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Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). Additionally we are shipping SNAP25 Antibodies (340) and SNAP25 Kits (19) and many more products for this protein.
Showing 10 out of 31 products:
Human SNAP25 Protein expressed in Escherichia coli (E. coli) - ABIN2004395
Chen, Tomchick, Kovrigin, Araç, Machius, Südhof, Rizo: Three-dimensional structure of the complexin/SNARE complex. in Neuron 2002
Show all 2 references for ABIN2004395
Study showed that SNAP25 is synthesized in the motor nerve endings and that the level of SNAP25 mRNA affects the activity of exocytosis of the neurotransmitter
Data demonstrate a role for SNAP-25 in controlling PSD-95 (show DLG4 Proteins) clustering and open the possibility that genetic reductions of the protein levels may contribute to the pathology through an effect on postsynaptic function and plasticity.
Data suggest that porosome-associated proteins SNAP25, TREK-1 (show KCNK2 Proteins), syntaxin-1A (show STX1A Proteins), and Gai3 exhibit stability and functionality such that isolated proteins can be reconstituted as insulin (show INS Proteins)-secreting porosomes in cell membrane of live cells.
we demonstrate that Syb2 (show VAMP2 Proteins) and SNAP25 mediate the vesicular release of BDNF (show BDNF Proteins) in axons and dendrites of cortical neurons
The extreme C terminus of SNAP25 is a critical region for the GBetaGamma-SNARE (show VTI1B Proteins) interaction.
Data show a significant increase of vesicle-associated membrane protein 2 (VAMP-2 (show VAMP2 Proteins)) mRNA expression, however, the expressions of synaptosome-associated protein of 25 kDa (SNAP-25) and syntaxin 1A (show STX1A Proteins) did not exhibit the changes in hippocampus.
SNAP-25 phosphorylation is regulated in a stress-dependent manner through both central and peripheral mechanisms.
Results indicate that reduction of SNAP-25 expression is associated to generation of epileptiform discharges and cognitive dysfunctions, which can be effectively treated by antiepileptic drugs
direct interaction between TRIM9 (show TRIM9 Proteins) and the Netrin-1 (show NTN1 Proteins) receptor DCC (show DCC Proteins) as well as a Netrin-1 (show NTN1 Proteins)-sensitive interaction between TRIM9 (show TRIM9 Proteins) and the SNARE (show VTI1B Proteins) component SNAP25. The interaction with SNAP25 negatively regulates SNARE (show VTI1B Proteins)-mediated exocytosis and axon
SNAP-25 regulates the organization of the molecular apparatus needed for dendritic spine formation by recruiting and stabilizing p140Cap (show SRCIN1 Proteins).
Snap25 rs363050 (G) allele, which results in a reduced expression of Snap25, is associated with altered glycemic parameters in T2DM possibly because of reduced functionality in the exocytotic machinery leading to suboptimal release of insulin (show INS Proteins).
single nucleotide polymorphisms in either the region of NEUROD6 (show NEUROD6 Proteins) or SNAP25 were significantly associated with Alzheimer's Disease, in APOE4+ females and APOE4+ males, respectively.
BoNT-A injection, but not Lipotoxin instillation, effectively cleaves SNAP-25 in the suburothelium.
The expression of SNAP-25 within the enteric nervous system and its downregulation in DD suggest an essential role in enteric neurotransmission and as a marker for impaired synaptic plasticity in enteric neuropathies.
Upon glucose stimulation BAG3 (show BAG3 Proteins) is phosphorylated by FAK (show PTK2 Proteins) and dissociates from SNAP-25 allowing the formation of the SNARE (show NAPA Proteins) complex, destabilization of the F-actin network and insulin (show INS Proteins) release.
The SNAP-25 Ddel T/C genotype was more common in fibromyalgia syndrome patients compared to controls, and it related to behavioral symptoms, personality and psychological disorders.
This study demonstrated that SNAP-25 polymorphisms may be associated with Alzheimer's disease and correlate with alterations in categorical fluency and a reduced localized brain activity.
SNARE (show NAPA Proteins) complex genes and their interactions may play a significant role in susceptibility and working memory of ADHD.
Patterns of the immunoreactivity with antibodies to SNAP-25, synapsin-I (show SYN1 Proteins) and synaptophysin (show SYP Proteins) are completely appropriate to those of adult's OB on the 38-40 weeks of the prenatal development.
In individual chromaffin cells, we tracked conformational changes in SNAP25 by total internal reflection fluorescence resonance energy transfer (FRET) microscopy while exocytotic catecholamine release from single vesicles was simultaneously recorded
dynamic experiments using TIRFM revealed that attenuation of cortical F-actin movement clearly diminishes the mobility of SNAP-25 clusters.
Stable syntaxin/SNAP-25 dimers are a central principle of the SNARE (show NAPA Proteins) assembly pathway underlying regulated exocytosis.
microdomains carrying syntaxin1 (show STX1A Proteins)/SNAP-25 and different types of calcium channels act as the sites for physiological granule fusion in "in situ" chromaffin cells
These data demonstrate a differential ability of SNAP-25 homlog to support neuronal function.
data indicate that SNARE (show NAPA Proteins) proteins VAMP-2 (show VAMP2 Proteins) and SNAP-25 play an essential role in daughter blastomere apposition, possibly via the delivery of components that promote the cell-to-cell adhesion required for the successful completion of cytokinesis
Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for this gene.
synaptosomal-associated protein 25
, super protein
, synaptosomal-associated 25 kDa protein
, synaptosomal-associated protein, 25 kDa
, GENA 70
, blind drunk
, resistance to inhibitors of cholinesterase 4 homolog
, synaptosomal associated protein-25
, synaptosomal-associated protein 25 isoform SNAP25B
, synaptosomal-associated 25kD protein