Anti-Phospho-Ser<sup>9</sup> Synapsin I

Specific for ~78k synapsin I doublet protein phosphorylated at Ser9. The antibody also weakly labels the ~55k synapsin II protein which has a similar phosphorylation site to that of Ser9 on synapsin I. Immunolabeling is blocked by preadsorption of the antibody with the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. Immunolabeling is also completely eliminated by treatment with lambda phosphatase. Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.

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SPECIFICATIONS

Size

100 ul

Applications

IHC, WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat, Bov, ZF/Fish

Format

Affinity purified, polyclonal antibody

Presku

OAPC00196

Target

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. In addition to its role in plasticity, the expression of synapsin I is a precise indicator of synapse formation (Moore and Bernstein, 1989; Stone et al., 1994). Thus, synapsin I immunocytochemistry provides a valuable tool for the study of synaptogenesis. The role of synapsin in synaptic plasticity and in synaptogensis is regulated by phosphorylation (Jovanovic et al., 2001; Kao et al., 2002). Serine 9 is the site on synapsin I that is phosphorylated by cAMP-dependent protein kinase and by calcium calmodulin kinase I (Czernik et al., 1987). Phosphorylation of this site is thought to regulate synaptic vesicle function and neurite outgrowth (Kao et al., 2002).

Weight

~78kDa

Gene Id

281510