Overview
- Peptide (C)RLHKKLGTEEFP(G), corresponding to amino acid residues 234 - 245 of rat Synapsin-1 (Accession P09951). Intracellular, region C.
Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain synaptosomal fractions:1,2. Anti-Synapsin I (SYN1) Antibody (#ANR-014), (1:400).
3,4. Anti-Synapsin I (SYN1) Antibody, preincubated with Synapsin I/SYN1 Blocking Peptide (#BLP-NR014).
Expression of Synapsin-1 in mouse cerebellumImmunohistochemical staining of perfusion-fixed frozen mouse brain sections using Anti-Synapsin I (SYN1) Antibody (#ANR-014), (1:400), followed by anti-rabbit-Alexa-488 antibody. Synapsin-1 staining (green) appears in Purkinje cell bodies (horizontal arrows) and in segments of the dendritic tree (vertical arrows). Nuclei are stained with DAPI (blue).
- Cruceanu, C. et al. (2013) Neuropsychopharmacology 38, 239.
- Fiumara, F. et al. (2007) J. Cell Sci. 120, 3228.
- Bennett, A.F. et al. (1991) Biochem. J. 276, 793.
- Hall, F.L. et al. (1990) J. Biol. Chem. 265, 6944.
- Yamagata, Y. (2003) J. Pharmacol. Sci. 93, 22.
Synapsins are a family of synaptic vesicle associated phosphoproteins consisting of three members: SYN1, SYN2, and SYN3, with several alternative splicing leading to 10 different isoforms. They are involved in synaptic transmission and plasticity, several stages of neurodevelopment, such as axon outgrowth and synapse formation. Synapsins are localized in presynaptic nerve terminals of central neurons1.
Synapsin I is a peripheral membrane protein of synaptic vesicles that is phosphorylated at least at three different sites by various protein kinases. All synapsins have a single phosphorylation site in the short N-terminal domain A (site 1) that regulates neurite elongation and synaptic vesicle mobilization2.
Synapsin I exhibits an asymmetric structure and exists in two forms, designated synapsin Ia and synapsin Ib. The primary structure of synapsin I is highly conserved, 95% of the protein’s residues are invariant and contain two major structural domains. The protein is divided into a hydrophobic, collagenase resistant head region and a proline rich, collagenase sensitive tail3,4.
Synapsin I has been suggested to play an important role in the regulation of neurotransmitter release and the organization of cytoskeletal organization including actin filaments, microtubules and spectrin in the presynaptic terminal5.
In vitro studies show that the dephospho-form of synapsin I binds synaptic vesicles, binds and bundles F-actin, and promotes G actin polymerization5.
Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of rat Synapsin I. Anti-Synapsin I (SYN1) Antibody (#ANR-014) can be used in western blot and immunohistochemistry applications. It has been designed to recognize Synapsin I from rat, mouse and human samples.
Powered by Bioz
