Anti-Synaptotagmin-like Protein 4 (SYTL4) Antibody, clone 7D2.2 clone 7D2.2, from mouse

Synaptotagmin-like protein 4 (UniProt Q96C24; also known as Exophilin-2, Granuphilin) is encoded by the SYTL4 (also known as SLP4) gene (Gene ID 94121) in human. SYLT4 belongs to the synaptotagmin-like protein family, which contains an N-terminal RabBD (Rab-binding) domain and two C-terminal C2 domains. The characteristic feature of this family is the N-terminal domain, which is not found in other C-type tandem C2 proteins. SYLT4 is detected close to the plasma membrane and on secretory granules. Interacts with vesicles containing negatively charged phospholipids in a Ca2+-independent manner. It can bind to both the GTP- and GDP-bound forms of Rab27A and inhibits a specific GTP/GDP exchange cycle required for dense-core vesicle exocytosis. It is the first regulatory in the exocytosis pathway that functions by directly connecting Rab and SNARE. It modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. It is not only essential for the docking of insulin granules, but also simultaneously imposes a fusion constraint on them through an interaction with syntaxin-1alpha fusion machinery.