An ELISA method for the detection and quantification of human heparanase

Itay Shafat, Eyal Zcharia, Benjamin Nisman, Yona Nadir, Farid Nakhoul, Israel Vlodavsky, Neta Ilan

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80 Scopus citations


Heparanase is a mammalian endo-β-D-glucuronidase that cleaves heparan sulfate side chains at a limited number of sites. Heparanase enzymatic activity is thought to participate in degradation and remodeling of the extracellular matrix and to facilitate cell invasion associated with tumor metastasis, angiogenesis, and inflammation. Traditionally, heparanase activity was well correlated with the metastatic potential of a large number of tumor-derived cell types. More recently, heparanase upregulation was detected in an increasing number of primary human tumors, correlating, in some cases, with poor postoperative survival and increased tumor vascularity. The present study was undertaken to develop a highly sensitive ELISA suitable for the determination and quantification of human heparanase in tissue extracts and body fluids. The assay preferentially detects the 8 + 50 kDa active heparanase heterodimer vs. the latent 65 kDa proenzyme and correlates with immunoblot analysis of heparanase containing samples. It detects heparanase at concentrations as low as 200 pg/ml and is suitable for quantification of heparanase in tissue extracts and urine.

Original languageEnglish
Pages (from-to)958-963
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 24 Mar 2006
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by grants from the Israel Science Foundation (Grant 532/02); National Cancer Institute, NIH (Grant RO1-CA106456); the Israel Cancer Research Fund; and the Rappaport Family Institute Fund.


  • Antibody
  • Heparanase
  • Urine


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