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Rab8A (show RAB8A Proteins) GTPase (show RACGAP1 Proteins) Ser (show SIGLEC1 Proteins)(111) phosphorylation is not directly regulated by PINK1 (show PINK1 Proteins) in vitro and demonstrate in cells the time course of Ser (show SIGLEC1 Proteins)(111) phosphorylation of Rab8A (show RAB8A Proteins), 8B and 13 is markedly delayed compared to phosphorylation of Parkin (show PARK2 Proteins) at Ser (show SIGLEC1 Proteins)(65).
Rab8b is involved in trafficking of WNV particles from recycling endosomes to the plasma membrane.
Simultaneous loss of Rab8a (show RAB8A Proteins) and Rab8b has little effect on ciliogenesis, whereas additional loss of Rab10 (show RAB10 Proteins) greatly affects ciliogenesis.
Rab8b siRNA diminished autophagic killing of BCG, reduced the number of LC3 puncta in a high-content imaging analysis of cells stably expressing fluorescent protein fusion with LC3 and impeded basal clearance of the autophagic adaptor p62.
These results suggest that the interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions.
Otoferlin-Rab8b interaction links otoferlin to the basolateral endocytic and secretory trafficking.
RAB proteins, like RAB8B, are low molecular mass monomeric GTPases that localize on the cytoplasmic surfaces of distinct membrane-bound organelles. RAB proteins function in intracellular vesicle transport by aiding in the docking and/or fusion of vesicles with their target membranes (summary by Chen et al., 1997
RAB8B, member RAS oncogene family
, RAB-8b protein
, ras-related protein Rab-8B
, RAB44, member RAS oncogene family
, GTPase Rab8b