pH-Sensitive KV Channel Antibody Explorer Kit

A Screening Package of pH-Sensitive KV Channel Antibodies Economically Priced
  • Lyophilized Powder
  • Antigen Incl.
Cat #: AK-470
Sizes: 20 Vials
Last update: 24/04/2019

Alomone Labs is pleased to offer the pH-Sensitive KV Channel Antibody Explorer Kit (#AK-470). The Explorer Kit contains pH-sensitive KV channel antibodies, ideal for screening purposes.

For research purposes only, not for human use
Compounds
Product Name Cat # Size
Anti-KV1.2 (KCNA2) Antibody
APC-010 1 x 50 µl
Anti-KV1.2 (KCNA2) (extracellular) Antibody
APC-162 1 x 50 µl
Anti-KV1.3 (KCNA3) Antibody
APC-002 1 x 50 µl
Anti-KV1.3 (KCNA3) (extracellular) Antibody
APC-101 1 x 50 µl
Anti-KV1.4 Antibody
APC-007 1 x 50 µl
Anti-KV1.4 (extracellular) Antibody
APC-167 1 x 50 µl
Anti-KV1.5 (KCNA5) Antibody
APC-004 1 x 50 µl
Anti-KV1.5 (KCNA5) (extracellular) Antibody
APC-150 1 x 50 µl
Anti-KV11.1 (HERG) Antibody
APC-062 1 x 50 µl
Anti-KV11.1 (HERG) (extracellular) Antibody
APC-109 1 x 50 µl
Scientific Background
Scientific Background

KV1.2 and KV1.5 are pH sensitive. KV1.5 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, KV1.2 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 KV1.5 current amplitudes but does not seem to affect KV1.2 current amplitudes. It is hypothesized that the reduction of KV1.5 currents at pH 6.3 is caused by the accumulation of KV1.5 wild-type channels in the C-type inactivated state. External acidification slows the recovery of KV1.5 channels from inactivation by shifting the voltage dependence of activation of KV1.5 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 KV1.2 recovery from inactivation.

The KV1.3 channel is also pH-sensitive and its properties are altered by acidic pH. Current amplitude and magnitude of inactivation of KV1.3 is reduced by acidic extracellular pH, an affect hypothesized to be induced by protonation of a histidine residue located near the channel’s pore1.

Other KV channels like KV1.4 and KV11.1 are also known to be pH-sensitive.

References
  1. Steidl, J.V. and Yool, A.J. (1999) Mol. Pharmacol. 55, 812.
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