Anti-uPAR (human, urokinase plasminogen activator receptor)
Mouse monoclonal antibody
Cat.No. MON R-3
Preparation: Protein-A purified
Content: Available in 200 µL and 1 mL
Concentration: 1 mg/mL
Solvent: 0.01 M phosphate buffer, pH 7.4, with 0.5 M NaCl and 15 mM sodium azide
Storage: In the dark at 4-8ºC
Urokinase plasminogen activator receptor (uPAR), also known as CD87, is a glycolipid anchored cell surface protein consisting of three homologous domains. It binds uPA with high affinity and enhances and localizes uPA catalyzed plasminogen activation, and thereby plays a key role in cancer invasion and in several tissue remodelling processes (1-3). In addition uPAR also binds to vitronectin and may thereby have biological functions independent of its role in uPA mediated proteolysis (4,5). Elevated levels of uPAR are associated with poor prognosis in many types of cancer (2,3,6,7).
Native human uPAR
MON R-3 is specific for human uPAR. No cross-reactivity is observed with murine uPAR, human uPA, human tPA or human PAI-1 when tested by ELISA and immunoblotting.
MON R-3 reacts with an epitope on domain 1 and differs from that of MON R-5
MON R-3 reacts with native uPAR (8), but not with reduced protein. MON R-3 reacts with domain 1 when tested by immunoprecipitation of proteolytic fragments of recombinant suPAR. It is suitable for Western blotting of non-reduced proteins (9). MON R-3 inhibits uPAs binding to uPAR in solution and on cells. MON R-3 can be used as detection antibody in ELISA
| Method | Usability | Dilution guideline | References |
| ELISA | Yes | 1/1000 | 7, 10 |
| Immunoblotting | Yes | 9 | |
| Immunohistochemistry | Not determined |
The dilution guideline for ELISA is based on use as detection antibody. Users should determine the optimal dilutions for their own purposes.
1. Llinas P, Le Du MH, Gårdsvoll H, Danø K, Ploug M, Gilquin B, Stura EA, Ménez A (2005) Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide. EMBO J 24:1655-1663.
2. Andreasen PA, Kjøller L, Christensen (1997) The urokinase plasminogen activator system in cancer metastasis. A review. Int J Cancer 2:1-22.
3. Danø K, Behrendt N, Høyer-Hansen G, Johnsen M, Lund LR, Ploug M, Rømer J (2005) Plasminogen activation and cancer. Thromb Haemo 93:676-681.
4. Mazzier R, Blasi F (2005) The urokinase receptor and the regulation of cell proliferation. Thromb Haemo 93:641-646.
5. Madsen CD, Ferraris GM, Andolfo A, Cunningham O, Sidenius NJ (2007) uPAR-induced cell adhesion and migration: vitronectin provides the key. Cell Biol 177:927-939.
6. Stephens RW, Nielsen HJ, Christensen IJ, Thorlacius-Ussing O, Danø K, Brünner N (1999) Plasma urokinase receptor in colorectal cancer patients: Relation to prognosis. J Natl Cancer Inst 91:869-874.
7. Grøndahl-Hansen J, Peters HA., van Putten WLJ, Look MP, Pappot H, Rønne E, Danø K, Klijn JGM, Brünner N, Foekens JA (1995) Prognostic significance of the receptor for urokinase plasminogen activator in breast cancer. Clin Cancer Res 1:1079-1087
8. Rønne E, Behrendt N, Ellis V, Ploug M, Danø K, Høyer-Hansen G (1991) Cell induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2 -terminal domain of the urokinase receptor. FEBS Lett 288:233 236.
9. Solberg H, Rømer J, Brünner N, Holm A, Sidenius N, Danø K, Høyer-Hansen G (1994) A cleaved form of the receptor for urokinase-type plasminogen activator in invasive transplanted human and murine tumors. Int J Cancer 58:877-881.
10. Rønne E, Høyer-Hansen G, Brünner N, Pedersen H, Rank F, Osborne CK, Clark GM, Danø K, Grøndahl-Hansen J (1995) Urokinase-receptor in breast cancer tissue extracts. Enzyme-linked immunosorbent assay with a combination of mono- and polyclonal antibodies. Breast Cancer Res Treatm 33:199-207.
