Voltage gate K+ (KV) channels form functional entities by the assembly of four a subunits and auxiliary subunits. Various auxiliary subunits are known to interact with KV channels thereby modulating various properties such as gating, activation and inactivation of the channels as well as influence the trafficking of the channels to the cell’s plasma membrane1.
KChIPs (KV Channel Interacting Proteins) are cytoplasmic proteins which belong to the neural Ca2+ sensor (NCS) family of Ca2+ binding EF-hand proteins. To date, KChIP1-4 have been identified. All four KChIPs have a conserved C-terminal domain, which has four EF-hand-like Ca2+ binding motifs. The N-terminal region is differs among the various KChIPs and attributes different properties regarding the regulation of KV channels1. KChIPs regulate different properties of KV channels such as their cell surface expression (mediated by proper trafficking of the various subunits), channel assembly and gating1-4. Specifically, KChIP1 strongly regulates the activity of the KV4 channel family1. KChIP1 has also been found to assist GABA-mediated IPSCs (inhibitory postsynaptic currents) by increasing the release of presynaptic transmitter5. Furthermore, KChIP knockout mice display an increase in anxiety-like behavior compared to their wild type counterparts5.
KChIP1, 3, and 4 are mostly expressed in the brain while KChIP2 is expressed in the heart and in the brain4-6.
Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of rat KChIP1. Anti-KChIP1 antibody (#AG1081) can be used for Western blot analysis. It has been designed to recognize KChIP1 from human mouse and rat samples.
