of the tarantula Phrixotrichus auratus. 2. Phrixotoxins specifically block Kv4.3 and Kv4.2 currents
Ryan C Smith et al.
Reproductive biology and endocrinology : RB&E, 5, 41-41 (2007-11-06)
Uterine smooth muscle cells exhibit ionic currents that appear to be important in the control of uterine contractility, but how these currents might produce the changes in contractile activity seen in pregnant myometrium has not been established. There are conflicting
Natalie J Saez et al.
Toxins, 2(12), 2851-2871 (2011-11-10)
Spiders are the most successful venomous animals and the most abundant terrestrial predators. Their remarkable success is due in large part to their ingenious exploitation of silk and the evolution of pharmacologically complex venoms that ensure rapid subjugation of prey.
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