The RPL8A antibody is a specialized immunological tool designed to detect and study ribosomal protein L8A (RPL8A), a conserved component of the eukaryotic 60S ribosomal subunit. This antibody plays a critical role in investigating ribosomal biogenesis, protein synthesis, and quality control mechanisms. RPL8A is essential for rRNA processing and ribosome assembly, with its dysfunction linked to translational inefficiencies and cellular stress responses .
ABIN2855107: Validated in HepG2, Molt-4, and mouse brain tissues .
16981-1-AP: Confirmed specificity in HepG2 and MCF-7 cell lines via Western blot (WB) .
Studies in Saccharomyces cerevisiae reveal that RPL8A undergoes ubiquitin-independent CTPD when nascent polypeptide folding is inefficient. Key findings include:
Degron Exposure: The N-terminal region (residues 1–100) of RPL8A contains a degron that triggers degradation if folding is delayed. This degron is masked in mature RPL8A through interactions with its C-terminal domain .
Ubiquitin Fusion Experiments: Adding an N-terminal ubiquitin (Ub) moiety to RPL8A stabilizes the protein by inhibiting CTPD, as shown by elevated steady-state levels in Ub-RPL8Aha strains compared to wild-type .
RPL8A interacts with ABF2, a mitochondrial DNA-binding protein, suggesting cross-compartmental regulatory roles in yeast . This interaction highlights RPL8A’s potential involvement in mitochondrial genome maintenance and stress responses.