Anti-Rab8 antibody produced in rabbit

Rab proteins contain conserved regions involved in guanine-nucleotide binding and hypervariable COOH-terminal domains with a cysteine motif. Rab8 localizes to the trans-Golgi network (TGN), recycling endosomes, tubular structures in the cytosol, membrane protrusions and plasma membrane.

Anti-Rab8 antibody produced in rabbit has been used in immunoblotting and immunofluorescence staining.

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 guanosine triphosphate (GTPases) regulate vesicle formation, actin- and tubulin-dependent vesicle movement and membrane fusion. The guanine-nucleotide binding and hypervariable COOH-terminal domains are implicated in subcellular targeting. Each Rab shows a characteristic subcellular distribution. Therefore, antibodies to Rab proteins may serve as useful tools for studying subcellular localization and membrane organization.

Rab8 (Ras-related protein Rab-8A) controls polarized trafficking, that helps in the formation of protrusion, ciliogenesis or intestinal epithelial. It may involve in the malignant development of EC (endometrial cancer). In human, Rab8 also participates in the dengue virus infection. It controls the translocation of in muscle cells.

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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