KChIPs belong to the family of small cytosolic calcium-binding proteins and consists of four different KChIP isoform ranging between 216 and 270 amino acids. They all have a reasonably conserved core region of 185 amino acids and a heterogeneous N-terminal. KChIPs have calcium-binding EF hands which appear important for modulation KV channels but not for CaV channels.nThe cardiac KChIP2 gene generates three protein isoforms of 220, 252, and 270 amino acids via alternative splicing of exons 2 and 3. It is well established that KChIP2 functionally increases peak KV4 current, slows channel inactivation and accelerates recovery from inactivation. Furthermore, KChIP2 has been reported to increase I Ca ,L and suggested to decrease KV1.5 cell surface expression and facilitate INa