Technoclone Anti-uPA Polyclonal Antibody, 1mg

Reacts with urokinase and its complexes; no reaction with other plasma proteins. Can be used as precipitating antibody in RIA (2,3), as antibody in an ELISA (3) or for immunoaffinity purification of urokinase (4).

Immunizing antigen

High molecular weight urokinase

Immunized species



The antibody is purified from rabbit serum by ammonium sulphate precipitation followed by DEAE ion-exchange chromatography.

Characteristics of the antibody

(1) Reacts with high and low molecular weight urokinase as well with scu-PA (urine, tissue culture and recombinant); also reacts with u-PA inhibitor complexes.


The antibody is lyophilized from a 1 mg/ml solution in isotonic phosphate buffered saline, pH 7.4, containing 0.02% sodium azide and 20 mg/ml mannitol. It is supplied in vials of 1mg and should be reconstituted with 1mL distilled water.

For extensive dilutions a protein containing solution should be used (e.g. 1% bovine serum albumin in PBS).

Lyophilized antibody should be stored at 4°C. Reconstituted antibody should be aliquoted and stored at -20°C or lower. Avoid repeated freeze-thaw cycles.

1) K.Huber, J.Kirchheimer, B.R.Binder: Rapid isolation of high molecular weight urokinase from native human urine. Thromb.Haemost. 47: 197 – 202, 1982.

2) K.Huber, J.Kirchheimer, B.R.Binder: Characterization of a specific anti-human urokinase antibody: development of a sensitive competition radioimmunoassay for urokinase antigen. J.Lab.Clin.Med. 103: 684 – 694, 1984.

3) J.Wojta, B.R.Binder, K.Huber, R.L.Hoover: Evaluation of fibrinolytic capacity in plasma during thrombolytic therapy with single (scu-PA) or two chain urokinase type plasminogen activator (tcu-PA) by a combined assay system for urokinase type plasminogen activator antigen and function. Thromb. Haemost. 61: 289-293,1989.

4) B.Grasl, M.Jörg, B.R.Binder: Isolation of a plasminogen activator from human plasma by affinity chromatography on anti-urokinase-Sepharose. Partial characterization of the enzyme. In: Progress in fibrinolysis, Vol. 6, Churchill Livingstone, Edinburgh, London, Melbourne, New York, pp. 50-53, 1983.