|Tested species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 of rat SYN1 conjugated to KLH|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1,000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody is predicted to react with bovine, human, mouse, Xenopus and zebrafish based on 100% sequence homology.
In Western blot, this antibody detects an ~78 kDa protein representing Phospho-Ser9 Synapsin protein. It also weakly labels the ~ 55 kDa Synapsin II protein which has a similar phosphorylation site to that of SER9 on Synapsin I.
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).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.