Anti-Synaptotagmin antibody produced in rabbit

Synaptotagmin (Syt, p65) is an abundant synaptic vesicle (SV) membrane protein. It is characterized by a short intravesicular N-terminal domain, a single transmembrane region and two copies of highly conserved internal repeats, known as the C2A and C2B domains, which are homologous to the C2 regulatory region of protein kinase C (PKC) in the cytoplasmic domain. At least eight different isoforms of synaptotagmin (SytI-VIII) are expressed in the brain, four of which (Syt IV, V, VII and VIII) are also expressed in non-neuronal tissues.

The sequence is highly conserved among species (SytI) and is not found in other known synaptotagmin isoforms (SytII-VIII).

synthetic peptide corresponding to N-terminus of synaptotagmin I (SytI) of rat origin (amino acids 1-16 with C-terminally added lysine), conjugated to KLH.

Anti-Synaptotagmin antibody produced in rabbit has been used:

• for cell surface labelling of synaptotagmin I (SytI)
• in immunofluorescence microscopy
• in western blotting

Synaptotagmin binds Ca²⁺ phospholipids with high affinity and has a central role in Ca²⁺ regulated neurotransmitter release. Synaptotagmin functions as a Ca²⁺ sensor and is required for efficient exocytosis, particularly in the vesicle docking and/or fusion step with the plasma membrane. Ca²⁺ influx triggers synaptotagmin to interact with either syntaxin or SNAP-25 and the cytoplasmic domain of neurexin leading to fusion and exocytosis. Mutations or deletion of synaptotagmin result in severely impaired Ca²⁺ triggered neurotransmitter release. Synapses of SytI knockout mice lack the fast-component of Ca²⁺ dependent neurotransmitter release, but exhibit no changes in the slow, Ca²⁺ independent component of synaptic vesicle exocytosis.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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