A panel of monoclonal antibodies (Mab) recognizing at least four epitopes of Tamm-Horsfall protein (TH P), or Uromodulin, the specific kidney antigen and most abundant urine protein, was developed. All epitopes retain their ability to bind Mab after protein deglycosilation. Three Mab are directed to a cluster of conformation-dependent spatially close epitopes. The interaction with these determinants was increased after reduction of TH P by means of dithiothhreitol Among others the first Mab recognizes linear epitope in the stretch including Zona pellucid domain, the second one interacts with epitope located in elastase-sensitive part of molecule, the third is specific to determinant topographically isolated from all other mentioned epitopes. On the basis of developed Mab a multideterminant ELISA system for TH P determination in urine was constructed. The mixture of three Mab recognizing different epitopes of TH P were used for capture the antigen on the solid phase. As developing reagent the peroxidase-labelled Mab directed to most spatially isolated epitope was used. Calibrating samples were prepared on the basis of TH P purified from the urine of healthy individuals and solibilised in the buffer preventing its aggregation. Mab also may be used for affinity purification and for investigation of TH P structure.