SynGAP-alpha1 (F8I5Q) Rabbit Monoclonal Antibody recognizes endogenous levels of total SynGAP-α1 protein. This antibody does not cross-react with SynGAP-α2, β, or γ isoforms.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human SynGAP-α1 protein.

SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations, specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains of SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123, among other sites (2,3). Phosphorylation of SynGAP results in stimulation of the GTPase activity of Ras, and PSD95-dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development as mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced long-term potentiation (LTP) and perform poorly in spatial memory tasks (6).

Alternative splicing of the SynGAP1 gene generates four isoforms with distinct C-terminal sequences (α1, α2, β, and γ). These isoforms exhibit unique spatiotemporal expression patterns, subcellular localizations, and proposed functions in health and disease (7-9).