Synapsin I Antibody (Phospho-Ser603)

Polyclonal Antibody

Wet Ice

The antibody has been directly tested for reactivity in Western blots with rat tissue. It is anticipated that the antibody will react with bovine, human, mouse, Xenopus and zebra fish tissue based on the fact that these species have 100% homology with the amino acid sequence used as antigen.
Western blot of rat cortex lysate showing specific immunolabeling of the ~78k synapsin I phosphorylated at Ser603 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda -Ptase). The blot is identical to the control except that it was incubated in lambda -Ptase (1200 units for 30 min) before being exposed to the phospho-Ser603 synapsin I antibody. The immunolabeling is completely eliminated by treatment with lambda -Ptase.

Liquid. 100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

Synapsin I plays a key role in synaptic plasticity in brain (Feng et al., 2002; Nayak et al., 1996). This effect is due in large part to the ability of the synapsins to regulate the availability of synaptic vesicles for release. The role of synapsin in synaptic plasticity and in synaptogensis is regulated by phosphorylation (Jovanovic et al., 2001; Kao et al., 2002). Serine 603 is the site on synapsin I that is phosphorylated by calcium calmodulin kinase II and by p21-activated kinases (Sakurada et al., 2002; Czernik et al., 1987). Phosphorylation of this site is thought to regulate synaptic vesicle function (Nayak et al., 1996; Bahler and Greengard, 1987; McGuinness et al., 1989).

Synapsin-1

Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.

Cow; Human; Mouse; Rat; Zebrafish