Rab35 is a member of the Rab GTPase family, which regulates intracellular vesicle trafficking, membrane dynamics, and organelle organization. As a small GTP-binding protein, Rab35 cycles between active GTP-bound and inactive GDP-bound states, mediated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). It plays critical roles in endocytic recycling, cytokinesis, neurite outgrowth, and receptor signaling. Dysregulation of Rab35 is linked to cancer progression, neurodevelopmental disorders, and immune response defects.
Rab35 antibodies are essential tools for studying its expression, localization, and function. These antibodies, often produced in rabbits or mice, target specific epitopes of Rab35 for applications like Western blotting, immunofluorescence, immunoprecipitation, and flow cytometry. Monoclonal antibodies offer high specificity, while polyclonal antibodies may detect diverse isoforms. Validated antibodies help assess Rab35’s involvement in cellular processes or diseases by identifying overexpression, phosphorylation, or interaction partners.
Research using Rab35 antibodies has revealed its role in exosome secretion, autophagy, and cytoskeletal remodeling. Commercial antibodies typically undergo validation via knockout cell lines or siRNA knockdown to confirm target specificity. Proper controls, like isotype-matched IgG or lysates from Rab35-deficient models, are critical to avoid off-target artifacts. Overall, Rab35 antibodies are pivotal in elucidating its contributions to cellular homeostasis and pathology.