PEPD Antibody / Peptidase D, 100 ug

PEPD antibody detects Peptidase D, a cytosolic metalloprotease involved in the final step of collagen degradation and proline recycling. PEPD hydrolyzes dipeptides containing proline or hydroxyproline at the carboxy terminus, contributing to amino acid salvage and collagen turnover. The PEPD antibody is widely used in metabolism, connective tissue, and enzymology research to study peptide hydrolysis, collagen catabolism, and metabolic disorders.

PEPD is encoded by the PEPD gene located on human chromosome 19q13.11. The protein is approximately 493 amino acids long and requires manganese as a cofactor for catalytic activity. PEPD functions as a homodimer, with each subunit contributing to the active site. It is expressed in a wide range of tissues, particularly in the liver, kidney, and fibroblasts, where it facilitates collagen metabolism and amino acid homeostasis.

The PEPD antibody detects a 54 kilodalton band by western blot and shows cytosolic distribution under immunofluorescence microscopy. PEPD participates in proline recycling for collagen resynthesis, making it essential for connective tissue maintenance and wound healing. Mutations in PEPD cause prolidase deficiency, a rare metabolic disorder characterized by skin ulcers, developmental delay, and recurrent infections due to impaired collagen degradation and imbalanced proline metabolism.

In addition to its metabolic role, PEPD modulates cell signaling by acting as an extracellular ligand for epidermal growth factor receptor (EGFR), activating proliferative and survival pathways in response to tissue injury. It also influences immune responses by regulating proline-derived metabolites that affect macrophage activation and oxidative balance.

Because PEPD connects collagen metabolism, cell signaling, and tissue repair, it serves as an important target in research on fibrosis, wound healing, and metabolic disorders. NSJ Bioreagents provides a validated PEPD antibody optimized for its applications, supporting investigations into collagen turnover, amino acid metabolism, and regenerative biology.