Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
VAMP8 encodes an integral membrane protein that belongs to the synaptobrevin/vesicle-associated membrane protein subfamily of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs).
Showing 7 out of 8 products:
our study suggested that VAMP8 gene variants might not contribute to glioma susceptibility and associated with glioma in the Chinese Han population.
Vesicle-associated membrane protein 8 as a novel oncogene (show RAB1A Proteins) by promoting cell proliferation and therapeutic resistance in glioma. Targeting VAMP8 may serve as a potential therapeutic regimen for the treatment of glioma.
Starvation-induced MTMR13 and RAB21 (show RAB21 Proteins) activity regulates VAMP8 to promote autophagosome-lysosome fusion.
Cytotoxic granule exocytosis is a sequential, multivesicle fusion process requiring VAMP8-mediated recycling endosome fusion before cytotoxic granule fusion.
Inhibition of VAMP8, but not VAMP7 (show VAMP7 Proteins), significantly reduces viral entry.
VAMP8 regulates mucin (show SLC13A2 Proteins) granule exocytosis in airway goblet cells, and reduction of its expression may provide a novel therapeutic target to ameliorate airway mucus obstruction in lung diseases
Assessment of KIF6 genotype is not useful in predicting low density lipoprotein cholesterol lowering response to pravastatin, and heart disease risk reduction in the elderly.
Dynamics of FIP3 (show IKBKG Proteins)- and VAMP8-containing endosomes reflect the progressive stages of abscission.
The VAMP8 rs1010 polymorphism was associated with CHD risk in Chinese Han population, the A allele might serve as a genetic risk factor of coronary heart disease.
Results suggest that the combinational SNARE proteins VAMP8 and Vti1b mediate the fusion of antimicrobial and canonical autophagosomes with lysosomes, an essential event for autophagic degradation.
in addition to a secretory role, VAMP8-mediates trafficking of NOX2 (show CYBB Proteins) to endosomes and phagosomes and this promotes induction of cytolytic T cell immune responses
This report highlights the importance of the VAMP8 secretory machinery in facilitating mucus release from intestinal goblet cells and the dire consequences that occur during disease pathogenesis if these pathways are not functional.
acute inhibition of VAMP8-mediated secretion during pancreatitis triggers intracellular trypsin accumulation and loss of the early endosomal compartment
These findings reveal a role for VAMP8 in LC3 (show MAP1LC3A Proteins)-associated phagocytosis and highlight a novel mechanism exploited by L. major promastigotes to interfere with the host antimicrobial machinery
VAMP8-mediated secretion is dependent on anterograde endosomal trafficking.
Leishmania evades host immunity by GP63 (show LMLN Proteins)-mediated VAMP8 cleavage.
VAMP8 mediates insulin (show INS Proteins) granule recruitment to the plasma membrane, which partly accounts for GLP-1 (show GCG Proteins) potentiation of glucose-stimulated insulin (show INS Proteins) secretion.
VAMP8 knockout mice were used to show that the SNARE (show VTI1B Proteins) machinery plays a critical role in the process of granule homotypic fusion.
that granule-to-granule fusion is regulated by VAMP8 containing SNARE (show VTI1B Proteins) complexes distinct from those that regulate primary granule fusion.
This gene encodes an integral membrane protein that belongs to the synaptobrevin/vesicle-associated membrane protein subfamily of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). The encoded protein is involved in the fusion of synaptic vesicles with the presynaptic membrane.
vesicle-associated membrane protein 8
, vesicle-associated membrane protein 8 (endobrevin)
, Vesicle-associated membrane protein 8