Phospho-Synapsin I (S9) Antibody Summary
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Phospho-Synapsin I (S9) by Western Blot. Western blot of rat brain lysate showing specific immunolabeling of the approximately 78 kDa Synapsin I phosphorylated at S9 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda PPase). The blot is identical to the control except that it was incubated in lambda PPase (1200 units for 30 minutes) before being exposed to the anti-phospho-S9 Synapsin I. The immunolabeling is completely eliminated by treatment with lambda PPase.
Preparation and Storage
Background: Synapsin I
Synapsin I is an 85 kDa neuron-specific, O-GlcNAcylated phosphoprotein that interacts with synaptic vesicles and regulates neurotransmitter release. It is concentrated in presynaptic terminals where it anchors synaptic vesicles to the underlying cytoskeleton. Phosphorylation at various sites reduces synapsin I binding to neurosecretory vesicles, making them available for neurotransmitter release. Rat synapsin I is 704 amino acids (aa) in length and contains five domains, named A - E/F. Domains A - D lie between aa 1 - 655, while E and F are alternate splice forms. Domain A (28 aa) regulates neurotransmitter release in a phosphorylation-dependent manner. Domains C (328 aa) and E (49 aa) anchor to actin in the synaptic region. Domains B (84 aa) and D (235 aa) promote actin and secretory vesicle interaction, and actin nucleation. Phosphorylation of S603 and 566 in domain D, and S9 in domain A, reduces the affinity of synapsin I for actin and secretory vesicles.
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- Cole, R.N. and G.W. Hart (1999) J. Neurochem. 73:418.
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