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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 Proteins (14) and many more products for this protein.
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Human Polyclonal SNAP23 Primary Antibody for ICC, IF - ABIN4354884
Stadler, Hjelmare, Neumann, Jonasson, Pepperkok, Uhlén, Lundberg: Systematic validation of antibody binding and protein subcellular localization using siRNA and confocal microscopy. in Journal of proteomics 2012
Show all 2 references for ABIN4354884
Chicken Polyclonal SNAP23 Primary Antibody for WB - ABIN2783437
Okayama, Arakawa, Mizoguchi, Tajima, Takuma: SNAP-23 is not essential for constitutive exocytosis in HeLa cells. in FEBS letters 2007
Human Polyclonal SNAP23 Primary Antibody for ELISA, WB - ABIN4354882
Gratacòs, Costas, de Cid, Bayés, González, Baca-García, de Diego, Fernández-Aranda, Fernández-Piqueras, Guitart, Martín-Santos, Martorell, Menchón, Roca, Sáiz-Ruiz, Sanjuán, Torrens, Urretavizcaya et al.: Identification of new putative susceptibility genes for several psychiatric disorders by association analysis of regulatory and non-synonymous SNPs of 306 genes involved in neurotransmission and ... in American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics 2009
Human Polyclonal SNAP23 Primary Antibody for ELISA, WB - ABIN4354883
Boström, Andersson, Vind, Håversen, Rutberg, Wickström, Larsson, Jansson, Svensson, Brånemark, Ling, Beck-Nielsen, Borén, Højlund, Olofsson: The SNARE protein SNAP23 and the SNARE-interacting protein Munc18c in human skeletal muscle are implicated in insulin resistance/type 2 diabetes. in Diabetes 2010
SNAP23 is selectively expressed in airway secretory cells and mediates baseline and stimulated mucin (show SLC13A2 Antibodies) secretion.
these data suggest that SNAP23 is a key component of the endothelial SNARE (show VTI1B Antibodies) 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 Antibodies), synaptotagmin-7 (show SYT7 Antibodies)) mice in combination with viral transduction showed that SNAP-23-driven release is triggered by endogenous synaptotagmin-7 (show SYT7 Antibodies)
Results suggest that Plin2 (show PLIN2 Antibodies) inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets.
morphine suppresses TLR4 (show TLR4 Antibodies)-induced TNF (show TNF Antibodies) release in mast cells, preventing the IKK (show CHUK Antibodies)-dependent phosphorylation of SNAP-23, which is necessary for TNF (show TNF Antibodies) exocytosis, and this inhibition correlates with the formation of a beta (show SUCLA2 Antibodies)-arrestin-2 (show ARRB2 Antibodies)/TRAF6 (show TRAF6 Antibodies) 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 Antibodies) protein SNAP23 mediates cAMP-stimulated renin (show REN Antibodies) 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 Antibodies) complex underlying regulated exocytosis in these cells.
Study identified SNAP23 as a novel oncogene (show RAB1A Antibodies) in Ovarian Cancer (OC). It is over-expressed in OC and could promote the proliferation, migration and invasion of OC in vitro.
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 Antibodies) machinery that mediates endothelial exocytosis.
Increased level of SNAP23-Syntaxin4 (show STX4 Antibodies)-VAMP7 (show VAMP7 Antibodies) interaction correlates with decreased Syntaxin4 (show STX4 Antibodies) phosphorylation and trafficking of MT1-MMP (show MMP14 Antibodies) to invadopodia during cellular invasion.
The association of Src (show SRC Antibodies), EGFR (show EGFR Antibodies) and beta1 integrin is dependent upon membrane traffic that is mediated by syntaxin13 (officially known as STX12 (show STX12 Antibodies)) and SNAP23.
Data suggest SNAP23 and VAMP3 (vesicle-associated membrane protein 3 (show VAMP3 Antibodies)) participate in interleukin-1beta-, interleukin-1 receptor-, calcium signaling-dependent secretion/exocytosis of interleukin-6 (show IL6 Antibodies) and tumor necrosis factor alpha (show TNF Antibodies) from synoviocytes.
STX-3 (show STX3 Antibodies) 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 Antibodies) domain of SNAP-23 into neutrophils as an HIV transactivator of transcription (TAT (show TAT Antibodies)) fusion protein significantly inhibits exocytosis of neutrophil granule subsets without altering signal transduction pathway activation.
mRNA levels of BSCL2 (show BSCL2 Antibodies) and SNAP23, but not COPA (show COPA Antibodies), increased during adipocyte differentiation. Redistribution of SNAP23 protein to different cellular compartments was observed when comparing undifferentiated mesenchymal stem cells and differentiated adipocytes.
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