Recombinant Human RPLP0 protein

**Background of RPLP0 Recombinant Protein**

The ribosomal protein lateral stalk subunit P0 (RPLP0), also known as acidic ribosomal phosphoprotein P0. is a core component of the 60S ribosomal subunit. It plays a critical role in translation elongation by forming the "stalk" structure along with P1 and P2 proteins, facilitating GTPase interaction during the peptide chain elongation cycle. As a housekeeping gene product, RPLP0 is constitutively expressed across tissues, making it a common reference control in gene expression studies (e.g., qPCR, Western blot). However, its expression may vary under certain pathological conditions, such as cancer or ribosomopathies, necessitating cautious interpretation.

Recombinant RPLP0 protein is engineered using bacterial (e.g., *E. coli*) or eukaryotic expression systems to study its structural and functional roles. The bacterial system offers high yield but lacks post-translational modifications, while mammalian systems (e.g., HEK293 cells) preserve native modifications. Purified recombinant RPLP0 is widely utilized to investigate ribosome assembly, protein synthesis mechanisms, and interactions with translational regulators. It also serves as an antigen for antibody development and a standard in diagnostic assays (e.g., ELISA).

In disease research, RPLP0 dysregulation is linked to tumor progression, chemotherapy resistance, and viral infections (e.g., hepatitis C), where ribosomal functions are hijacked. Recombinant variants enable exploration of these pathways and therapeutic targeting. Challenges include ensuring proper folding, solubility, and stability during production, as well as addressing species-specific homology in cross-reactive studies.

Overall, RPLP0 recombinant protein is a vital tool for dissecting ribosome biology and disease mechanisms, though its application requires careful experimental design to account for contextual expression variability and technical constraints.