This recombinant protein product features a 246-amino acid fragment (residues 269-514) of the human Nuclear receptor ROR-alpha (RORA), encompassing the complete ligand-binding domain (LBD). It serves as an essential tool for investigating RORA's roles in circadian rhythm, metabolism, immune function, and development, offering researchers a domain-specific reagent for functional and interaction studies.

Nuclear receptor ROR-alpha (RORA) is a key transcriptional regulator in Homo sapiens, localized to the nucleus, where it binds as a monomer to ROR response elements. It is critically involved in embryonic development, cellular differentiation, lipid and glucose metabolism, circadian rhythm regulation, and immune responses, such as T-helper 17 cell differentiation. RORA exhibits intrinsic transcriptional activity modulated by ligands like oxysterols and interacts with cofactors to influence genes including those for clock components (e.g., BMAL1, CRY1), metabolic enzymes (e.g., CYP7B1), and immune factors (e.g., IL17). Its functions span photoreceptor and cerebellum development, hypoxia signaling, and anti-inflammatory pathways, making it a pivotal protein in physiological and disease contexts.