Heparanase is an endo ß-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).

Polyclonal rabbit anti-human HPA1 is a Protein G affinity purified polyclonal antibody raised against the 50 kDa-8 kDa Heparanase heterodimer.

Each vial contains 0.29 mg or 0.57 mg of antibody in 50 or 100 µL, respectively, of 20 mM sodium phosphate; 150 mM NaCl; pH 7.2, containing 0. 01% Thimerosal.

Western blotImmunohistochemistry

Western blot analysis: The antibody reacts with the 65 kDa precursor as well as the 50 kDa and 8 kDa subunits of human or mouse Heparanase.Immunohistochemistry: The antibody interacts with Heparanase in paraffin sections and blood smears.Recommended dilution range for Western blot analysis: 1:2000.Recommended dilution range for immunohistochemistry: 1:100.

Store at 4°C. For extended storage, freeze in working aliquots at -20°C.Avoid repeated freeze-thaw cycles.

Polyclonal and monoclonal Anti-heparanase antibodies and their uses are protected by US. Patents No. 6,177,545; 6,531,129, additional US patent applications and patents and patent applications worldwide.

1. I. Vlodavsky, Y. Friedmann, M. Elkin, H. Aingorn, R. Atzmon, R. Ishai-Michaeli, M. Bitan, O. Pappo, T. Peretz, I. Michal, L. Spector, I. Pecker. 1999. Mammalian heparanase: gene cloning, expression and function in tumor progression andmetastasis. Nat. Med. 5: 793-802.2. I. Vlodavsky, Y. Friedmann. 2001. Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J. Clin. Invest. 108: 341-347.3. C.R. Parish, C. Freeman, M.D. Hulett. 2001. Heparanase: a key enzyme involved in cell invasion. Biochem. Biophys. Acta 1471: M99-M108.4. I. Vlodavsky, G. Korner, R. Ishai-Michaeli, P. Bashkin, R. Bar-Shavit, and Z. Fuks. 1990. Extracellular matrix-resident growth factors and enzyme: Possible involvement in tumor metastasis and angiogenesis. Cancer Metastasis Rev. 9: 203-226.5. P. Bashkin, S. Doctrow, M. Klagsbrun, C.M. Svahn, J. Folkman, and I. Vlodavsky. 1989. Basic fibroblast growth factor binds to subendothelial extracellular matrix and is released by heparitinase and heparin-like molecules. Biochemistry 28: 1737-1743.6. M.B. Fairbanks, A.M. Mildner, J.W. Leone, G.S. Cavey, W.R. Mathews, R.F. Drong, J.L. Slightom, M.J. Bienkowski, C.W. Smith, C.A. Bannow, R.L. Heinrikson. 1999. Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer. J. Biol. Chem. 274: 29587-29590.7. A. Koliopanos, H. Friess, J. Klee, X. Shi, Q. Liao, I. Pecker, I. Vlodavsky, A. Zimmermann, M.W. Buchler. 2001. Heparanase expression in primary and metastatic pancreatic cancer. Cancer Res. 61: 4655-4659.8. K. Gohji, H. Hirano, M. Okamoto, S. Kitazawa, M. Toyoshima, J. Dong, Y. Katsuoka, M. Nakajima. 2001. Expression of three extracellular matrix degradative enzymes in bladder cancer. Int. J. Cancer 95: 295-301.

To view the FULL VERSION click Here:

SDS

ProSpec"s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.