Rab5 is a 24kDa member of the Rab family of small guanosine triphosphatases (GTPases), Ras superfamily. Rab GTPases are central regulators of membrane trafficking in the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP -bound inactive and GTP- bound active states. This conversion is regulated by GDP/GTP exchange factors (GEPs), GDP dissociation inhibitors (GDIs) and GTPase-activating proteins (GAPs) (1, 2). Activation of a Rab protein is coupled to its association with intracellular membranes, allowing it to recruit downstream effector proteins to the cytoplasmic surface of a subcellular compartment (3). Through these proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion(1). Rab proteins contain conserved regions involved in guanine-nucleotide binding, and hypervariable COOH-terminal domains with a cysteine motif implicated in subcellular targeting. Post-translational modification of the cysteine motif with one or two geranyl groups is essential for the membrane association and correct intracellular localization of Rab proteins(3). Each Rab shows a characteristic subcellular distribution (4). In particular, Rab5 is ubiquitously expressed in human tissues. It localizes mainly to early endosomes, but is also present on the plasma membrane. It regulates the fusion between endocytic vesicles and early endosomes, as well as the homotypic fusion between early endosomes (5). Among the proteins recruited by the GTP-bound active Rab5 are Rabaptin-5 and EEA1 (6). Anti-Rab5 may be used as an early endosome marker.