pH-Sensitive KV Channel Antibody Explorer Kit,Alomone Labs,AK-470_KIT

K V 1.2 and K V 1.5 are pH sensitive. K V 1.5 currents are highly sensitive to acidic pH and decrease in amplitude by 46% at pH 6.3 and 96% at pH 5.3 when compared to current amplitude at pH 7.3. In contrary, K V 1.2 current amplitudes are relatively insensitive to an increase in proton concentration and only decrease by 3% at pH 6.3 and 17% at pH 5.3 when compared to currents at pH 7.3. Alkaline pH slightly increases K V 1.5 current amplitudes but does not seem to affect K V 1.2 current amplitudes. It is hypothesized that the reduction of K V 1.5 currents at pH 6.3 is caused by the accumulation of K V 1.5 wild-type channels in the C-type inactivated state. External acidification slows the recovery of K V 1.5 channels from inactivation by shifting the voltage dependence of activation of K V 1.5 to more depolarized voltages and increasing the time required to reach maximum current amplitude in response to depolarization. External acidification has little apparent effect on the rate of K V 1.2 recovery from inactivation. The K V 1.3 channel is also pH-sensitive and its properties are altered by acidic pH. Current amplitude and magnitude of inactivation of K V 1.3 is reduced by acidic extracellular pH, an affect hypothesized to be induced by protonation of a histidine residue located near the channel’s pore 1 . Other K V channels like K V 1.4 and K V 11.1 are also known to be pH-sensitive.