HPSE Active

Heparanase is an endo Beta-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).
Heparanase Active Enzyme is produced in CHO cells.The protein is purified by several orthogonal chromatography steps.

The specific activity of Heparanase Active Enzyme in-house standard is about 0.7 Units (1 unit = 1 µmole of reducing ends of heparan sulfate substrate formed per minute per mg Heparanase Active Enzyme at 37°C). The enzymatic activity of each Heparanase Active Enzyme batch is comparable to the standard as determined by activity assay in which immobilized heparan, released due to heparanase activity, is quantified colorimetrically. Recommended reaction buffer: 20 mM Citrate Phosphate buffer, pH 5.4; 50mM NaCl; 1mM CaCl2.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

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