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V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. Additionally we are shipping Vesicle Transport through Interaction with T-SNAREs Homolog 1A (Yeast) Proteins (6) and and many more products for this protein.
Showing 10 out of 62 products:
Rat (Rattus) Polyclonal VTI1A Primary Antibody for ICC, IP - ABIN1742351
Laufman, Hong, Lev: The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport. in The Journal of cell biology 2011
Show all 3 Pubmed References
Transfection of LS174T cells showed that the VTI1A promoter is highly active compared to the TCF7L2 promoter, and that CDX2 activates transcription of VTI1A.
Novel variants of VTI1A-TCF7L2 fusion transcripts, including a novel fusion partner gene, RP11-57H14.3, was identified and demonstrated detectable levels in a large fraction of colorectal cancer samples.[RP11-57H14.3]
our results indicate that genetic variants in VTI1A may modify individual susceptibility to non-GBM of glioma in the Han Chinese population and support the role of the VTI1A genes in the occurrence of glioma.
The AA genotype of VTI1A (rs7086803) polymorphism had an increased risk of developing NSCLC compared with the GG genotype. Smoking lung cancer patients with the AA genotype of VTI1A gene (rs7086803) had a poor survival rate.
analysis of a new susceptibility locus for colorectal cancer in VTI1A [meta-analysis]
Data indicate that depletion of VAMP4, syntaxin 6, syntaxin 16, and Vti1a disrupted the Golgi ribbon structure.
We found a colorectal carcinoma cell line harboring the fusion gene to be dependent on VTI1A-TCF7L2 for anchorage-independent growth using RNA interference-mediated knockdown.
The present results suggest that a SNARE complex containing VAMP7 and Vti1a defines a novel traffic pathway to the cell surface in both neuronal and non-neuronal cells.
In adrenal chromaffin cells, vti1a localizes to a compartment near the trans-Golgi-network, but is absent from secretory granules.Vti1a is not required for final fusion of dense-core vesicles, but is needed for their generation.
VTI1A, a vesicular transport associated factor is a novel regulator of hepatitis C virus release but not replication.
Lack of the endosomal SNAREs vti1a and vti1b led to significant impairments in neuronal development
V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers.
vesicle transport through interaction with t-SNAREs homolog 1A
, vesicle transport through interaction with t-SNAREs homolog 1A (yeast)
, SNARE Vti1a-beta protein
, vesicle transport v-SNARE protein Vti1-like 2
, vesicle transport through interaction with t-SNAREs 1 homolog