Heparanase 1 (HPA1), Polyclonal

Product Name: Heparanase 1 (HPA1), Polyclonal

Product No: ANT-155

Synonym(s): Heparanase 1 (HPA1), Polyclonal Rabbit Anti-Human

Application: Western blotImmunohistochemistry

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

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

Specificity: 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.

Patent Protected Countries: 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.

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 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.

Special Note(s): 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.