Abstract: A method is disclosed to make any protein in a form that can be isolated rapidly from a solution using a specific monoclonal antibody designated "HPC-4". It has now been determined that it is possible to form a fusion protein of the epitope with a protein to be isolated, and isolate the protein using HPC-4-based affinity chromatography. In the preferred embodiment, a specific protease cleavage site is inserted between the epitope and the protein so that the epitope can be easily removed from the isolated protein. In an example, a functionally active soluble tissue factor including the twelve amino acid epitope recognized in combination with calcium by HPC-4 and a factor Xa cleavage site was expressed from a vector inserted into a procaryotic expression system. The recombinant tissue factor can be rapidly isolated in a single chromatographic step using the HPC-4 monoclonal antibody immobilized on a suitable substrate.

Abstract: Murine hybridomas producing monoclonal antibodies capable of immunoreacting with huTFh and polypeptide analogs are described. Also contemplated are immunologic methods for detecting huTF heavy chain in body fluid, detecting thrombic events in vivo, isolating coagulation factor, and neutralizing VII/VIIa coagulation factor binding in vivo.

Abstract: DNA segments include DNA sequences defining a structural gene coding for a human tissue factor heavy chain protein and a precursor form of that protein are disclosed. Recombinant DNA molecules capable of expressing a human tissue factor heavy chain protein are also disclosed. Further disclosed are human tissue factor heavy chain binding site polypeptide analogs as well as methods for their use.

Abstract: In a silver stain method for protein in gels utilizing treatment with a reducing agent followed by treatment with a silver salt and actuating irradiation, the improvement comprising the use of a reducing agent consisting essentially of dithiothreitol in an amount effective to stain the protein but keep background staining to a minimum.