|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||74111 Da|
|Other Names||Synapsin-1, Brain protein 41, Synapsin I, SYN1|
|Target/Specificity||A synthetic phospho-peptide corresponding to residues surrounding serine 9 of human synapsin I protein.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|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||Synapsin I Antibody Phospho (pS9) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level.|
|Cellular Location||Cell junction, synapse. Golgi apparatus|
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Provided below are standard protocols that you may find useful for product applications.
Synapsin I is a member of neuron-specific phosphoproteins that associate with synaptic vesicles (1). Three mammalians synapsins have been identified, Synapsin I, II and III. Generated by differential splicing, Synapsin Ia and Synapsin Ib differ in their Carboxyl termini (2). Synapsin I also functions in binding synaptic vesicles to several elements of the cytoskeleton including actin filaments, microtubules and spectrin. (3) Fairly abundant protein of the brain (0.4%), Synapsin I is best known to be CaM kinase II substrate in addition to cAMP-dependent protein kinase. (4) Phosphorylation at site Ser 566 and Ser 603 by CaM kinase II will cause a 5 fold decrease in the affinity of synaptic vesicles binding. A phosphorylation of serine 9 on synapsin amino-terminal can lead to inhibition in its binding to phospholipids and dissociation of synapsins from synaptic vesicles.
1. Greengard P., et al. Science 259:780
3. Bahler M, Greengard P, Nature 326:704
4. Huttner WB., et al. J Biol Chem 256:1482
5. Schiebler, W, et al. J. Biol Chem. 261, 8383-8390, 1986.
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