The PEPD antibody targets prolidase, a manganese-dependent dipeptidase encoded by the PEPD gene, which catalyzes the hydrolysis of imidodipeptides containing C-terminal proline or hydroxyproline. This enzyme plays a critical role in collagen turnover, recycling proline for protein synthesis and tissue repair. PEPD deficiency, a rare autosomal recessive disorder, is linked to chronic skin ulcers, recurrent infections, and developmental delays, underscoring its biological importance.
PEPD antibodies are essential tools in biomedical research, enabling the detection and quantification of prolidase expression in tissues or cell lysates through techniques like Western blotting, immunohistochemistry (IHC), and ELISA. These antibodies aid in studying PEPD's role in connective tissue disorders, neurodegenerative diseases, and cancer, where altered prolidase activity has been implicated. Recent studies also explore PEPD's potential involvement in modulating insulin signaling and oxidative stress, expanding its relevance to metabolic and age-related conditions.
Structurally, prolidase functions as a homodimer, requiring manganese ions for activation. PEPD antibodies often recognize specific epitopes within conserved regions, ensuring cross-reactivity across species like humans, mice, and rats. Commercial PEPD antibodies are typically validated for specificity using knockout controls or siRNA-mediated gene silencing. Researchers utilize these reagents to investigate PEPD's subcellular localization, enzymatic activity regulation, and interactions with other proteins, contributing to therapeutic development for PEPD-associated pathologies.