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Peptide (C)SGTLKEPDSSKTP, corresponding to amino acid residues 438-450 of rat Synapsin-2 (Accession Q63537). Intracellular, region G.
Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain membranes:1,2. Anti-Synapsin II (SYN2) Antibody (#ANR-015), (1:200).
3,4. Anti-Synapsin II (SYN2) Antibody, preincubated with the control peptide antigen.
Expression of Synapsin-2 in mouse ventral striatum and rat hippocampusImmunohistochemical staining of perfusion-fixed frozen mouse brain sections with Anti-Synapsin II (SYN2) Antibody (#ANR-015), (1:200), followed by goat-anti-rabbit-AlexaFluor-488 (green staining). A. Synapsin-2 staining in the mouse ventral striatum region shows dense patches of immunoreactivity within the islands of Calleja (IC) (horizontal arrow) that are delineated by DAPI-positive granule cells (in blue and marked by a vertical arrow). B. Synapsin-2 staining in the rat hippocampal dentate gyrus is detected in the dentate hilus (H) but not in the granule layer (G). Cell nuclei are stained with DAPI (blue).
Synapsins are a family of ten homologous neuronal phosphoproteins evolutionarily conserved in invertebrate and vertebrate organisms. Synapsins appear to be crucial determinants for the fine-tuning of synaptic transmission and for synaptic remodeling. This is particularly evident in several paradigms of short-term plasticity (STP), which are specifically affected by mutations or malfunctioning of synapsin proteins. Notably, knockout of synapsin-2 in mice causes fully generalized forebrain seizures from the age of 2 months1.
All synapsins, including synapsin-2, are composed of a highly homologous N-terminal region, and a more variable C-terminus. The N-terminal homologous region can be divided in three domains, namely domain A, B and C, which, except for domain B, are highly conserved across isoforms and species. Domain A is contains the phosphorylation site for PKA and CaMKI. Domain B, rich in small amino acids, is considered as a linker region connecting domain A to domain C. Domain C is a large region of about 300 amino acids, containing both hydrophobic and highly charged sequences with the potential to assume α-helix and β-sheet conformations. It shows extensive homology amongst the various members of the family, and mediates the core functions of synapsins1.
Species reactivity key:
Immuno-colocalization of Synapsin-2 and GABA(A) α1 Receptor in rat striatum.Immunohistochemical staining of immersion-fixed, free floating rat brain frozen sections using rabbit Anti-Synapsin II (SYN2) Antibody (#ANR-015), (1:300) and Guinea pig Anti-GABA(A) α1 Receptor (extracellular) Antibody (#AGP-083), (1:600). A. Synapsin-2 staining (red) appears in Islands of Calleja (IC), (arrow). B. GABA(A) α1 Receptor (green) is also detected in Islands of Calleja and in adjacent neurons. C. Merge of the two images demonstrates colocalization in IC while adjacent GABA(A) α1 positive neurons do not express Synapsin-2. Cell nuclei are stained with DAPI (blue).
Anti-Synapsin II (SYN2) Antibody (#ANR-015) is a highly selective antibody directed against an epitope of the rat protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize Synapsin II from mouse, human, and rat samples. This antibody will recognize both canonical isoforms (also known as Synapsin IIa) and the shorter isoform (Synapsin IIb).