(Honey Bee, Apis mellifera)
4364-s 0.1 mg | 130.00 EUR
Ala- Leu- Cys- Asn- Cys- Asn- Arg- Ile- Ile- Ile- Pro- His- Met- Cys- Trp- Lys- Lys- Cys- Gly- Lys- Lys- NH2
Synthetic Product (disulfide bonds between Cys3– Cys14 and Cys5– Cys18 )
The purity is guaranteed to be higher than 99% by HPLC
Tertiapin, a high-affinity inhibitor for inward-rectifier K+ channels
Tertiapin, a 21 amino acid residue peptide was originally isolated from honey bee venom and has been described recently as a novel K+ channel blocker.
Tertiapin blocks a G protein-gated channel (GIRK1/4) and the ROMK1 channel with nanomolar affinity.
About selectivity, tertiapin is insensitive to IRK1-channel, a closely related channel to GIRK1/4 and the ROMK1. Tertiapin will be a very useful tool for studying the physiological and the structure-function relationship of these channels.
Inward-rectifier K+ channels accomplish many important and diversified biological roles. Thus far, there are no high-affinity inhibitors that directly target any inward-rectifier K+ channels. Only Lq2, scorpion toxin, blocks the ROMK1 inward-rectifier K+ channel, but the affinity is rather low (Kd = 0.4 mM) [Biochemistry, 36, 6936 (1997)].
- W. Jin and Z. Lu, Biochemistry, 37, 13291 (1998) (Original; Pharmacol.)
- X. Xu and J.W. Nelson, Proteins Struct. Funct. Genet., 17, 124 (1993) (Structure of Tertiapin; S-S Bond)