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anti-Mouse (Murine) VAMP2 Antibodies:
anti-Rat (Rattus) 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
Show all 4 Pubmed References
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
Show all 3 Pubmed References
Human Polyclonal VAMP2 Primary Antibody for ICC, IF - ABIN407569
Kong, Wong, Chan, Lo: Chronic exposure of adult rats to low doses of methylmercury induced a state of metabolic deficit in the somatosensory cortex. in Journal of proteome research 2013
findings reveal a novel signalling pathway involved in development of the semicircular canal system, and suggest a previously unrecognized role for NCS-1 (show NCS1 Antibodies) 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 (show SYP Antibodies) clears Syb2 from the presynaptic active zone to prevent short-term depression.
The balance between synaptophysin (show SYP Antibodies) and sybII levels is critical for the correct targeting of sybII to synaptic vesicles and suggests that alterations in synaptophysin (show SYP Antibodies) 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 (show TTN Antibodies) greatly improves its function
Vamp2 mutations impair the ability of Munc18-1 (show STXBP1 Antibodies) to promote trans-SNARE (show VTI1B Antibodies) zippering. These mutations inhibit spontaneous as well as evoked neurotransmitter release, providing evidence for the Vamp2-regulating function of Munc18-1 (show STXBP1 Antibodies) in synaptic exocytosis.
These results provide a novel molecular mechanism for autocrine negative feedback regulation of insulin (show INS Antibodies) 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 (show SNAP25 Antibodies) mediate the vesicular release of BDNF (show BDNF Antibodies) 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 (show GOSR1 Antibodies) involved in GLUT4 (show SLC2A4 Antibodies) trafficking to the surface of 3T3-L1 adipocytes.
these results indicate that the activation of beta-ARs (show SLURP1 Antibodies) induces secretory granules and cell membrane fusion via the interaction of VAMP-2 and syntaxin-4 (show STX4 Antibodies) in a PKA- and F-actin-dependent manner in human submandibular gland. Up-regulated beta-ARs (show SLURP1 Antibodies) might participate in altering protein secretion in transplanted submandibular gland by promoting the interaction of VAMP-2 with syntaxin-4 (show STX4 Antibodies).
miR (show MLXIP Antibodies)-493-5p overexpression promotes cell apoptosis and inhibits the proliferation and migration of liver cancer cells by negatively regulating the expression of VAMP (show VAMP Antibodies).
Data suggest that A-syn (show FYN Antibodies) (alpha-synuclein) promotes SNARE (show NAPA Antibodies)-dependent vesicle docking; phosphatidylserine (PS) removal from t-SNARE (show NAPA Antibodies)-bearing vesicles causes A-syn (show FYN Antibodies) to inhibit vesicle docking; PS removal from v-SNARE (show VTI1B Antibodies)-bearing vesicles promotes vesicle docking; the C-terminal 45 residues of A-syn (show FYN Antibodies) are required for promotion of vesicle docking. (Here, t-SNARE (show NAPA Antibodies) is SNAP-25 (show SNAP25 Antibodies); v-SNARE (show VTI1B Antibodies) is VAMP2.)
A significant interactive two-locus model of STX1A_rs4363087|VAMP2_rs2278637 (presynaptic genes) was observed among SVC (show COL4A1 Antibodies) 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 (show NRG1 Antibodies) is a novel oncogenic fusion gene representing a new addition to the list of NRG1 (show NRG1 Antibodies) 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 (show SNAP91 Antibodies) is crucial to sustain efficient neurotransmission.
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 (show NAPA Antibodies) (soluble N-ethylmaleimide-sensitive fusion protein (show NSF Antibodies) 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 (show CA2 Antibodies)+ 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