Monoclonal Anti-Human Heparanase 1 (HPA1) Antibody
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Introduction:
Heparanase is an endo-β-D-glucuronidase, which degrades heparin 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 an 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 HP130 is a Protein G affinity purified monoclonal antibody raised against the 65 kDa Heparanase precursor. It recognizes the Cterminal region of both the latent pro-Heparanase and the active heterodimeric enzyme.

Ig Class:
Mouse IgG1κ

Product:
Each vial contains 100 μg of Mab HP130 in 500 μl of 0.22 micron filtered solution of 20 mM Sodium Phosphate; 150 mM NaCl; pH 7.2, containing 0.01% Thimerosal.

Applications:
Mab HP130 was shown to be active in:
FACS and Immunofluorescence analysis (9,10)
Immunohistochemistry (IHC) (11,12,13,14,15,16, 20)
Western blot (7,11,12,17,19,21)
Immunoprecipitation (IP) (18)

Specifocoty:
In immunoblot analysis Mab HP130 reacts with the 50 kDa subunit and with the 65 kDa precursor of human Heparanase.
Western blot analysis: recommended dilution range 1:200 (1μg/ml).
IHC: recommended dilution range: 1:20 (10μg/ml).
The antibodies cross react with the chicken Heparanase.

Purity:
>95% on SDS-PAGE.

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 Mab HP130 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. 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.
9. M. Bitan, A. Polliack, G. Zecchina, A. Nagler, Y. Friedmann, L. Nadav, V. Deutsch, I. Pecker, A. Eldor, I. Vlodavsky, and B.Z. Katz. 2002. Heparanase expression in human leukemias is restricted to acute myeloid leukemias. Exp. Hematol. 30: 34–41.
10. S. Benhamron, H. Nechushtan, I. Verbovetski, A. Krispin, G. Abboud-Jarrous, E. Zcharia, E. Edovitsky, E. Nahari,T. Peretz, I Vlodavsky, and D. Mevorach. 2006. Translocation of active Heparanase to cell surface regulates degradation of extracellular matrix heparan sulfate upon transmigration of mature monocytederived dendritic cells. J. Immunol. 176: 6417-6424.
11. L. Nadav, A. Eldor, O.Yacoby-Zeevi, E. Zamir, I. Pecker, N. Ilan, B. Geiger, I. Vlodavsky, and B.Z. Katz. 2002. Activation, processing and trafficking of extracellular Heparanase by primary human fibroblasts. J. Cell Science 115, 2179-2187.
12. J.P. Li, M. L. Escobar Galvis, F. Gong, X. Zhang,, E. Zcharia, S. Metzger, I.Vlodavsky, R. Kisilevsky, and U. Lindahl. 2005. In vivo fragmentation of heparan sulfate by Heparanase overexpression renders mice resistant to amyloid protein amyloidosis. Proc. Natl. Acad. Sci. 3(102): 6473-6477.
13. O. Goldshmidt, R. Yeikilis, N. Mawasi, M. Paizi, N. Gan, N. Ilan, O. Pappo, I. Vlodavsky and G. Spira. 2004. Heparanase expression during normal liver development and following partial hepatectomy. J. Pathol. 203: 594–602.
14. S. Gingis-Velitski, A. Zetser, V. Kaplan, O. Ben-Zaken, E. Cohen, F. Levy-Adam, Y. Bashenko, M. Y. Flugelman, I. Vlodavsky, and N. Ilan. 2004. Heparanase uptake is mediated by cell membrane heparan sulfate proteoglycans. J. Biol. Chem. 279(42): 44084-44092.
15. O. Goldshmidt, L Nadav, H. Aingorn, I. Cohen, N. Feinstein, N. Ilan, E. Zamir, B. Geiger, I. Vlodavsky and B. Z. Katz. 2002. Human Heparanase is localized within lysosomes in a stable form. Exp. Cell Res. 281:50–62.
16. O. Goldshmidt, E. Zcharia, H. Aingorn, Z. Guatta-Rangini, R. Atzmon, I. Michal, I. Pecker, E. Mitrani and I. Vlodavsky. 2001. Secretion and expression pattern of human and chicken Heparanase are determined by their signal peptide sequences. J. Biol. Chem. 276.
17. Y. Xiao. J. Kleeff , X. Shi, M.W. Büchler, and H. Friess. 2003. Heparanase expression in hepatocellular carcinoma and the cirrhotic Liver. Hepatology Res. 26:192 -198.
18. A. Zetser, F. Levy-Adam, V. Kaplan, S. Gingis-Velitski, Y. Bashenko, S. Schubert, M. Y. Flugelman, I. Vlodavsky, and N. Ilan. 2004. Processing and activation of latent Heparanase occurs in lysosomes . J. Cell Sci. 117: 2249-2258.
19. E. Zcharia, R. Zilka, A. Yaar, O.Yacoby-Zeevi, A. Zetser, S. Metzger, R. Sarid, A. Naggi, B. Casu, N. Ilan, I. Vlodavsky and R. Abramovitch. 2005. Heparanase accelerates wound angiogenesis and wound healing in mouse and rat models. FASEB J. 19: 211-221.
20. V. Temkin, H. Aingorn, I. Puxeddu, O. Goldshmidt, E. Zcharia, G. J. Gleich, I. Vlodavsky, and F. Levi-Schaffer. 2004. Eosinophil major basic protein: First identified natural Heparanase-inhibiting protein. J Allergy Clin. Immunol. 113: 703-709.
21. P. Beckhove, B. M. Helmke, Y. Ziouta, M. Bucur, W. Dorner, C. Mogler, G. Dyckhoff, and C. Herold-Mende. 2005. Heparanase expression at the invasion front of human head and neck cancers and correlation with poor prognosis. Clin. Cancer Res. 11(08): 2899-2906

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