Recombinant Human PPIL3 protein

PPIL3 (Peptidylprolyl Isomerase Like 3) is a member of the cyclophilin family, a group of proteins characterized by their ability to catalyze the cis-trans isomerization of proline peptide bonds, a critical step in protein folding and conformational regulation. This post-translational modification activity, known as PPIase (peptidylprolyl isomerase) activity, is essential for modulating protein structure, stability, and interactions. PPIL3 shares structural homology with other cyclophilins, particularly in its conserved cyclophilin-like domain, but exhibits distinct tissue expression patterns and functional roles.

Initially identified through genomic sequencing, PPIL3 is encoded in humans by the *PPIL3* gene located on chromosome 2. While its biological functions remain less characterized compared to well-studied cyclophilins like cyclophilin A (CypA), emerging evidence suggests PPIL3 involvement in transcriptional regulation, RNA splicing, and cellular stress responses. It interacts with components of the spliceosome complex, hinting at a role in mRNA processing. Additionally, PPIL3 may participate in signaling pathways linked to apoptosis and immune regulation, though mechanistic details are still under investigation.

Recombinant PPIL3 protein is engineered for in vitro studies to elucidate its biochemical properties and interactions. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains PPIase activity and serves as a tool for structural analysis (e.g., X-ray crystallography) or screening for inhibitors. Its recombinant form is particularly valuable in dissecting its potential involvement in diseases such as cancer, neurodegenerative disorders, or viral infections, where cyclophilin dysregulation is implicated. Recent studies also explore PPIL3's utility as a biomarker or therapeutic target, though further functional validation is required to fully understand its pathophysiological relevance.