Anti-Synaptotagmin antibody produced in rabbit

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.

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

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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.

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.

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