Monoclonal Anti-Human Heparanase 1 (HPA1) Antibody
Clon HP3/17                                                                                                 Download as PDF

Background:
Heparanase is an endo-b-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).

Type:
Monoclonal Antibody.

Source:
Mab HP3/17 is a Protein G affinity purified monoclonal antibody raised against a polypeptide from the 50 kDa subunit of Heparanase.

Ig Class:
Mouse IgG2Bk

Product:
Each vial contains 50, 100 or 150 μg in 12.5, 25 or 37.5 μl respectively, of 0.22 micron filtered solution of 20 mM Sodium Phosphate; 150 mM NaCl; pH 7.2, containing 0.001% Thimerosal.

Applications:
Western blot
Immunohistochemistry

Specificity:
HP3/17 reacts with the 50 kDa subunit and with the 65 kDa precursor of human or mouse Heparanase by Western blotting and immunohistochemistry.
Recommended dilution range for Western blot analysis: 1:4000.
Recommended dilution range for immunohistochemistry: 1:40.

Purity:
>98% on SDS-PAGE when loaded 50 µg/lane.

Storage:
Store at 4˚C. Stable for six months from the date of shipment. For extended storage, freeze in working aliquots at -20˚C. Avoid repeated freeze-thaw cycles.

Research use:
For in vitro research use only. Not for use in diagnostic procedures.

Patents:
Anti-heparanase antibodies and their uses, including HP3/17 and its uses, are protected by US. Patents No. 6,177,545; 6,531,129, additional US patent applications and patents and patent applications worldwide.

References:
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 and metastasis. Nat. Med. 5: 793–802.
2. I. Vlodavsky, Y. Friedman. 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. Vlodasvsky, G. Korner, R. Ishai-Michaeli, P. Bashkin, R. Bar-Shavit, 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, 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. 1992. 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