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Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. Additionally we are shipping Synaptosomal-Associated Protein, 23kDa Antibodies (103) and many more products for this protein.
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Human SNAP23 Protein expressed in Escherichia coli (E. coli) - ABIN667088
Faigle, Colucci-Guyon, Louvard, Amigorena, Galli: Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery. in Molecular biology of the cell 2000
Show all 2 references for ABIN667088
these data suggest that SNAP23 is a key component of the endothelial SNARE (show VTI1B Proteins) machinery that mediates endothelial exocytosis.
Data indicate that acute depletion of synaptosomal-associated protein 23 (SNAP-23) in fibroblasts leads to rapid apoptotic cell death.
Use of neurons from double-knock-out (SNAP-25 (show SNAP25 Proteins), synaptotagmin-7 (show SYT7 Proteins)) mice in combination with viral transduction showed that SNAP-23-driven release is triggered by endogenous synaptotagmin-7 (show SYT7 Proteins)
Results suggest that Plin2 (show PLIN2 Proteins) inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets.
morphine suppresses TLR4 (show TLR4 Proteins)-induced TNF (show TNF Proteins) release in mast cells, preventing the IKK (show CHUK Proteins)-dependent phosphorylation of SNAP-23, which is necessary for TNF (show TNF Proteins) exocytosis, and this inhibition correlates with the formation of a beta (show SUCLA2 Proteins)-arrestin-2 (show ARRB2 Proteins)/TRAF6 (show TRAF6 Proteins) complex
We report the regulation of platelet secretion via phosphorylation of SNAP-23 at Ser95.
Results suggest that phagosomal SNAP-23 is one of the key players regulating the phagosomal environment in macrophages.
We concluded that the SNARE (show VTI1B Proteins) protein SNAP23 mediates cAMP-stimulated renin (show REN Proteins) release.
SNAP23 display robust and ubiquitous pattern of expression in adult hippocampal astrocytes and are therefore likely to be molecularly associated in the core SNARE (show VTI1B Proteins) complex underlying regulated exocytosis in these cells.
By altering the levels of individual components of the VAMP3 (show VAMP3 Proteins)/Stx4 (show STX4 Proteins)/SNAP23 complex we show here that this SNARE (show VTI1B Proteins) complex regulates efficient macrophage adhesion, spreading and migration on fibronectin (show FN1 Proteins).
Localization of SNAP23 was found in plasma membrane, lipid droplets and mitochondria of skeletal muscle.
these data suggest that SNAP23 is a key component of the endothelial SNARE (show NAPA Proteins) machinery that mediates endothelial exocytosis.
Increased level of SNAP23-Syntaxin4 (show STX4 Proteins)-VAMP7 (show VAMP7 Proteins) interaction correlates with decreased Syntaxin4 (show STX4 Proteins) phosphorylation and trafficking of MT1-MMP (show MMP14 Proteins) to invadopodia during cellular invasion.
The association of Src (show SRC Proteins), EGFR (show EGFR Proteins) and beta1 integrin is dependent upon membrane traffic that is mediated by syntaxin13 (officially known as STX12 (show STX12 Proteins)) and SNAP23.
Data suggest SNAP23 and VAMP3 (vesicle-associated membrane protein 3 (show VAMP3 Proteins)) 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.
STX-3 (show STX3 Proteins) and SNAP-23 are crucial for the release of all chemokines in mature human mast cells
Data show that knockdown of SNAP-23 inhibited the production of virus.
Introduction of the SNARE (show NAPA Proteins) domain of SNAP-23 into neutrophils as an HIV transactivator of transcription (TAT (show TAT Proteins)) fusion protein significantly inhibits exocytosis of neutrophil granule subsets without altering signal transduction pathway activation.
SNAP23 and SNAP25 (show SNAP25 Proteins) palmitoylation is regulated by DHHC palmitoyl transferases
Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues. The protein encoded by this gene is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion. Two alternative transcript variants encoding different protein isoforms have been described for this gene.
synaptosomal-associated protein 23
, synaptosomal-associated protein 23 isoform SNAP23A
, synaptosomal-associated protein, 23kDa
, synaptosomal-associated protein, 23kD
, vesicle-membrane fusion protein SNAP-23
, synaptosomal-associated protein 23 kD
, synaptosomal-associated protein, 23 kD