The HRAS antibody is a crucial tool in molecular and cancer research, targeting the HRAS protein—a small GTPase belonging to the RAS family. HRAS plays a pivotal role in regulating cell signaling pathways, including the MAPK/ERK and PI3K/AKT cascades, which control cell proliferation, differentiation, and survival. Mutations in the HRAS gene (e.g., G12V, G13D) result in constitutively active HRAS proteins, driving uncontrolled cell growth and contributing to tumorigenesis. These mutations are linked to various cancers, such as bladder, thyroid, and colorectal carcinomas, as well as developmental disorders like Costello syndrome.
HRAS antibodies are designed to detect endogenous HRAS protein levels, localization, and activation status in experimental models. They are widely used in techniques like Western blotting (WB), immunohistochemistry (IHC), immunofluorescence (IF), and flow cytometry. Specific antibodies may distinguish between wild-type and mutant HRAS or recognize post-translational modifications (e.g., farnesylation) critical for membrane localization and function. Monoclonal antibodies offer high specificity, while polyclonal variants may detect broader epitopes.
In research, HRAS antibodies help elucidate oncogenic mechanisms, evaluate therapeutic targets (e.g., RAS inhibitors), and assess drug efficacy in preclinical studies. Their application extends to diagnostic pathology for identifying HRAS-driven malignancies. Given the challenges in directly targeting RAS proteins, these antibodies remain vital for studying downstream effectors and compensatory pathways in cancer biology.