Anti-Phospho-Synapsin I (Ser9) Syn1 Antibody

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. In addition to its role in plasticity, the expression of synapsin I is a precise indicator of synapse formation (Moore and Bernstein, 1989; Stone et al., 1994) . Thus, synapsin I immunocytochemistry provides a valuable tool for the study of synaptogenesis. The role of synapsin in synaptic plasticity and in synaptogenesis is regulated by phosphorylation (Jovanovic et al., 2001; Kao et al., 2002) . Serine 9 is the site on synapsin I that is phosphorylated by cAMP-dependent protein kinase and by calcium calmodulin kinase I (Czernik et al., 1987) . Phosphorylation of this site is thought to regulate synaptic vesicle function and neurite outgrowth (Kao et al., 2002) .

Brain protein 4.1 antibody, SYN 1 antibody, SYN 1a antibody, SYN 1b antibody, SYN I antibody, SYN1 antibody, SYN1_HUMAN antibody, SYN1a antibody, SYN1b antibody, Synapsin 1 antibody, Synapsin I antibody, Synapsin-1 antibody, Synapsin1 antibody, SynapsinI antibody, SYNI antibody

Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 of rat synapsin, conjugated to keyhole limpet hemocyanin (KLH) . Immunogen species is Rat.

Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. Regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxide functions at a presynaptic level.

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. After date of receipt, stable for at least 1 year at -20°C.

Specific for endogenous levels of the ~78 kDa synapsin I doublet protein phosphorylated at Ser9. Also weakly labels the ~55 kDa synapsin II protein which has a similar phosphorylation site to that of Ser9 on synapsin I. Immunolabeling is completely eliminated by treatment with λ-phosphatase.