Rab7 is a member of the Rab family of small guanosine triphosphatases (GTPases). Rab proteins contain conserved regions involved in guanine nucleotide binding, and hypervariable COOH-terminal domains with a cysteine motif, implicated in subcellular targeting. Each Rab protein shows a characteristic subcellular distribution. The antibody is affinity-purified using the immunizing peptide immobilized on agarose.
Rab family of small guanosine triphosphatases (GTPases) are central regulators of membrane trafficking between the different subcellular compartments of the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP-bound inactive and GTP-bound active states. Conversion from one state to the other is regulated by GDP/GTP exchange factors (GEPs), GDP dissociation inhibitors (GDIs) and GTPase-activating proteins (GAPs). 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. Through their effector proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. Rab7 is also involved in the maturation of late autophagic vacuoles. Among Rab7 effectors are RILP (Rab-interacting lysosome protein) that controls late endosomal and lysosomal transport by mediating the recruitment of dynein/dynactin motors, Rabring7 (Rab7- interacting ring finger protein),(10) and the hVPS34/p150 complex. Anti-Rab7 may be used as a marker for late endosomes.
