A fully validated, highly specific rabbit polyclonal anti-serum to Serine-197 phosphorylated forms Calcineurin

Cytoplasmic Ca2+ binds to calmodulin and activates the phosphatase calcineurin (Cn) a 60 kDa protein, and CaM kinase II (CaMKII). One action of Cn is to dephosphorylate cytoplasmic NFAT (nuclear factor of activated T cells), inducing its translocation to the nucleus where it activates antiapoptotic and hypertrophic target genes. The phosphorylation of Cn at Phospho Ser-197 site has been observed in cultured neonatal rat ventricular myocytes (NRVMs) over-expressing constitutively active CAMKII. This appears to inhibit Cn activity which in turn prevents the dephosphorylation of NFAT and prevents activation of NFAT regulated genes.

Tested applications: Western blot (1:200 dilution). Species recognition: The antibody recognises Calcineurin in mouse/rat/human/monkey/other, when phosphorylated on Ser-197.