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Human Monoclonal EXOC3 Primary Antibody for ELISA, WB - ABIN524747
Imai, Yoshie, Haga-Tsujimura, Nashida, Shimomura: Exocyst subunits are involved in isoproterenol-induced amylase release from rat parotid acinar cells. in European journal of oral sciences 2012
Show all 2 Pubmed References
Sec5, Sec6 and Sec8 act as a complex, each member dependent on the others for proper localization and function
Sec6 is an exocyst complex component believed to bind secretory vesicles to plasma membrane sites. Sec6 mutations cause cell death and disrupt plasma membrane growth. In developing photoreceptor cells (PRCs) Sec6 shows accumulation at adherens junctions
The Drosophila exocyst component sec6 in epithelial cells results in DE-Cad accumulation in an enlarged Rab11 recycling endosomal compartment and inhibits DE-Cad delivery to the membrane.
In PRsec6 mutants, primary root growth was retarded, and lateral root initiation were compromised. Primary roots were sensitive to exogenous auxin 1-napthalene acetic acid but not 2,4-dichlorophenoxy. The results further demonstrated that the exocyst complex plays an important role in PIN protein recycling and polar auxin transport in Arabidopsis primary root.
results demonstrated that, like KEULE, SEC6 plays a physiological role in cytokinesis, and the SEC6-KEULE interaction may serve as a novel molecular linkage between arriving vesicles and membrane fusion
SEC6 copurifies in a high molecular mass fraction of 900 kD, interacts with SEC8, and functions as a subunit in a exocyst complex that plays important roles in morphogenesis.
Sec6 increased the phosphorylation of p38 MAPK through the activation of MAPK kinase 3/6 (MKK3/6). Moreover, Sec6 knockdown suppressed the phosphorylation of HSP27 at Ser(78) and Ser(82) sites via suppression of activated MK2.
Sec6 regulate Bcl-2 and Mcl-1 expressions but not Bcl-xl in malignant peripheral nerve sheath tumor cells.
Sec6 regulates NF-kappaB transcriptional activity via the control of the phosphorylation of IkappaBalpha, p90RSK1, and ERK
The study explores the role of the exocyst complex component Sec6/8 in genomic stability.
Sec6 regulates cytoplasmic translocation of p27 through p27 phosphorylation at Thr157, thereby promoting p27 degradation in the cytoplasm via interaction with Jab1 and Siah1 and suppressing cell cycle progression.
Data demonstrate that the expression of alpha-E-catenin is increased by Sec6 siRNAs, and E-cadherin and beta-catenin localize mainly at the cell-cell contact region in HSC3 cells, which were transfected with Sec6 siRNA.
the exocyst complex serves to selectively regulate the docking of insulin-containing vesicles at sites of release close to the plasma membrane
The protein encoded by this gene is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. The complex is also essential for the biogenesis of epithelial cell surface polarity.
, exocyst complex component 3
, SEC6-like 1
, Sec 6 homolog
, exocyst complex component Sec6
, Sec6 protein