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SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion (Ilardi et al., 1999. Additionally we are shipping SNAP-Associated Protein Proteins (15) and SNAP-Associated Protein Kits (8) and many more products for this protein.
Showing 10 out of 35 products:
Human Polyclonal SNAPIN Primary Antibody for ELISA, WB - ABIN525251
Yun, Park, Ho, Kim, Kim, Oh, Ga, Seo, Chang, Son, Seol: LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25. in Experimental & molecular medicine 2013
Disruption of Snapin-PKR2 (show PROKR2 Antibodies) interaction did not affect PKR2 (show PROKR2 Antibodies) signaling, but increased the ligand-induced degradation, implying a role of Snapin in the trafficking of PKR2 (show PROKR2 Antibodies).
Authors propose that Snapin connects chlamydial inclusions with the microtubule network by interacting with both Chlamydia psittaci IncB and dynein.
Snapin, a SNAP (show NAPA Antibodies)-25 (synaptosomal-associated protein-25 (show SNAP25 Antibodies)) interacting protein, interacts with LRRK2 (show LRRK2 Antibodies).
Our findings reveal that Atg14L, previously considered to be solely a Beclin 1 (show BECN1 Antibodies)-binding autophagy protein, plays a novel role in the late stage of endocytic trafficking in conjunction with Snapin
These observations identify Snapin as a novel endogenous TLR2 (show TLR2 Antibodies) ligand in rheumatoid arthritis, and thus support a role for persistent TLR2 (show TLR2 Antibodies) signalling in pathogenesis.
These results suggest that Snapin may play a key role in regulating the cellular localization of human cytomegalovirus UL70, leading to modulation of viral DNA synthesis and progeny production.
PKA-dependent phosphorylation of snapin increases interaction among insulin (show INS Antibodies) secretory vesicle-associated proteins, thereby potentiating glucose-stimulated insulin (show INS Antibodies) secretion.
results suggest that RGS7 could play a role in synaptic vesicle exocytosis through its interaction with snapin
EBAG9 (show EBAG9 Antibodies) and Snapin have roles in controlling exocytosis processes
results demonstrate that snapin is a binding partner of dysbindin-1 (show DTNBP1 Antibodies) in vitro and in the brain; both dysbindin-1 (show DTNBP1 Antibodies) and snapin are concentrated in tissue enriched in synaptic vesicle membranes and less commonly in postsynaptic densities
Snapin-dysbindin interaction regulates synaptic vesicle positional priming through BLOC-1/AP-3-dependent sorting.
Snapin reduces APP (show APP Antibodies) processing by enhancing BACE1 (show BACE Antibodies) lysosomal degradation.
Transmembrane prostatic acid phosphatase (show ACPP Antibodies) (TMPAP) interacts with snapin and deficient mice develop prostate adenocarcinoma.
Snapin accelerates exocytosis at low intracellular calcium concentration in mouse chromaffin cells.
Snapin-dynein coupling is one of the primary mechanisms driving BDNF (show BDNF Antibodies)-TrkB (show NTRK2 Antibodies) retrograde transport, thus providing mechanistic insights into the regulation of neuronal growth and survival.
AC6 (show ADCY6 Antibodies)-mediated inhibition of neurite outgrowth was reversed by the overexpression of Snap25 (show SNAP25 Antibodies) or a Snapin mutant that could not be phosphorylated.
Snapin has a role in regulating autophagy-lysosomal function
Snapin deficiency leads to reduced cell density in cortical plates, apoptotic death in the cortex & third ventricle, enhanced membrane-bound LC3 (show MAP1LC3A Antibodies)-II staining, and accumulation of polyubiquitinated proteins in the cortex and hippocampus in knockout mice
highlights new mechanistic insights into how Snapin-intermediate chain coordinates retrograde transport and late endosomal-lysosomal trafficking critical for autophagy-lysosomal function, and thus neuronal homeostasis.
The protein encoded by this gene is a coiled-coil-forming protein that associates with the SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) complex of proteins and the BLOC-1 (biogenesis of lysosome-related organelles) complex. Biochemical studies have identified additional binding partners. As part of the SNARE complex, it is required for vesicle docking and fusion and regulates neurotransmitter release. The BLOC-1 complex is required for the biogenesis of specialized organelles such as melanosomes and platelet dense granules. Mutations in gene products that form the BLOC-1 complex have been identified in mouse strains that are models of Hermansky-Pudlak syndrome. Alternative splicing results in multiple transcript variants.
, SNARE-associated protein Snapin
, BLOC-1 subunit 7
, SNAP-25-binding protein
, SNARE associated protein snapin
, biogenesis of lysosomal organelles complex-1, subunit 7
, biogenesis of lysosome-related organelles complex 1 subunit 7
, synaptosomal-associated protein 25-binding protein
, synaptosomal-associated protein 25 binding protein
, synaptosomal-associated protein, 25 kDa, binding protein