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anti-Mouse (Murine) VAMP2 Antibodies:
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Cow (Bovine) Polyclonal VAMP2 Primary Antibody for FACS, IF - ABIN4364759
Rosado, Redondo, Salido, Sage, Pariente: Cleavage of SNAP-25 and VAMP-2 impairs store-operated Ca2+ entry in mouse pancreatic acinar cells. in American journal of physiology. Cell physiology 2004
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Human Polyclonal VAMP2 Primary Antibody for ICC, IP - ABIN1742194
Kung, Gong, Adedoyin, Ng, Bhargava, Ohara, Jasmin: Evidence for glutamate as a neuroglial transmitter within sensory ganglia. in PLoS ONE 2013
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Human Monoclonal VAMP2 Primary Antibody for ELISA, WB - ABIN532957
Jacobsson, Piehl, Meister: VAMP-1 and VAMP-2 gene expression in rat spinal motoneurones: differential regulation after neuronal injury. in The European journal of neuroscience 1998
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findings reveal a novel signalling pathway involved in development of the semicircular canal system, and suggest a previously unrecognized role for NCS-1 in mitochondrial function via its association with several mitochondrial proteins.
These observations provide evidence that the synaptobrevin-2 transmembrane domain catalyzes the membrane fusion process by its structural flexibility, actively setting the pace of fusion pore expansion.
Syp1 clears Syb2 from the presynaptic active zone to prevent short-term depression.
The balance between synaptophysin and sybII levels is critical for the correct targeting of sybII to synaptic vesicles and suggests that alterations in synaptophysin levels might affect the localisation of sybII and subsequent presynaptic performance.
Thus, lipid-anchored syb2 provides little or no support for exocytosis, and anchoring syb2 to a membrane by a TMD greatly improves its function
Vamp2 mutations impair the ability of Munc18-1 to promote trans-SNARE zippering. These mutations inhibit spontaneous as well as evoked neurotransmitter release, providing evidence for the Vamp2-regulating function of Munc18-1 in synaptic exocytosis.
These results provide a novel molecular mechanism for autocrine negative feedback regulation of insulin secretion.
Results suggest that side chains in the syb2 transmembrane domain influence the kinetics of exocytosis by perturbing the packing of the surrounding lipids
we demonstrate that Syb2 and SNAP25 mediate the vesicular release of BDNF in axons and dendrites of cortical neurons
Here we report on transgenic mice expressing a ubiquitinated synaptic vesicle protein (Ub(G76V)-GFP-Syb2) that develop progressive degeneration of motor nerve terminals.
VAMP2 is the major v-SNARE involved in GLUT4 trafficking to the surface of 3T3-L1 adipocytes.
These results indicate a role for the syb2 TMD in nascent fusion pores, but in a very different structural arrangement from that of the syntaxin transmembrane domains.
Data show a significant increase of vesicle-associated membrane protein 2 (VAMP-2) mRNA expression, however, the expressions of synaptosome-associated protein of 25 kDa (SNAP-25) and syntaxin 1A did not exhibit the changes in hippocampus.
Clustering was dependent on specific interactions of native alpha-synuclein with both synaptobrevin-2/VAMP2 and anionic lipids
Findings indicate an essential role for VAMP2 in GLP-1 exocytosis from the GLUTag L cell in response to a variety of established secretagogues.
synaptobrevin2 is expressed in cytotoxic T lymphocytes and exclusively localized on granzyme B-containing lytic granules.
Data suggest that tryptophans W89/W90 in juxtamembrane region/transmembrane domain of Syb2 act as fusion clamp in chromaffin cells; in mutant protein, alanines A89/A90 promote spontaneous membrane fusion.
The tryptophan moiety in SybII keeps secretory vesicles in the release-ready state and support a model wherein tryptophan-mediated protein-lipid interactions assist in bridging the apposing membranes before fusion.
microelectrode array measurements in specific hippocampal subregions of VAMP2(+/-) mice showed significant reductions in potassium-evoked glutamate release
VAMP2 and VAMP3 are expressed in JG cells, but only VAMP2 is targeted to renin-containing granules and mediates the stimulatory effect of cAMP on renin exocytosis.
Synaptophysin controls synaptobrevin (sybII)traffic in nerve terminals during synaptic vesicle (SV) endocytosis, an interaction that may act as an adjustable regulator of SV retrieval efficiency.
these results indicate that the activation of beta-ARs induces secretory granules and cell membrane fusion via the interaction of VAMP-2 and syntaxin-4 in a PKA- and F-actin-dependent manner in human submandibular gland. Up-regulated beta-ARs might participate in altering protein secretion in transplanted submandibular gland by promoting the interaction of VAMP-2 with syntaxin-4.
miR-493-5p overexpression promotes cell apoptosis and inhibits the proliferation and migration of liver cancer cells by negatively regulating the expression of VAMP.
Data suggest that A-syn (alpha-synuclein) promotes SNARE-dependent vesicle docking; phosphatidylserine (PS) removal from t-SNARE-bearing vesicles causes A-syn to inhibit vesicle docking; PS removal from v-SNARE-bearing vesicles promotes vesicle docking; the C-terminal 45 residues of A-syn are required for promotion of vesicle docking. (Here, t-SNARE is SNAP-25; v-SNARE is VAMP2.)
A significant interactive two-locus model of STX1A_rs4363087|VAMP2_rs2278637 (presynaptic genes) was observed among SVC variants in all epilepsy cases.
VAMP2 is a promising new plasma cell marker
VAMP2 is involved in Porphyromonas gingivalis recycling pathway.VAMP2 is localized in early endosomes in gingival epithelial cells.
The present study addressed for the first time the unique substrate recognition mechanism of LC/F5 substrate cleavage of VAMP-2 by Botulinum Neurotoxin subtype F5.
This study showed that decreased Levels of VAMP2 correlate with Duration of Dementia.
VAMP2-NRG1 is a novel oncogenic fusion gene representing a new addition to the list of NRG1 fusion genes, which together may form an important diagnostic and clinical category of lung adenocarcinoma cases
A large vesicular pool of VAMP2 maintained by AP180 is crucial to sustain efficient neurotransmission.
SNARE complex genes and their interactions may play a significant role in susceptibility and working memory of ADHD.
miR-206 regulates lung surfactant secretion by limiting the availability of VAMP-2 protein.
The genetic variations of VAMP2, Synaptotagmin XI might be indication of the relationship between these genes and idiopathic generalized epilepsy
BoNT/F5 cleaves substrate synaptobrevin-2 in a different location than the other BoNT/F subtypes, between (54)L and (55)E.
unique mechanism of SNARE motif-dependent endocytic sorting and identify the ANTH domain proteins AP180 and CALM as cargo-specific adaptors for synaptobrevin 2 endocytosis
This protein has been found differentially expressed in thalami from patients with schizophrenia.
VAMP2 mediates the trafficking of alpha5beta1 integrin to the plasma membrane and VAMP2-dependent integrin trafficking is critical in cell adhesion, migration and survival.
SNAP-23 and syntaxin-4 are expressed in human eosinophils and are likely candidates for association with VAMP-2 during docking, which is followed by exocytosis
VAMP-2 mediates exocytosis of specific and tertiary granules of neutrophils through its interaction with Q-SNARE/R-SNARE complexes located at the neutrophil plasma membrane.
VAMP-2 can be one of the v-SNAREs for constitutive exocytosis
VAMP-2 is critical to lysosome fusion in membrane raft clustering, and this VAMP-2-mediated lysosome-MR signalosomes contribute to redox regulation of coronary endothelial function.
VAMP2 is restricted from forming the SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) complex in chromaffin granules from adrenal medullae to the same degree as in brain-purified synaptic vesicles.
Lengthening juxtamembrane region of synaptobrevin-2 severely reduced occurrence of rapid single events, leaving slow ones unchanged. It also impaired increase in fast-fusion mode that normally follows elevation of intracellular Ca2+ levels.
The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is thought to participate in neurotransmitter release at a step between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin. It is a likely candidate gene for familial infantile myasthenia (FIMG) because of its map location and because it encodes a synaptic vesicle protein of the type that has been implicated in the pathogenesis of FIMG.
vesicle-associated membrane protein 2 (synaptobrevin 2)
, synaptobrevin II
, vesicle-associated membrane 2
, Synaptobrevin 2 (vesicle-associated membrane protein VAMP-2)
, Vesicle-associated membrane protein (synaptobrevin 2)
, synaptobrevin 2
, vesicle associated membrane protein 2
, vesicle-associated membrane protein 2