Anti-STRN3 from rabbit

Striatin-3 (UniProt: Q13033; also known as Cell cycle autoantigen SG2NA, S/G2 antigen) is encoded by the STRN3 (also known as GS2NA, SG2NA) gene (Gene ID: 29966) in human. Striatin-3 is a calmodulin-binding protein that bonds calmodulin a calcium dependent manner and may function as scaffolding or signaling protein. Two isoforms of Striatin-3 have been reported that are produced by alternative splicing. Its calmoduln-binding region is located within amino acids 166-183. It also contains a caveolin-binding region (aa 71-79), six WD repeats, and a coiled coil region (aa 77-136). The coiled coil domain and the PP2A subunit can form a stable core complex with a 2:2 stoichiometry. The coiled coil domain of striatin-3 is a novel type of PP2A regulatory subunit that functions as a scaffold for the assembly of the STRIPAK complex. PP2A and certain kinases, such as germinal central kinase III (GCKIII) interact with striatin to form striatin-interacting phosphatase and kinase (STRIPAK) complex that are known to regulate multiple cellular events. Wild-type striatin-3 is shown to strongly suppress apoptosis in Jurkat cells induced by the GCKIII kinase MST3. However, mutant forms of striatin-3 fail to exhibit this effect. (Ref.: Lu, Q., et al. (2004). Proc. Natl. Acad. Sci. USA 101(49); 17126-17131; Chen, C., et al. (2014). J. Biol. Chem. 289(14); 9651-61).