Selective blocker of SK2 (KCa2.2) channels

Tamapin is a peptide toxin isolated from the venom of the Indian red scorpion Mesobuthus Tamulus. Tamapin is amidated at its C-terminal tyrosine residue. Tamapin binds to small conductance Ca2+-activated K+ channels (SK channels) with high affinity and inhibits SK channel-mediated currents in pyramidal neurons of the hippocampus as well as in cell lines expressing distinct SK channel subunits. Contrary to Apamin or Leiurotoxin-1 (Scyllatoxin), Tamapin is an excellent toxin to discriminate among SK channel subtypes because it presents different affinities for SK1 (42 nM), SK2 (24 pM) and SK3 (1.7 nM) channels. This toxin is also the most potent SK2 channel blocker characterized so far (IC50 for SK2 channels = 24 pM).

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AA sequence: Ala-Phe-Cys3-Asn-Leu-Arg-Arg-Cys8-Glu-Leu-Ser-Cys12-Arg-Ser-Leu-Gly-Leu-Leu-Gly-Lys-Cys21-Ile-Gly-Glu-Glu-Cys26-Lys-Cys28-Val-Pro-Tyr-NH2
Disulfide bridges: Cys3-Cys21; Cys8-Cys26; Cys12-Cys28
Length (aa): 31
Formula: C146H237N44O41S6
Molecular Weight: 3459.00 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number: not available
Source: Synthetic
Purity rate: > 97 %






Small conductance Ca2+-activated K+ channels as targets of CNS drug development

Tamapin, a venom peptide from the Indian red scorpion (Mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and afterhyperpolarization currents in central neurons