RAB35 Human

RAB35 cycles between an inactive GDP-bound form and an active GTP-bound form. In its active state, it recruits various downstream effectors responsible for vesicle formation, movement, tethering, and fusion . This protein is essential for the fast recycling pathway back to the plasma membrane and is involved in the process of endocytosis . During cytokinesis, RAB35 is required for the postfurrowing terminal steps, including intercellular bridge stability and abscission .

RAB35 is located in several cellular components, including clathrin-coated endocytic vesicles, clathrin-coated pits, and intercellular bridges . It is also involved in the regulation of phosphatidylinositol 4,5-bisphosphate (PIP2) and SEPT2 localization at the intercellular bridge, which is crucial for cytokinesis .

Mutations or dysregulation of RAB35 have been associated with various diseases, including tetraploidy and bleeding disorder, platelet-type 19 . The gene is also involved in pathways related to Rab regulation of trafficking and vesicle-mediated transport .

The human recombinant RAB35 protein is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 221 amino acids. It has a molecular mass of approximately 25.2 kDa and is fused to a 20 amino acid His-tag at the N-terminus . This recombinant protein is purified using proprietary chromatographic techniques .

RAB35 is widely studied for its role in intracellular trafficking and its involvement in various cellular processes. It is also a subject of interest in cancer research due to its association with the RAS oncogene family. Researchers use recombinant RAB35 protein in various assays to study its function and interactions with other proteins.