Selective blocker of ClC2 (CLCN2) chloride channels

GaTx2 (gating modifier of anion channels 2) was isolated from the venom of Leiurus quinquestriatus hebraeus. GaTx2 is the most potent peptide inhibitor of ClC-2 (CLCN2) chloride channel ever described. Kd value is close to 20 pM. GaTx2slows ClC-2 activation but without altering channel conductance. The effect is voltage-dependent. This inhibitory effect was highlighted on rabbit ClC-2 channels expressed in oocytes. It has no effect on ClC-0, ClC-1, ClC-3, ClC-4, CFTR, GABAC, Xenopus ClCa, Shaker B or Kv1.2 channels. Structurally, GaTx2 is composed of two β-strands and one α-helix.This peptide is also called Leiuropeptide II. Bears 89, 93 and 96% identity with OdK1, neurotoxin PO1 and leiuropeptide III, respectively.

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AA sequence: Val-Ser-Cys3-Glu-Asp-Cys6-Pro-Asp-His-Cys10-Ser-Thr-Gln-Lys-Ala-Arg-Ala-Lys-Cys19-Asp-Asn-Asp-Lys-Cys24-Val-Cys26-Glu-Pro-Ile-OH
Disulfide bonds between: Cys3-Cys19, Cys6-Cys24, and Cys10-Cys26
Length (aa): 29
Formula: C125H199N39O47S6
Molecular Weight: 3191.25 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number: not available
Source: Synthetic
Purity rate: > 98 %


Dual activation of CFTR and CLCN2 by lubiprostone in murine nasal epithelia

Isolation and characterization of a high affinity peptide inhibitor of ClC-2 chloride channels