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Synaptotagmins, like SYT2, are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (Hilbush and Morgan, 1994. Additionally we are shipping Synaptotagmin II Antibodies (75) and Synaptotagmin II Proteins (7) and many more products for this protein.
knockdown of synaptotagmin 2 (syt2) reduces synchronous release, whereas knockdown of synaptotagmin 7 (syt7 (show SYT7 ELISA Kits)) reduces the asynchronous component of release.
SYT2 mutations cause a novel complex presynaptic congenital myasthenic syndrome characterized by motor neuropathy causing lower limb wasting and foot deformities, reflex potentiation following exercise and a prolonged period of posttetanic potentiation
Synaptotagmin 2 mutations cause an autosomal-dominant form of lambert-eaton myasthenic syndrome and nonprogressive motor neuropathy.
Human SytII is not an effective receptor for Botulinum neurotoxin D-C.
synaptotagmin-II is not a high affinity receptor for BoNT/B and G due to a phenylalanine to leucine mutation in its luminal domain present only in humans and chimpanzees
role for synaptotagmin II as calcium-sensor during phagocytosis and secretion in neutrophils
both synaptotagmins I and II can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25 (show SNAP25 ELISA Kits)) dimer
WNK1 (show WNK1 ELISA Kits) selectively binds to and phosphorylates synaptotagmin 2 (Syt2) within its calcium binding C2 domains. Endogenous WNK1 (show WNK1 ELISA Kits) and Syt2 coimmunoprecipitate and colocalize on a subset of secretory granules in INS-1 (show FOXM1 ELISA Kits) cells.
A recombinant fragment from the luminal domain of the human receptor protein syt (show SS18 ELISA Kits) II can bind specifically to botulinum neurotoxin B and its Hc domain.
Mutation of overexpressed Syt2 transgene leaves intrinsic calcium sensitivity of vesicles intact while it destabilizes the readily releasable pool of vesicles and loosens the tight coupling between calcium influx and release.
The 2.3-A structure of a ternary complex of botulinum neurotoxin type B bound to both its protein receptor synaptotagmin II and its ganglioside receptor GD1a, is reported.
Synaptotagmins 1 and 2 as mediators of rapid exocytosis at nerve terminals: the dyad hypothesis
Syt2 make it an excellent marker for analyzing the development and plasticity of perisomatic inhibitory innervations onto both excitatory and inhibitory neurons in the visual cortex.
Syt2 increases the dynamic range of synapses by driving release with a high Ca(2 (show CA2 ELISA Kits))+ cooperativity, as well as by suppressing a remaining, near-linear Ca(2 (show CA2 ELISA Kits))+ sensor.
Transient expression of Syt2 is no longer detected in cochlear inner hair cells (IHCs) after the onset of hearing, indicating that the most common calcium-sensors in central nervous system synapses are not involved in mature IHC ribbon synapse.
SYT2 was a negative regulator of chemotaxis
The readily releasable pool was rescued by Syt2 overexpression. The kinetics of fusion was slightly slower than in cells expressing Syt1. Syt2 has a lower Ca2+ affinity for phospholipid binding than Syt1 because of a difference in the C2A domain.
Data suggest that synaptotagmins 1 and 2 perform equivalent functions in the Ca2 (show CA2 ELISA Kits)+ triggering of action potential-induced neurotransmitter release and in the restriction of spontaneous release.
Synaptotagmin-2 is an essential synaptotagmin isoform that functions in concert with other synaptotagmins in the calcium-ion triggering of neurotransmitter release.
The cell-, temporal-, and species-specific expression of synaptotagmin isoforms suggests that each may have distinct functions in neurotransmitter release
Synaptotagmins, like SYT2, are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (Hilbush and Morgan, 1994
, synaptotagmin 2