- Peptide (C)RSPTKDSLEYPDGK, corresponding to amino acid residues 119-132 of rat SynDIG1 (Accession Q58DZ9). Intracellular, N-terminus.
- Rat and mouse brain lysates and human SH-SY5Y cell lysate (1:200-1:600).
- Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain lysates:1,2. Anti-SynDIG1 Antibody (#AGC-049), (1:200).
3,4. Anti-SynDIG1 Antibody, preincubated with SynDIG1 Blocking Peptide (#BLP-GC049).
- Western blot analysis of human SH-SY5Y neuroblastoma cell line:1. Anti-SynDIG1 Antibody (#AGC-049), (1:400).
2. Anti-SynDIG1 Antibody, preincubated with SynDIG1 Blocking Peptide (#BLP-GC049).
SynDIG1 (Synapse differentiation induced gene 1) is a brain-specific, highly conserved type II integral membrane protein detected at excitatory synapses. The protein is responsible for the regulation of excitatory synapse number and strength in hippocampal neurons. The protein plays an important role during synapse development in regulating AMPA receptor (AMPAR) and PSD-95 content at excitatory synapses1,2.
SynDIG family includes four members: SynDIG1-4. SynDIG1 structure includes a large intracellular N-terminal region followed by a single transmembrane domain and a second hydrophobic segment that does not span the membrane. The membrane-associated region forms a three-helical bundle with two cysteine residues located at positions 191 and 192 in the juxta-transmembrane region exposed to the cytoplasm1,2.
In studies conducted on mice, deletion of endogenous SynDIG1 in the mouse brain results in a significant decrease in excitatory synapse maturation, but not in synapse composition. Thus, SynDIG1 is not required for synaptogenesis in vivo1. Contrarily, overexpression of SynDIG1 in cultures of dissociated rat hippocampal neurons shows a significant increase in excitatory synapse strength and number.