Recombinant Human UBL5 protein

UBL5 (Ubiquitin-like protein 5) is a small, highly conserved protein belonging to the ubiquitin-like protein family, which shares structural similarities with ubiquitin but serves distinct regulatory roles. Unlike ubiquitin, UBL5 does not directly participate in proteasomal degradation but is implicated in diverse cellular processes, including transcriptional regulation, RNA splicing, and stress response. It is evolutionarily conserved across eukaryotes, highlighting its fundamental biological importance. In humans, UBL5 interacts with components of the spliceosome, such as the SART3 complex, to modulate pre-mRNA splicing. It also plays a role in the DNA damage response and mitochondrial function, linking it to cellular homeostasis and disease pathways.

Recombinant UBL5 protein is typically produced using bacterial or mammalian expression systems, enabling large-scale purification for functional and structural studies. Its recombinant form retains the ability to fold into the characteristic β-grasp ubiquitin-like fold, critical for interactions with partner proteins. Researchers utilize UBL5 recombinant protein to explore its binding partners, enzymatic activity, and post-translational modifications. Studies have revealed its involvement in stress adaptation, particularly under heat shock or oxidative conditions, where it may act as a molecular chaperone or signaling mediator. Additionally, UBL5 has been linked to metabolic regulation and neurodegenerative disorders, making it a potential therapeutic target. Its small size (∼10 kDa) and solubility facilitate experimental applications in crystallography, NMR, and biochemical assays. Ongoing research aims to clarify its precise mechanisms and tissue-specific functions, leveraging recombinant UBL5 as a tool to dissect its role in health and disease.