anti-Synaptosomal-Associated Protein, 23kDa (SNAP23) Antibodies

Mouse (Murine) Synaptosomal-Associated Protein, 23kDa (SNAP23) interaction partners

1. SNAP-23 phosphorylation at Ser95 played an important role in the regulation of SNARE-dependent membrane fusion during FcR-mediated phagocytosis.

2. PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23.

3. These results demonstrate opposing roles for SNAP23 in the secretion mechanisms of the endocrine and exocrine pancreas.

4. SNAP23 is selectively expressed in airway secretory cells and mediates baseline and stimulated mucin secretion.

5. these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis.

6. Data indicate that acute depletion of synaptosomal-associated protein 23 (SNAP-23) in fibroblasts leads to rapid apoptotic cell death.

7. Use of neurons from double-knock-out (SNAP-25, synaptotagmin-7) mice in combination with viral transduction showed that SNAP-23-driven release is triggered by endogenous synaptotagmin-7

8. Results suggest that Plin2 inhibits glucose uptake by interacting with, and regulating cellular targeting of SNAP23 to lipid droplets.

9. morphine suppresses TLR4-induced TNF release in mast cells, preventing the IKK-dependent phosphorylation of SNAP-23, which is necessary for TNF exocytosis, and this inhibition correlates with the formation of a beta-arrestin-2/TRAF6 complex

10. We report the regulation of platelet secretion via phosphorylation of SNAP-23 at Ser95.

11. Results suggest that phagosomal SNAP-23 is one of the key players regulating the phagosomal environment in macrophages.

12. We concluded that the SNARE protein SNAP23 mediates cAMP-stimulated renin release.

13. SNAP23 display robust and ubiquitous pattern of expression in adult hippocampal astrocytes and are therefore likely to be molecularly associated in the core SNARE complex underlying regulated exocytosis in these cells.

14. By altering the levels of individual components of the VAMP3/Stx4/SNAP23 complex we show here that this SNARE complex regulates efficient macrophage adhesion, spreading and migration on fibronectin.

15. These data reveal a critical role for SNAP-23 during embryogenesis.

16. SNAP-23, but not SNAP-25, is important for the functional regulation of postsynaptic glutamate receptors.

17. the majority of SNAP-23 is associated with non-caveolar, cholesterol-rich lipid rafts

18. Palmitoylated peptides from the cysteine-rich domain of this protein cause membrane fusion depending on peptide length, position of cysteinees, and extent of palmitoylation.

19. Interacts with tomosyn and plays a role in insulin-stimulated GLUT4 translocation.

20. Overexpression of SNAP-23 resulted in a distinct phenotype; SNAP-23 did not support a standing pool of primed secretory vesicles.

Human Synaptosomal-Associated Protein, 23kDa (SNAP23) interaction partners

1. Data suggest that acylation of SNAP23 (synaptosome associated protein 23) and STX11 (syntaxin-11) regulates exocytosis in platelets; maintaining acylation states of SNAP23 and STX11 is important for platelet function.

2. PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23.

3. SNAP23 suppressed progression of cervical cancer and induced cell cycle G2/M arrest via upregulating p21(cip1) and downregulating CyclinB1

4. Knockdown of VAMP3 and SNAP23 reduces endothelial secretion of miR-126-3p and miR-200a-3p, as well as the proliferation, migration, and suppression of contractile markers in smooth muscle cells caused by vascular endothelial cell-coculture.

5. Study showed that SNAP23 was recruited to the close sites of lipid droplet (LD) in HCV-infected cells, implying that SNAP23 was required for HCV-induced LD enlargement and, HCV production.

6. A novel regulatory mechanism for SNAP23-dependent mast cell activation of T. vaginalis-secreted LTB4 involving surface trafficking of BLT1.

7. Study identified SNAP23 as a novel oncogene in Ovarian Cancer (OC). It is over-expressed in OC and could promote the proliferation, migration and invasion of OC in vitro.

8. Localization of SNAP23 was found in plasma membrane, lipid droplets and mitochondria of skeletal muscle.

9. these data suggest that SNAP23 is a key component of the endothelial SNARE machinery that mediates endothelial exocytosis.

10. Increased level of SNAP23-Syntaxin4-VAMP7 interaction correlates with decreased Syntaxin4 phosphorylation and trafficking of MT1-MMP to invadopodia during cellular invasion.

11. The association of Src, EGFR and beta1 integrin is dependent upon membrane traffic that is mediated by syntaxin13 (officially known as STX12) and SNAP23.

12. Data suggest SNAP23 and VAMP3 (vesicle-associated membrane protein 3) participate in interleukin-1beta-, interleukin-1 receptor-, calcium signaling-dependent secretion/exocytosis of interleukin-6 and tumor necrosis factor alpha from synoviocytes.

13. Results suggest that phagosomal SNAP-23 is one of the key players regulating the phagosomal environment in macrophages.

14. STX-3 and SNAP-23 are crucial for the release of all chemokines in mature human mast cells

15. Data show that knockdown of SNAP-23 inhibited the production of virus.

16. Introduction of the SNARE domain of SNAP-23 into neutrophils as an HIV transactivator of transcription (TAT) fusion protein significantly inhibits exocytosis of neutrophil granule subsets without altering signal transduction pathway activation.

17. SNAP23 and SNAP25 palmitoylation is regulated by DHHC palmitoyl transferases

18. the importance of SNAP23 in the trafficking of matrix metalloproteinases during degradation of extracellular matrix substrates and subsequent cellular invasion

19. 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.

20. cleaved by calpain in activated platelets

Pig (Porcine) Synaptosomal-Associated Protein, 23kDa (SNAP23) interaction partners

1. mRNA levels of BSCL2 and SNAP23, but not COPA, increased during adipocyte differentiation. Redistribution of SNAP23 protein to different cellular compartments was observed when comparing undifferentiated mesenchymal stem cells and differentiated adipocytes.