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Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Additionally we are shipping VAMP3 Antibodies (56) and many more products for this protein.
Showing 8 out of 14 products:
Human VAMP3 Protein expressed in Escherichia coli (E. coli) - ABIN667721
Hu, Hardee, Minnear: Membrane fusion by VAMP3 and plasma membrane t-SNAREs. in Experimental cell research 2007
Show all 2 references for ABIN667721
Human VAMP3 Protein expressed in Escherichia coli (E. coli) - ABIN2006198
Hager, Roberts, Cross, Proux-Gillardeaux, Bader: Identification of a novel Bves function: regulation of vesicular transport. in The EMBO journal 2010
phosphatidylinositol 4-kinase (show PI4KB Proteins) IIalpha knockdown inhibited vesicle-associated membrane protein 3 trafficking to perinuclear membranes and impaired the rate of VAMP3-mediated recycling of the transferrin receptor
The small GTPase (show RACGAP1 Proteins) Rab8 (show RAB8A Proteins) interacts with VAMP-3 to regulate the delivery of recycling T-cell receptors to the immune synapse.
phosphatidylinositol 4-kinase (show PI4KA Proteins) IIalpha knockdown inhibited vesicle-associated membrane protein 3 trafficking to perinuclear membranes and impaired the rate of VAMP3-mediated recycling of the transferrin receptor
highlight the role that VAMP3 and VAMP7 (show VAMP7 Proteins) play in selection of the pathways leading to generation of ultrastructurally different LC3 (show MAP1LC3A Proteins) compartments
Liquid chromatography-MS/MS analysis showed that the HHV-6 gM/gN complex interacts with the v-SNARE (show VTI1B Proteins) protein, vesicle-associated membrane protein 3 (VAMP3).
These results indicated that Uukuniemi virus relies on VAMP3 for penetration, providing an indication of added complexity in the trafficking of viruses through the endocytic network.
Genome-wide expression profiling identified the transcription of ADIPOR1, VAMP3 and C11ORF10 to be correlated with decreased ANRIL expression in a time-dependent manner.
Data suggest VAMP3 and SNAP23 (synaptosomal-associated protein 23 (show SNAP23 Proteins) kDa) participate in interleukin-1beta-, interleukin-1 receptor-, calcium signaling-dependent secretion/exocytosis of interleukin-6 (show IL6 Proteins) and tumor necrosis factor alpha (show TNF Proteins) from synoviocytes.
Data suggest a new integrin trafficking pathway in which endocytosed integrins are transported from VAMP3-containing recycling endosomes to STX6 (show STX6 Proteins)-containing trans-Golgi network before being recycled to the plasma membrane.
mutation of the Godzilla ubiquitylation target lysines on VAMP3 abrogates the formation of enlarged endosomes induced by either Godzilla or RNF167 (show RNF167 Proteins).
Endothelial cells specifically select VAMP 3 over VAMP8 (show VAMP8 Proteins) to cooperate with syntaxin 4 (show STX4 Proteins) and SNAP23 (show SNAP23 Proteins) in the Ca(2 (show CA2 Proteins)+)-triggered fusion of Weibel-Palade bodies with the plasma membrane.
Although a slight decrease in the rate of recovery of surviving bacteria was observed between 12 h and 36 h post-infection with Brucella melitensis, this was not significant indicating that VAMP3 is not involved in Brucella survival.
Protein kinase D (show PRKD1 Proteins) activates GLUT4 (show SLC2A4 Proteins) translocation via a VAMP3-dependent trafficking step.
This important SNARE (show VTI1B Proteins) complex facilitates macrophage adhesion, spreading, and persistent macrophage migration on fibronectin (show FN1 Proteins) through the delivery of VAMP3-positive membrane with its cargo to expand the plasma membrane.
VAMP3 mediates fusion of recycling endosome-derived vesicles with the oligodendroglial plasma membrane in the course of the secretory pathway
Cellubrevin alterations and Mycobacterium tuberculosis phagosome maturation arrest.
SNARE (show VTI1B Proteins) proteins (cellubrevin, syntaxin 4 (show STX4 Proteins)) are involved in late steps of GLUT4 (show SLC2A4 Proteins) translocation in adipocyte differentiation.
The requirement of vamp3 in phagocytosis in macrophages was determined in vamp3 knockout mice
cellubrevin/VAMP-3 is not a requirement for the platelet release reaction in mice.
From these results we concluded that cellubrevin-dependent membrane trafficking is involved in TEX101-transport to the surface of male germ cells.
Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein 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 a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Because of its high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, the protein encoded by this gene was shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
vesicle-associated membrane protein 3
, synaptic vesicle SNARE
, vesicle-associated membrane protein 3 (cellubrevin)