Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Mouse (Murine) Antibodies:
anti-Rat (Rattus) Antibodies:
Go to our pre-filtered search.
Human Polyclonal SNAPIN Primary Antibody for WB - ABIN1742322
Vites, Rhee, Schwarz, Rosenmund, Jahn: Reinvestigation of the role of snapin in neurotransmitter release. in The Journal of biological chemistry 2004
Show all 4 Pubmed References
Mammalian Monoclonal SNAPIN Primary Antibody for ISt, IHC - ABIN1304965
Makani, Sultana, Sie, Orjiako, Tatangelo, Dowling, Cai, Pierce, Allan Butterfield, Hill, Park: Annexin A1 complex mediates oxytocin vesicle transport. in Journal of neuroendocrinology 2014
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
These observations suggest an important role for SNAPIN and autophagy in the homeostasis of macrophages, particularly long-lived tissue resident macrophages.
These results provide the evidence of a direct regulatory role of Snapin on Cav1.3 channels in atrial myocytes.
Inhibition of Snapin enhanced localization of HIV-1 with TLR8(+) early endosomes, triggered a pro-inflammatory response, and inhibited trans-infection of CD4(+) T cells.
Taken together, these results suggest that Snapin, the pUL130 interacting protein, has a role in modulating HCMV DNA synthesis.
Disruption of Snapin-PKR2 interaction did not affect PKR2 signaling, but increased the ligand-induced degradation, implying a role of Snapin in the trafficking of PKR2.
Authors propose that Snapin connects chlamydial inclusions with the microtubule network by interacting with both Chlamydia psittaci IncB and dynein.
Snapin, a SNAP-25 (synaptosomal-associated protein-25) interacting protein, interacts with LRRK2.
Our findings reveal that Atg14L, previously considered to be solely a Beclin 1-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 ligand in rheumatoid arthritis, and thus support a role for persistent TLR2 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 secretory vesicle-associated proteins, thereby potentiating glucose-stimulated insulin secretion.
results suggest that RGS7 could play a role in synaptic vesicle exocytosis through its interaction with snapin
EBAG9 and Snapin have roles in controlling exocytosis processes
results demonstrate that snapin is a binding partner of dysbindin-1 in vitro and in the brain; both dysbindin-1 and snapin are concentrated in tissue enriched in synaptic vesicle membranes and less commonly in postsynaptic densities
Snapin links the alpha(1A)-AR to TRPC6, augmenting Ca(2+) influx via ROC channels
Data describe for the first time the expression of SNAPIN in germ cells which raises possibility that SNAPIN plays an extra role in mammals which is germ cell specific.
Snapin plays an important role as a linker between the water channel and the t-SNARE complex, leading to the fusion event, and the pairing with specific t-SNAREs is essential for the specificity of membrane recognition and fusion.
Snapin-dysbindin interaction regulates synaptic vesicle positional priming through BLOC-1/AP-3-dependent sorting.
Snapin reduces APP processing by enhancing BACE1 lysosomal degradation.
Transmembrane prostatic acid phosphatase (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-TrkB retrograde transport, thus providing mechanistic insights into the regulation of neuronal growth and survival.
AC6-mediated inhibition of neurite outgrowth was reversed by the overexpression of Snap25 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-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.
Mutations in the human genes encoding Snapin and the BLOS proteins could underlie novel forms of Hermansky-Pudlak syndrome as seen in mouse models
These data suggested that Snapin is a new interactive protein of the granulocyte colony-stimulating factor receptor.
snapin is a new substrate of CK1delta
Progesterone-progesterone receptor-mediated SNAP25 expression in cumulus oocyte complexes and granulosa cells regulates cytokine and chemokine secretion via an exocytosis system.
Results show that Snapin interacts with the exocyst and plays a modulatory role in GLUT4 vesicle trafficking.
torsinA plays a role together with snapin in regulated exocytosis
Our studies provide mechanistic insights into a dual role of Snapin in enhancing the efficacy of SV priming and in fine-tuning synchronous SV fusion.
Snapin associates with late endocytic compartments and interacts with late endosomal SNAREs.
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