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Phospho-Ser603 Synapsin I Antibody
Affinity purified rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | P17599 |
| Reactivity | Rat |
| Predicted | Bovine, Human, Mouse, Xenopus, Zebrafish |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 78 KDa |
| Gene ID | 281510 |
|---|---|
| Gene Name | SYN1 |
| Other Names | Synapsin-1, Synapsin I, SYN1 |
| Target/Specificity | Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser603 conjugated to KLH. |
| Dilution | WB~~ 1:1000 |
| 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. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
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).
References
Bahler M, Greengard P (1987) Synapsin I bundles F-actin
in a phosphorylation-dependent manner. Nature (London)
326:704-707.
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)
84:7518-7522.
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-
4380.
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
2+
-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-
437.
McGuinness TL, Brady ST, Gruner JA, Sugimori M, L
linás RR, Greengard P (1989)
Phosphorylation-dependent
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
603
by p21-activated kinases (PAKs)
in vitro
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.
Garner (2008)
Piccolo modulation of Synapsin1a dynamics regulates synaptic vesicle exocytosis
.
J. Cell Biol., 181:
831 - 846.
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