The ribosomal protein S6 (RPS6) is a component of the 40S ribosomal subunit, playing a critical role in mRNA translation and cellular homeostasis. As a downstream effector of the mTOR (mechanistic target of rapamycin) signaling pathway, RPS6 is phosphorylated at specific serine residues (e.g., Ser235/236. Ser240/244) in response to growth factors, nutrients, or stress, regulating ribosome biogenesis and protein synthesis. Antibodies targeting RPS6 or its phosphorylated forms (p-RPS6) are widely used as biomarkers to study mTOR pathway activity, cellular proliferation, and metabolic states in various contexts, including cancer, immune responses, and neurodegenerative diseases.
RPS6 antibodies are essential tools in basic and translational research, enabling detection of mTORC1 activation via techniques like Western blotting, immunofluorescence, and immunohistochemistry. They help elucidate mechanisms underlying diseases linked to dysregulated mTOR signaling, such as tuberous sclerosis, diabetes, and cancer. Additionally, p-RPS6 antibodies are used to assess drug efficacy in preclinical studies, particularly for mTOR inhibitors like rapamycin.
The specificity of RPS6 antibodies varies depending on the epitope targeted, with some recognizing total RPS6 and others specific to phosphorylated isoforms. Validation in relevant experimental models is crucial to ensure accurate interpretation. Overall, RPS6 antibodies serve as vital reagents for probing translational regulation and cellular adaptation in health and disease.