Alomone Labs is pleased to offer the pH-Sensitive KCNK (K2P) Channel Antibody Explorer Kit (#AK-465). The Explorer Kit contains pH-sensitive KCNK channel antibodies, ideal for screening purposes.
|Product Name||Cat #||Size|
|APC-110||1 x 50 µl|
|APC-047||1 x 50 µl|
|APC-024||1 x 50 µl|
|APC-108||1 x 50 µl|
|APC-037||1 x 50 µl|
|APC-040||1 x 50 µl|
|APC-044||1 x 50 µl|
|APC-055||1 x 50 µl|
|APC-170||1 x 50 µl|
Two-pore domain potassium (K2P) channels have four transmembrane domains, two pore-forming loops between transmembrane domains 1 and 2 as well as 3 and 4, and a large extracellular linker region between transmembrane domain 1 and the first pore-forming loop, which forms the K+ selectivity filter.
The TASK subfamily of this group is highly sensitive to variations in extracellular pH. TASK-1, TASK-2 and TASK-3 homo- and heteromers are inhibited by extracellular acidification but are left unaffected by intracellular pH changes. Acid-induced inhibition of TASK channel activity enhances nerve excitability and thus indirectly indicates the presence of acid. The high proton sensitivity of the TASK channels suggests a role in surveillance of tissue acidification by ischemia, inflammation or back-diffusion of luminal acid.
TREK-1 and TREK-2 do not respond to changes in extracellular pH but are inhibited by intracellular alkalization and are activated by intracellular acidification such that they become constitutively active.
TRESK K2P member is blocked by extra- and intracellular acidification and is activated by extra and intracellular alkalization.
Additional pH-sensitive K2P channels include TWIK-1 and TWIK-2 which are inhibited by intracellular acidification, TRAAK channels that are activated by intracellular alkalization but not acidification and lastly, TALK-1 and TALK-2 are blocked by extracellular acidification but are gated open by extracellular alkalization1.
- Holzer, P. (2009) Handb. Exp. Pharmacol. 194, 283.