Heparanase 2 (HPSE2) is a member of the heparanase protein family, sharing structural homology with heparanase 1 (HPSE1), a well-studied endo-β-glucuronidase that cleaves heparan sulfate (HS) chains in the extracellular matrix (ECM). Unlike HPSE1. HPSE2 lacks enzymatic activity due to critical amino acid substitutions in its catalytic domain. Instead, it is hypothesized to function as a regulator, potentially modulating HPSE1 activity or interacting with HS-binding proteins to influence ECM remodeling, cell signaling, and tissue homeostasis.
HPSE2 is expressed in various tissues, including the kidneys, bladder, and nervous system. Research links HPSE2 mutations to urofacial syndrome (UFS), a rare autosomal recessive disorder characterized by urinary bladder dysfunction and congenital facial anomalies. This association highlights its role in developmental and functional processes of the urinary tract.
HPSE2 antibodies are essential tools for investigating its biological roles, localization, and expression patterns. They are widely used in techniques like immunohistochemistry, Western blotting, and immunofluorescence to study HPSE2 in disease models, particularly UFS and cancer, where altered HS metabolism may contribute to pathogenesis. Recent studies also explore HPSE2's potential tumor-suppressive effects, contrasting with HPSE1's pro-tumorigenic properties. Further research aims to clarify its regulatory mechanisms and therapeutic relevance.