Specific for the ~65k Munc-18 protein phosphorylated at Ser515. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide.
Munc-18 ( mammalian homologue of Unc-18) is a protein that is thought to be involved in regulating exocytosis due, at least in part, to it ability to bind syntaxin (Ciufo et al., 2005). Munc18-1 is a neuron-specific member of the Sec1/Munc18 protein family that binds to syntaxin1A and is thought to stabilize the complex (Liu et al., 2004). The function of Munc-18 is thought to be regulated by PKC phosphorylation of Ser515 on the Munc-18 protein (Sassa et al., 1996). Anti-Phospho-Ser515 Munc-18 Western blot of rat cortex lysate showing specific immunolabeling of the ~65k Munc-18 protein phosphorylated at Ser515. Immunolabeling is blocked by the phosphopeptide (peptide) used as antigen but not by the corresponding dephosphopeptide (not shown). .