Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
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 Proteins (7) and many more products for this protein.
Showing 10 out of 75 products:
Rat (Rattus) Monoclonal SYT2 Primary Antibody for IP, WB - ABIN1449191
Heald, Nogales: Microtubule dynamics. in Journal of cell science 2002
Show all 5 references for ABIN1449191
Human Polyclonal SYT2 Primary Antibody for IP, IHC - ABIN1742202
Johnson, Franz, Kuhn, Furness, Rüttiger, Münkner, Rivolta, Seward, Herschman, Engel, Knipper, Marcotti: Synaptotagmin IV determines the linear Ca2+ dependence of vesicle fusion at auditory ribbon synapses. in Nature neuroscience 2009
Show all 3 references for ABIN1742202
Human Polyclonal SYT2 Primary Antibody for IF - ABIN401604
Cnops, Hu, Burnat, Arckens: Influence of binocular competition on the expression profiles of CRMP2, CRMP4, Dyn I, and Syt I in developing cat visual cortex. in Cerebral cortex (New York, N.Y. : 1991) 2008
Show all 3 references for ABIN401604
knockdown of synaptotagmin 2 (syt2) reduces synchronous release, whereas knockdown of synaptotagmin 7 (syt7 (show SYT7 Antibodies)) 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 (show BoNT/B Antibodies) 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 Antibodies)) dimer
WNK1 (show WNK1 Antibodies) selectively binds to and phosphorylates synaptotagmin 2 (Syt2) within its calcium binding C2 domains. Endogenous WNK1 (show WNK1 Antibodies) and Syt2 coimmunoprecipitate and colocalize on a subset of secretory granules in INS-1 (show FOXM1 Antibodies) cells.
A recombinant fragment from the luminal domain of the human receptor protein syt (show SS18 Antibodies) 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 (show BoNT/B Antibodies) 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 Antibodies))+ cooperativity, as well as by suppressing a remaining, near-linear Ca(2 (show CA2 Antibodies))+ 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 Antibodies)+ 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