Technoclone Anti-uPA Polyclonal Antibody, 5mg
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).
High molecular weight urokinase purified from human urine according to the method of Huber et al. (1).
The antibody is purified from rabbit serum by ammonium sulphate Precipitation and purity is tested by SDS-PAGE.
Characteristics of the antibody
(2) Reacts with high and low molecular weight urokinase as well as with scu-PA (urine, tissue culture and recombinant); also reacts with uPA inhibitor complexes. Functional inhibition of u-PA activity.
The antibody is lyophilized from a 5 mg/ml 50mM sodium acetate pH 5.0, solution containing 100mM glycine, and 20 mg/ml mannitol. It is supplied in vials of 5 mg and should be reconstituted with 1 ml 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