- CITATIONS: 1
|Application ||WB, IHC|
|Predicted||Bovine, Human, Mouse, Xenopus, Zebrafish|
|Calculated MW||78 KDa|
|Other Names||Synapsin-1, Synapsin I, SYN1|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 conjugated to KLH.|
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||Specific for ~78k synapsin I doublet protein phosphorylated at Ser9. Theantibody also weakly labels the ~55k synapsin II protein which has a similar phosphorylationsite to that of Ser9on synapsin I. Immunolabeling is blocked by preadsorption of the antibodywith the phosphopeptide used as antigen but not by the corresponding dephosphopeptide.Immunolabeling is also completely eliminated by treatment withλphosphatase.|
|Precautions||Phospho-Ser9 Synapsin I Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
Provided below are standard protocols that you may find useful for product applications.
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 plasti city, 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 phosphor ylation (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).
Czernik AJ, Pang DT, Greengard P (1987) Amino acid
sequences surrounding the cAMP-dependent and
calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I. Proc Natl Acad Sci (USA)
Feng J, Chi P, Blanpied TA, Xu YM, Magarinos AM, Fe
rreira A, Takahashi RH, Kao HT, McEwen BS, Ryan TA,
Augustine GJ, Greengard P (2002) Regulation of neurotransmitter release by synapsin III. J Neurosci 22:4372-
Jovanovic JN, Sihra TS, Nairn AC, Hemmings HC, Jr., Gr
eengard P, Czernik AJ (2001) Opposing changes in
phosphorylation of specific sites in synapsin I during Ca
-dependent glutamate release in isolated nerve
terminals. J Neurosci 21:7944-7953.
Kao HT, Song HJ, Porton B, Ming GL, Hoh J, Abraham M,
Czernik AJ, Pieribone VA, Poo MM, Greengard P (2002) A
protein kinase A-dependent molecular switch in synapsin
s regulates neurite outgrowth. Nature Neurosci 5:431-
Moore RY, Bernstein M (1989) Synaptogenesis in the rat suprachiasmatic nucleus demonstrated by electron
microscopy and synapsin I immunoreactivity. J Neurosci 9:2151-2162.
Nayak AS, Moore CI, Browning MD (1996) CaM Kinase II
phosphorylation of the presyn
aptic protein synapsin is
persistently increased during expression of long-term po
tentiation. Proc Natl Acad Sci (USA) 93:15451-15456.
Stone LM, Browning MD, Finger TE (1994) Differential dist
ribution of the synapsins in the rat olfactory bulb. J
Sachiko Shimomura, Tadashi Nagamine, Naoya Hatano, Noriyuki Sueyoshi, and Isamu Kameshita (2010)
Identification of an endogenou
s substrate of zebrafish doublecortin-like
protein kinase using a highly active
147: 711 - 722.
Note: Dr. Michael Browning co-author of t
he cited papers is the President and founder of
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