Heparanase (HPSE) antibody

Antigen: Heparanase (HPSE)

Synonyms: HPA, HPR1, HSE1, HPSE1, Hpa, Hpr1, Hep, HPSE, im:7144134

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Application: Western Blotting (WB), Immunohistochemistry (IHC)

Catalog no.: ABIN335036

Additional Information

Alternative name: Heparanase-1

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

Description: Heparanase is an endo b-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 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).

Application Details

Application Notes: Western blot analysis: The antibody reacts with the 65 kDa precursor as well as the 50kDa and 8 kDa subunits of human or mouse Heparanase. The antibody interacts with Heparanase in paraffin sections and blood smears. Recommended dilution range for Western blot analysis: 1:1000. Recommended dilution range for immunohistochemistry: 1:100.

Buffer: Each vial contains 0.24 mg or 0.48 mg of antibody in 100 or 200ul respectively of 20mM sodium phosphate 150 mM NaCl

Storage: Store at 4

Restrictions: For Research Use only

Publications

Publications: Vlodavsky, Korner, Ishai-Michaeli et al.: "Extracellular matrix-resident growth factors and enzymes: possible involvement in tumor metastasis and angiogenesis." in: Cancer metastasis reviews, Vol. 9, Issue 3, pp. 203-26, 1991 (PubMed).

Bashkin, Doctrow, Klagsbrun et al.: "Basic fibroblast growth factor binds to subendothelial extracellular matrix and is released by heparitinase and heparin-like molecules." in: Biochemistry, Vol. 28, Issue 4, pp. 1737-43, 1989 (PubMed).

Vlodavsky, Friedmann, Elkin et al.: "Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis." in: Nature medicine, Vol. 5, Issue 7, pp. 793-802, 1999 (PubMed).

Fairbanks, Mildner, Leone et al.: "Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer." in: The Journal of biological chemistry, Vol. 274, Issue 42, pp. 29587-90, 1999 (PubMed).

Parish, Freeman, Hulett: "Heparanase: a key enzyme involved in cell invasion." in: Biochimica et biophysica acta, Vol. 1471, Issue 3, pp. M99-108, 2001 (PubMed).

Koliopanos, Friess, Kleeff et al.: "Heparanase expression in primary and metastatic pancreatic cancer." in: Cancer research, Vol. 61, Issue 12, pp. 4655-9, 2001 (PubMed).

Vlodavsky, Friedmann: "Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis." in: The Journal of clinical investigation, Vol. 108, Issue 3, pp. 341-7, 2001 (PubMed).

Gohji, Hirano, Okamoto et al.: "Expression of three extracellular matrix degradative enzymes in bladder cancer." in: International journal of cancer. Journal international du cancer, Vol. 95, Issue 5, pp. 295-301, 2001 (PubMed).