Recombinant Human XPNPEP2 protein

**Background of XPNPEP2 Recombinant Protein**

XPNPEP2 (X-prolyl aminopeptidase 2), also known as membrane-bound prolyl carboxypeptidase (PRCP), is a zinc-dependent metalloprotease encoded by the *XPNPEP2* gene. It belongs to the M24B aminopeptidase family and plays a critical role in cleaving N-terminal proline residues from bioactive peptides, including bradykinin, angiotensin metabolites, and other regulatory substrates. This enzyme is predominantly localized to cell membranes and mitochondria, where it modulates peptide signaling pathways involved in blood pressure regulation, inflammation, and energy metabolism.

The recombinant XPNPEP2 protein is produced via genetic engineering in heterologous expression systems, such as *E. coli* or mammalian cell lines, to ensure high purity and bioactivity. Its recombinant form enables detailed biochemical studies, including substrate specificity, enzymatic kinetics, and inhibitor screening. Research has linked XPNPEP2 dysfunction to human diseases, such as hypertension, diabetic nephropathy, and autosomal recessive renal tubular dysfunction. Notably, mutations in *XPNPEP2* are associated with a rare genetic disorder causing hyperuricemia, renal stones, and progressive kidney failure.

In drug discovery, recombinant XPNPEP2 serves as a target for developing therapeutics targeting the renin-angiotensin and kallikrein-kinin systems. Additionally, it aids in biomarker studies for metabolic and cardiovascular disorders. Its role in degrading vasoactive peptides highlights its potential in modulating vascular tone and inflammation. Continued research on XPNPEP2 recombinant protein aims to unravel its physiological relevance and therapeutic applications in precision medicine.