PLOD2 Mouse mAb

PLOD2 (i.e., procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2, also known as lysyl hydroxylase 2) is a key collagen cross-linking enzyme encoded by the PLOD2 gene, localized in the endoplasmic reticulum lumen, where it catalyzes the hydroxylation of specific lysine residues in collagen molecules to generate hydroxylysine. This post-translational modification is critical for collagen maturation, as hydroxylysine serves not only as an essential precursor for the formation of covalent cross-links between collagen molecules but also provides the structural basis for collagen microfibril assembly and mechanical stability, exerting a decisive influence particularly on the tensile strength of collagen-rich tissues such as bone, tendons, and vascular walls. The activity of PLOD2 depends on iron ions (Fe²⁺), vitamin C (ascorbic acid), and molecular oxygen as cofactors; deficiency of these cofactors directly leads to reduced catalytic efficiency, which clinically can manifest as poor wound healing associated with scurvy. This protein also plays an important role in tissue fibrosis—its expression is upregulated by the TGF-β signaling pathway and is significantly elevated in pathological states such as liver fibrosis, pulmonary fibrosis, and scleroderma, promoting excessive cross-linked collagen deposition and exacerbating tissue stiffening. In addition, pathogenic mutations in the PLOD2 gene can lead to Bruck syndrome type 2 (a rare autosomal recessive disorder), characterized by congenital joint contractures and recurrent fractures, directly associated with increased bone fragility due to collagen cross-linking defects, while aberrant expression of this protein is also linked to keloid formation and the invasion and metastasis of certain malignancies.