Overview
- Peptide TLNFVEFNLEKHRS(C), corresponding to amino acid residues 185-198 of human KV11.2 (erg2) (Accession Q9H252). Intracellular, N-terminal part.
- Rat brain and cortex lysate (1:200).
Western blot analysis of rat brain (1 and 3) and cortex (2 and 4) lysate:1,2. Anti-KCNH6 (erg2) Antibody (#APC-114), (1:200).
3,4. Anti-KCNH6 (erg2) Antibody, preincubated with KCNH6/erg2 Blocking Peptide (#BLP-PC114).
- Rat brain sections. Mouse vomeronasal organ (VNO) (1:250) (Hagendorf, S. et al. (2009) J. Neurosci. 29, 206.).
KV11.2 (erg2) is a member of the ether-a-go-go (EAG) subfamily of voltage-dependent K+ channels. The erg subfamily includes the closely related proteins KV11.1 (erg1) and KV11.3 (erg3) that possess the signature structure of the voltage-dependent K+ channels: six membrane-spanning domains with intracellular N- and C-termini. As with all voltage-dependent K+ channels, the functional channel is a tetramer composed of four subunits. It has been suggested that the KV11 subfamily members can form functional heteromultimers within the subfamily.
KV11.2 produces currents characterized by strong inward rectification with slow activation and very rapid inactivation kinetics, which closely resemble those produced by the much studied channel KV11.1.
The expression of KV11.2 seems to be limited to the brain and the pituitary gland. The same is true for the KV11.3 protein, while KV11.1 is more widely expressed.
From a pharmacological point of view, KV11.2 channels can be blocked by well characterized organic blockers such as the anti-arrhythmic drug E-4031. In addition, the peptide toxins Ergtoxin-1 and BeKm-1 block KV11.2 with different potencies.
