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Phospho-Ser549 Synapsin I Antibody
Affinity purified rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC |
|---|---|
| Primary Accession | P17599 |
| Reactivity | Rat |
| Predicted | Bovine, Human, Mouse, Monkey |
| 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 Ser549 conjugated to KLH. |
| Dilution | WB~~ 1:1000 IHC~~ 1:500 |
| Format | Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephospho-peptide affinity columns. |
| Antibody Specificity | Specific for ~78k synapsin I doublet phosphorylated at Ser549.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-Ser549 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 ab ility of the synapsins to regulate the availability of synaptic vesicles for release. The role of synapsin in synaptic plasticity and in synaptogensis is regulated by phosphorylation (Jovanovic et al., 2001; Kao et al., 2002). Ser 549 along with Ser 62 and Ser 67 are the sites of synapsin I that are phosphorylated by MAP kinase (Jov anovic et al., 1996). Phosphorylation and subsequent dephosphorylation of this site is thought to play a key role in synaptic vesicle trafficking.
References
Jovanovic JN, Benfenati, F, Siow YL, Sihra TS, Sanghera JS, Pelech SL, Greeng
ard P,Czernik AJ (1996)
Neurotrophins stimulate phosphoryl
ation of Synapsin I by MAP kinase and regulate Synapsin
I-actin interactions. Neurobiology 93:3679-3683.
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.
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.
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