RCAN2 Human

RCAN2 is expressed in multiple isoforms, which differ at their N-terminus. The longer isoform (isoform 1) is expressed exclusively in the brain, while the shorter isoform (isoform 2) is ubiquitously expressed, with the highest levels found in the brain, heart, and muscle . Both isoforms bind to the catalytic subunit of calcineurin and inhibit its activity, although they differ in their C-terminal regions .

RCAN2 functions as an endogenous inhibitor of calcineurin. By binding to calcineurin, RCAN2 prevents the dephosphorylation of its substrates, thereby modulating various signaling pathways. This regulation is essential for maintaining cellular homeostasis and responding to changes in intracellular calcium levels .

Recent studies have identified RCAN2 as a centriolar protein involved in the regulation of cilia length. Cilia are microtubule-based structures that play a critical role in cell signaling and sensory functions. Defective cilia function can lead to a group of disorders known as ciliopathies, which are characterized by developmental defects affecting multiple tissues . RCAN2 localizes to centrioles and the basal body, and its expression is required to maintain normal cilia length .

RCAN2 is located near the minimal supernumerary fragment of chromosome 21, which is associated with Down syndrome. This suggests that RCAN2 may play a role in the pathophysiology of Down syndrome . Additionally, the regulation of calcineurin by RCAN2 is implicated in various diseases, including cardiac hypertrophy, neurodegenerative disorders, and immune system dysfunctions .

Human recombinant RCAN2 is produced using an expression system, typically in E. coli, and is purified for research purposes. It is used in various experimental applications, including blocking assays, immunohistochemistry, and Western blotting . The recombinant protein is often tagged for easy detection and purification, and it is stored under specific conditions to maintain its stability and activity .