Synaptotagmin-6 antibody

Background of Synaptotagmin-6 antibody

Synaptotagmins constitute a family of membranetrafficking proteins that are characterized by an N- terminal transmembrane region (TMR), a variable linker, and two C-terminal C2 domains - C2A and C2B. There are 15 members in the mammalian synaptotagmin family. There are several C2-domain containing protein families that are related to synaptotagmins, including transmembrane (Ferlins, E-Syts, and MCTPs) and soluble (RIMs, Munc13s, synaptotagmin-related proteins and B/K) proteins.  The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2 (1, 2).
Synaptotagmin-6 is localized to the endoplasmic reticulum and/or Golgi-like perinuclear compartment. It may be important for trafficking and calcium signaling as it is specially expressed in non-neuronal tissues. Also SytVI is present in the acrosomal region of mammalian spermatozoa. The cytosolic domain of SytVI can abrogate exocytosis by competing with the endogenous protein for essential interactions with the fusion machinery involved in a acrosomal exocytosis (3-5).