Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Syntaxin 1 is a component of the 7S and 20S SNARE complexes which are involved in docking and fusion of synaptic vesicles with the presynaptic plasma membrane. De plus, nous expédions STXBP5 Anticorps (8) et et beaucoup plus de produits pour cette protéine.
Showing 3 out of 3 products:
Glucose-dependent de-SUMOylation of tomosyn1 at K298 releases syntaxin1A and controls the amplification of exocytosis in concert with a recently-identified tomosyn1-interacting partner; the Ca(2+)-binding protein secretagogin, which dissociates from tomosyn1 in response to Ca(2+)-raising stimuli and is required for insulin granule trafficking and exocytosis downstream of Ca(2+) influx.
Using CRISPR/Cas9 genome editing, identified a human nonsynonymous SNP rs1039084 in the STXBP5 locus as a causal variant for a decreased thrombotic phenotype.
Genetic variations in STXBP5 and CLEC4M are associated with VWF level variation in type 1, but not in type 2 von Willebrand disease.
STXBP5 is required for normal arterial hemostasis, due to its contributions to platelet granule cargo packaging and secretion
STXBP5 inhibits endothelial exocytosis and promotes platelet secretion
Identify 3 loci associated with circulating tPA levels, the PLAT region, STXBP5, and STX2. Functional studies implicate a novel role for STXBP5 and STX2 in regulating tPA release.
Genetic variation in STXBP5 is associated with bleeding phenotype in female type 1 von Willebrand Disease patients.
Genetic variation in STXBP5 gene is associated with venous thrombosis.
multiple domains outside the R-SNARE of tomosyn are critical to the efficacy of inhibition by tomosyn on exocytotic secretion
Genetic variability in STXBP5 and STX2 affects both VWF concentration and activity in young individuals with premature arterial thrombosis.
Characterization of a related rat protein
Characterization of a related rat gene
Data indicate that bidirectional moving tomosyn-1 (Stxbp5) and tomosyn-2 (Stxbp5l) puncta were observed.
Mouse Embryonic Stem (mES) cells self-differentiated into arginine vasopressin (AVP) neurons (mES-AVP) that expressed tomosyn and two transmembrane SNARE proteins, including SNAP25 and syntaxin1. Tomosyn negatively regulates arginine vasopressin secretion in embryonic stem cell-derived neurons.
PIASgamma-dependent modification of tomosyn-1 with SUMO-2/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment.
regulates SNARE complex formation and synaptic vesicle fusion. (review)
It regulates vesicle fusion. (review)
Interacts with SNAP23 and Syntaxin4 and plays a role in Insulin-stimulated GLUT4 translocacion.
The interaction between syntaxin4 and Munc18c in adipocytes results in enhancement of insulin-stimulated GLUT4 externalization.
In the pancreatic beta-cell, tomosyn negatively regulates insulin exocytosis.
Tomosyn-1 is involved in a post-docking event that prepares secretory granules for fusion and is necessary to sustain exocytosis of pancreatic beta-cells in response to insulin secretagogues.
Tomosyn inhibits neurotransmitter release by catalyzing oligomerization of the SNARE complex through the N-terminal WD-40 repeat domain in addition to the inhibitory activity of the C-terminal (VAMP)-like domain.
Syntaxin 1 is a component of the 7S and 20S SNARE complexes which are involved in docking and fusion of synaptic vesicles with the presynaptic plasma membrane. This gene encodes a syntaxin 1 binding protein. In rat, a similar protein dissociates syntaxin 1 from the Munc18/n-Sec1/rbSec1 complex to form a 10S complex, an intermediate which can be converted to the 7S SNARE complex. Thus this protein is thought to be involved in neurotransmitter release by stimulating SNARE complex formation. Alternatively spliced transcript variants encoding different isoforms have been identified.
lethal(2) giant larvae protein homolog 3
, putative protein product of Nbla04300
, syntaxin-binding protein 5
, tomosyn 1