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Sec5 (show EXOC2 ELISA Kits), Sec6 (show EXOC3 ELISA Kits) and Sec8 act as a complex, each member dependent on the others for proper localization and function
No evidence that Sec8 is required for basal neurotransmission, though glutamate (show GRIN2A ELISA Kits) receptor trafficking was mildly disrupted in sec8 mutants.
Sec8 regulates N-cadherin (show CDH2 ELISA Kits) expression by controlling Smad3 (show SMAD3 ELISA Kits) and Smad4 (show SMAD4 ELISA Kits) expression through CBP (show CREBBP ELISA Kits), thereby mediating the epithelial-mesenchymal transition.
Sec8 regulate Bcl-2 (show BCL2 ELISA Kits) and Mcl-1 (show MCL1 ELISA Kits) expressions but not Bcl-xl (show BCL2L1 ELISA Kits) in malignant peripheral nerve sheath tumor cells.
Sec8 regulates histone-modifying proteins ATF2 (show ATF2 ELISA Kits) and RNF20 (show RNF20 ELISA Kits).
Sec8 knockdown in HSC3 cells resulted in reduced expressions of PAK1 (show PAK1 ELISA Kits) and PAK2 (show PAK2 ELISA Kits) by upregulating Pirh2 (show RCHY1 ELISA Kits) and Siah1 (show SIAH1 ELISA Kits) expression, which inhibited the ERK (show EPHB2 ELISA Kits) or p38 MAPK (show MAPK14 ELISA Kits) signalling pathway and cytokeratin8 phosphorylation and cell migration.
knockdown of Sec8 enhances the binding of JIP4 (show SPAG9 ELISA Kits) to MAPK (show MAPK1 ELISA Kits) kinase 4, thereby decreasing the phosphorylation of MAPK (show MAPK1 ELISA Kits) kinase 4, JNK (show MAPK8 ELISA Kits), and p38 (show CRK ELISA Kits).
Exome sequencing revealed a likely pathogenic mutation in three novel candidate MKS (show MKS1 ELISA Kits) disease genes-C5orf42, EVC2 (show EVC2 ELISA Kits) and SEC8 (also known as EXOC4), which encodes an exocyst protein with an established role in ciliogenesis
High Sec8 expression is associated with progression of oral squamous-cell carcinoma by secretion of matrix metalloproteinases.
EXOC4 is involved in insulin (show INS ELISA Kits)-stimulated glucose transport and may be a candidate for an association with type 2 diabetes.
The exocyst subunits Sec3 (show EXOC1 ELISA Kits) and Sec8 interact with the polarity protein IQGAP1 (show IQGAP1 ELISA Kits) and that this interaction is triggered by active Cdc42 (show CDC42 ELISA Kits) and RhoA (show RHOA ELISA Kits), which are essential for matrix degradation.
SAP102 (show DLG3 ELISA Kits) interacts with the PDZ (show INADL ELISA Kits)-binding domain of Sec8, a member of the exocyst complex. Interactions between the two proteins are involved in the delivery of N-methyl-D-aspartate receptors to the cell surface in heterologous cells and neurons.
the exocyst complex serves to selectively regulate the docking of insulin (show INS ELISA Kits)-containing vesicles at sites of release close to the plasma membrane
Sec8 controls the directional movement of AMPA (show GRIA3 ELISA Kits) receptors towards synapses through PDZ (show INADL ELISA Kits)-dependent interactions.
Insulin (show INS ELISA Kits) stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes.
Interaction of Discs large 1 (Dlg1 (show DLG4 ELISA Kits)) with the Sec8 exocyst component promotes membrane addition, whereas with myotubularin-related protein 2 (Mtmr2 (show MTMR2 ELISA Kits)), negatively regulates membrane formation.
The amount of pectinaceous mucilage and seed coat structure in sec8 and exo70A1 exocyst mutants, was characterized.
An allelic series of six independent T-DNA mutations reveal a role for SEC8 in male gametophyte function.
SEC8 copurifies in a high molecular mass fraction of 900 kD, interacts with SEC6 (show EXOC3 ELISA Kits), and functions as a subunit in a exocyst complex that plays important roles in morphogenesis.
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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
, funnel cakes
, SEC8 protein
, exocyst complex component 4
, SEC8-like 1
, exocyst complex component Sec8
, augmenter of liver regeneration (ALR) pseudogene
, secretory protein SEC8