Anti-Connexin 35/36 (Ser276) Antibody

Connexin 35/36 is the most abundant gap junction protein in the central nervous system. Connexin gap junction coupling in the retina has been shown to be regulated by light exposure and neurotransmitter signaling, but more recently has been observed to also depend on direct phosphorylation of connexin (Ouyang et al., 2005, Patel et al., 2006). PKA phosphorylation of Ser110 in the intracellular loop and Ser276 in the C-terminal domain can cause uncoupling of connexin 35 gap junctions (Ouyang et al., 2005). The largest uncoupling effect is seen when both of these sites are phosphorylated, with a much smaller degree of uncoupling observed when only one is phosphorylated (Kothmann et al., 2007). C-terminal domain phosphorylation of connexin 35 at Ser276 is observed in teleost, amphibian, and avian species, with connexin 36 phosphorylation at Ser293 being the mammalian equivalent.