PA1389XC rec. human Heparanase antigen
see all 3 rec. human Heparanase products
0.3 µg / please contact our distributor
NOVUS BIOLOGICALS
PO Box 802 Littleton, CO 80160, USA
E-Mail: novus@novus-biologicals.com
Homepage: http://www.novus-biologicals.com
PO Box 802 Littleton, CO 80160, USA
E-Mail: novus@novus-biologicals.com
Homepage: http://www.novus-biologicals.com
Quick Overview
Human rec. human Heparanase
Synonyms
HPA, HPSE,
Product Description
Human rec. human Heparanase
Properties
| Presentation | Purified |
| Species | Human |
| Source | CHO cells |
| Molecular Weight | 65/50 kD |
| Catalog Number | PA1389XC |
| Quantity | 0.3 µg |
| Price | please contact our distributor |
| Delivery | Worldwide |
| Manufacturer | Acris Antibodies GmbH |
| Datasheet | view  PA1389XC.pdf |
Datasheet Extract
| Alternate names | HEP, HPA, HPA1, HPR1, HPSE1, HSE1
|
| Concentration | 1.0 µg/ml |
| Background | 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 (7,8,9). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (10,11). 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 (1,12). 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 (13, 14). |
| Source | CHO cells |
| Format | State: Liquid BufferSystem: LDS-PAGE buffer: 140 mM Tris buffer pH 8.5, 10% glycerol, 2% LDS, 0.015% EDTA, 1.88% (v/v) of 1% Serva Blue G250 and 0.625 (v/v) of 1% Phenol red |
| Applications | Positive control for Western blot:
Use 20 μl of recombinant human heparanase 1 (HPA1) per lane, as a control for using monoclonal anti HPA1 clone HP3/17 antibodies or polyclonal rabbit anti HPA1 antibody. |
| Description | Recombinant Heparanase protein HPA1 - purified by several orthogonal chromatography steps
|
| Storage | Store at -20°C. Avoid repeated freezing and thawing.
Shelf life: one year from despatch. |
| References | 1. Oligomannurarate Sulfate, a Novel Heparanase Inhibitor Simultaneously Targeting Basic Fibroblast Growth Factor, Combats Tumor Angiogenesis and Metastasis. Cancer Res 2006 Sep 1;66(17):8779-8787
2. The close relationship between heparanase and cyclooxygenase-2 expressions in signet-ring cell carcinoma of the stomach. Hum Pathol 2006 Sep;37(9):1145-52 3. Development of heparanase inhibitors for anti-cancer therapy. Curr Med Chem 2006;13(18):2101-11 4. Regulation, function and clinical significance of heparanase in cancer metastasis and angiogenesis. Int J Biochem Cell Biol 2006 Jul 6. 5. Induction of glomerular heparanase expression in rats with adriamycin nephropathy is regulated by reactive ox ygen species and the Renin-Angiotensin system. J Am Soc Nephrol 2006 Sep;17(9):2513-20 6. Heparanase promotes angiogenesis through Cox-2 and HIF1alpha.Med Hypotheses 2006 Aug 3. 7. 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. 8. I. Vlodavsky, Y. Friedman. 2001. Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J. Clin. Invest. 108: 341-347. 9. C.R. Parish, C. Freeman, M.D. Hulett. 2001. Heparanase: a key enzyme involved in cell invasion. Biochem. Biophys. Acta 1471: M99-M108. 10. Shavit, Z. Fuks, 1990. Extracellular matrix-resident growth factors and enzyme: Possible involvement in tumor metastasis and angiogenesis. Cancer Metastasis Rev. 9: 203-226. 11. 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. 12. 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. 13. 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. 14. 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. Recombinant Heparanase is protected under U.S. patents no. 5,968,822; 6,348,344; 6,426,209, additional US patent applications and patents and patent applications wordwide. |
