|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 Ser603 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 Ser603.Immunolabeling of the synapsin I band is blocked byλ-phosphatase treatment.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Ser603 Synapsin I Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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. Th e 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).
Bahler M, Greengard P (1987) Synapsin I bundles F-actin
in a phosphorylation-dependent manner. Nature (London)
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-
McGuinness TL, Brady ST, Gruner JA, Sugimori M, L
linás RR, Greengard P (1989)
inhibition by synapsin I of organelle movement in squid axoplasm. J Neurosci 9:4138-4149.
Nayak AS, Moore CI, Browning MD (1996) CAM kinase II phos
phorylation of the presyn
aptic protein synapsin is
persistently increased during expression of long-term po
tentiation. Proc Natl Acad Sci (USA) 93:15451-15456.
Sakurada K, Kato H, Nagumo H, Hiraoka H, Furuya K, Ikuhar
a T, Yamakita Y, Fukunaga K, Miyamoto E, Matsumura
F, Matsuo YI, Naito Y, Sasaki Y (2002) Synapsin I is phosphorylated at Ser
by p21-activated kinases (PAKs)
and in PC12 cells stimulated with bradykinin. J Biol Chem 277:45473-45479.
Sergio Leal-Ortiz, Clarissa L. Waites, Ryan Terry-Lorenzo
, Pedro Zamorano, Eckart D.
Gundelfinger, and Craig C.
Piccolo modulation of Synapsin1a dynamics regulates synaptic vesicle exocytosis
J. Cell Biol., 181:
831 - 846.
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