Synaptotagmin-2 Antibody recognizes endogenous levels of total synaptotagmin-2 protein. Bands of unknown identity are detected at 100 kDa and 140 kDa with some lysates.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human synaptotagmin-2 protein. Antibodies are purified by peptide affinity chromatography.

Synaptotagmin-2 (SYT2), an integral membrane protein found in synaptic vesicles, functions as a calcium sensor for neurotransmitter release. The synaptotagmin family of proteins share a common molecular structure, composed of an amino-terminal transmembrane region, a central linker region, and a pair of calcium binding carboxy-terminal C2 domains, C2A and C2B (1,2). SYT2 is the major synaptotagmin isoform expressed at neuromuscular junctions (NMJs). Mutations in the C2 domains of SYT2 can lead to dysregulation of neurotransmitter release at NMJs, resulting in the development of an array of disorders, including congenital myasthenic syndrome (CMS), Lambert–Eaton myasthenic syndrome (LEMS), and motor neuropathy (3-5). In addition to its role at NMJs, SYT2 has been found to be expressed by parvalbumin positive inhibitory neurons in the CNS, including at GABAergic basket cell and purkinje cell synapses (6-8). SYT2 expression levels have also been linked to neurodegenerative diseases, including Alzheimer’s disease, and Parkinson’s disease (9,10).