ANTI-RAS-ASSOCIATED PROTEIN

Monoclonal Anti-Rab7 antibody produced in mouse may be used in ELISA, immunoblotting (~24 kDa), immunoprecipitation, immunohistochemistry, immunofluorescence and immunocytochemistry.

Rab7 is a member of the Rab family of small guanosine triphosphatases (GTPases). This family belongs to the rat sarcoma (Ras) superfamily of small GTPases. 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 geranylgeranyl groups is essential for the membrane association and correct intracellular localization of Rab proteins. The gene Rab7a in human chromosome is mapped to 3q21.3.

Rab GTPases are central regulators of membrane trafficking between different subcellular compartments in eukaryotic cells. The regulatory capacity of Rab GTPases depends on their ability to cycle between the GDP-bound inactive and GTP-bound active states. Activation of Rab proteins is coupled to their association with intracellular membranes, allowing them 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 regulates vesicle traffic from early to late endosomes, and from late endosomes to lysosomes. Rab7 is also involved in the maturation of late autophagic vacuoles. Among Rab7 effectors are Rab-interacting lysosome protein (RILP) that controls late endosomal and lysosomal transport by mediating the recruitment of dynein/dynactin motors, Rab-7-interacting ring finger protein (Rabring7) and the hVPS34/p150 complex.