The Rab proteins are small GTP-binding molecules that are localized to specific intracellular vesicles and organelles, and are important for vesicular traffic. It is thought that Rab proteins cycle through GTP- and GDP-bound forms and that this cycle is related to their function. Four highly homologous (77-85% identity) Rab3 proteins have been described: Rab3A, Rab3B, Rab3C, and Rab3D. Rab3A reportedly is expressed in neuronal and neuroendocrine cells and is associated with synaptic and synaptic-like vesicles. Rab3A is involved at a late stage of neurotransmitter exocytosis, perhaps at the recruitment of vesicles at the presynaptic membrane. Rab3B and Rab3C are also reportedly predominantly expressed in neurons and neuroendocrine tissues. In contrast, Rab3D has been reported to be highly enriched in fat cells and probably does not function sequentially in the same exocytic pathway as Rab3A.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.