Abstract: The present invention provides modified primers for use in the amplification of a nucleic acid sequence. Amplifications carried out using the modified primers result in less template-independent non-specific product (primer dimer) compared to amplifications carried out using unmodified primers.

Abstract: The present invention provides modified primers for use in the amplification of a nucleic acid sequence. Amplifications carried out using the modified primers result in less template-independent non-specific product (primer dimer) compared to amplifications carried out using unmodified primers.

Abstract: The present invention is directed to an isolated and purified, recombinant, unglycosylated and dimeric CSF-1, the dimeric CSF-1 being biologically active and essentially endotoxin and pyrogen-free, the dimeric CSF-1 consisting essentially of two monomeric human CSF-1 subunits. The present invention is further directed to pharmaceutical compositions comprising the same.

Abstract: The present invention is directed to a biologically active CSF-1 dimer comprising a first CSF-1 monomer and a second CSF-1 monomer, wherein at least one of the monomers is truncated at the C-terminus after residue position 223. The dimers also include point mutations in one or both of the CSF-1 monomer. The invention also includes pharmaceutical compositions that comprise the CSF-1 dimer in a pharmaceutical excipient.

Abstract: The present invention relates to the production of CSF-1 heterodimers and pharmaceutical formulations of the heterodimers. The heterodimers can be formed using CSF-1 monomers that have variations in sequence, N or C-terminal processing. For example, CSF/C.gradient.150 can be dimerized with LCSF/C.gradient. 190 to form a heterodimer. Dimerization may occur by separately preparing homodimers and mixing them together under the appropriate conditions. Thereafter, homodimers may be separated from the heterodimers by various chromatographic techniques. Once the heterodimers are isolated, pharmaceutical preparations can be prepared.

Abstract: A biologically active CSF-1 protein is selectively conjugated via certain amino acid residues or carbohydrate moieties to a water-soluble polymer selected from polyethylene glycol or polypropylene glycol homopolymers, polyoxyethylated polyols, or polyvinyl alcohol. The resulting conjugated CSF-1 is biologically active and has increased circulating half-life in mammals, compared to that of the unconjugated protein. The conjugated CSF-1 may be used to stimulate the immune response or to provide more cells to be stimulated.

Abstract: Immunotoxins comprising a cytotoxic moiety and monoclonal antibodies which bind to human ovarian cancer tissue having at least one of the following capabilities are claimed: cytotoxic ID.sub.50 of 10 nM or less against human ovarian cancer cells, retardation of human ovarian cancer tumor growth in mammals or extension of survival of a mammal carrying a human ovarian cancer tumor. Antigens to which the monoclonal antibody of the immunotoxin bind are identified and characterize the immunotoxins. Methods of killing human ovarian cancer cells, retarding the growth of human ovarian cancer tumors in mammals or extending the survival of mammals carrying human ovarian cancer tumors are claimed.

Abstract: Immunotoxins comprising a cytotoxic moiety and an antigen binding portion selected from the group consisting of Fab, Fab' and F(ab').sub.2 fragments of a monoclonal antibody, which binds to human ovarian cancer tissue, having one of the following capabilities are claimed: cytotoxic ID.sub.50 of about 10 nM or less against human ovarian cancer cells, retardation of human ovarian cancer tumor growth in mammals, or extension of survival of a mammal carrying a human ovarian cancer tumor. Antigens or epitopes to which the monoclonal antibodies bind are identified and characterize the immunotoxins. In a preferred embodiment an immunotoxin comprising at least an antigen binding portion of a monoclonal antibody, which binds to human transferrin receptor, but does not block binding of transferrin to the receptor, is described and claimed. Immunotoxin comprising the F(ab').sub.2 region of the antitransferrin monoclonal antibody are also claimed.

Abstract: Recombinant diphtheria toxin A fragment muteins which are enzymatically inactive but immunologically crossreactive with diphtheria toxin are disclosed. Intermediates and methods for preparing such proteins using recombinant techniques are also described.

Abstract: A system for expression of coding sequences for desired heterologous proteins in procaryotic hosts whereby the protein is produced intracellularly in soluble, biologically active form, is disclosed. The expression is obtained by ligation of the coding sequence downstream of, and proximally to, but out of reading frame with, the terminated leader encoding sequence for a secreted bacterial protein, such as alkaline phosphatase. The resultant proteins are influenced by the leader sequence codons to effect the desired three-dimensional conformation, but not to effect secretion.

Abstract: A process for recovering dimeric, biologically active CSF-1 from bacterially expressed recombinant CSF1 genes is described. The process comprises recovery of the solubilized monomeric form, followed by dimerization under refolding conditions and further purification of the dimer. Heterodimers may also be produced by this process.

Abstract: A method of isolating and purifying toxin conjugates using hydrophobic interaction chromatography. Crude conjugate mixtures are sized to remove unconjugated toxin, and loaded onto a column filled with a suitable hydrophobic gel. Elution is effected with salt solutions of decreasing ionic strength, which salt solutions optionally include increasing amounts of an organic solvent. Toxin conjugate substantially free of unconjugated Ig and unconjugated toxin is provided.