So far, two EAG isoforms Eag1 (KCNH1, Kv10.1) and Eag2 (KCNH5, Kv10.2) have been identified and they show similar electrophysiological features such as slow voltage-dependent activation, noninactivating, and inhibition by intracellular [Ca.sup.2+] [[[Ca.sup.2+]].sub.i] [4, 6, 7].
E65 causes an overall reduction in KV10.1 protein level and also reduces single channel current, whereas E70 mainly affected the glycosylation pattern but without detectably affecting the electrophysiological parameters .
Pardo, "Kv10.1 [K.sup.+] channel: from physiology to cancer," Pflugers Archiv European Journal of Physiology, vol.
Alves, "In vivo imaging of tumour xenografts with an antibody targeting the potassium channel Kv10.1," European Biophysics Journal, vol.
Sanchez et al., "Alternatively spliced isoforms of Kv10.1 potassium channels modulate channel properties and can activate cyclin-dependent kinase in Xenopus oocytes," The Journal of Biological Chemistry, vol.
Farsi et al., "Kv10.1 opposes activity-dependent increase in [Ca.sup.2+] influx into the presynaptic terminal of the parallel fibre-Purkinje cell synapse," Journal of Physiology, vol.