HPSE (E3N3H) Rabbit mAb #99756

Heparanase (HPSE) is an endo-β-D-endoglycosidase that catalyzes the cleavage heparan sulfate (HS) side chains from proteoglycans at the cell surface (1). The protein is synthesized as a 65 kDa inactive precursor that undergoes proteolytic processing, yielding 8 kDa and 50 kDa protein subunits that heterodimerize to form an active enzyme (2). HPSE serves as a key modulator of extracellular matrix (ECM) basic structure. The cleavage of HS from proteoglycans and associated changes at the ECM also cause the release of growth factors from the matrix to bind to their cognate receptors, leading to activation of downstream signaling pathways (3). A small percentage of HPSE localizes to specialized lipid raft regions. There, HPSE activates multiple signaling pathways, such as Akt, ERK, and Src pathways, by a nonenzymatic mechanism mediated by its C-terminal domain (4,5). HPSE is involved in the development of diseases such as fibrosis initiation, inflammation, tumor progression, and viral infection (6-9). HPSE inhibitors have been developed and pursued as novel therapeutics for these diseases (10-12).