Abstract: The invention relates to MIC-1 fusion proteins. More specifically it relates to compounds comprising fusion proteins comprising a MIC-1 protein or an analogue thereof at the C-terminus of the fusion protein and a functional variant of human A1AT (A1AT) at the N-terminus of the fusion protein connected via a peptide linker. The compounds of the invention have MIC-1 activity. The invention also relates to pharmaceutical compositions comprising such compounds and pharmaceutically acceptable excipients, as well as the medical use of the compounds.

Abstract: The present invention provides a method for producing peptides by recombinant means. The peptides are expressed as part of a fusion protein comprising the target peptide and an engineered intein. The invention also provides the engineered inteins, fusion proteins comprising these, and DNA constructs coding for these fusion proteins. Upon thiol-induced cleavage of the fusion protein the carboxy-terminal a-thioester of the target peptide is obtained. The carboxy-terminal ?-thioester can in principle react with any nucleophile and the strategy therefore allows a wider range of carboxy-terminal modifications such as chemical ligation, bioconjugation, or amidation.

Abstract: This invention relates to novel bifunctional fusion proteases useful for manufacturing a mature protein from a fusion protein. More specifically the present invention relates to bifunctional fusion proteases comprising a picornaviral 3C protease and a Xaa-Pro-dipeptidyl aminopeptidase.

Abstract: The present invention provides a method for producing peptides by recombinant means. The peptides are expressed as part of a fusion protein comprising the target peptide and an engineered intein. The invention also provides the engineered inteins, fusion proteins comprising these, and DNA constructs coding for these fusion proteins. Upon thiol-induced cleavage of the fusion protein the carboxy-terminal a-thioester of the target peptide is obtained. The carboxy-terminal ct-thioester can in principle react with any nucleophile and the strategy therefore allows a wider range of carboxy-terminal modifications such as chemical ligation, bioconjugation, or amidation.

Abstract: The present patent application concerns an enzyme capable of catalysing the conversion of a ?-hydroxyglycine to an ?-amide and the use of such enzymes for producing a C-terminal ?-amidated peptide.

Abstract: The invention relates to MIC-1 fusion proteins. More specifically it relates to compounds comprising fusion proteins comprising a MIC-1 protein or an analog thereof at the C-terminus of the fusion protein and a functional variant of human serum albumin at the N-terminus of the fusion protein connected via a peptide linker. The compounds of the invention have MIC-1 activity. The invention also relates to pharmaceutical compositions comprising such compounds and pharmaceutically acceptable excipients, as well as the medical use of the compounds.

Abstract: The invention relates to MIC-1 fusion proteins. More specifically it relates to compounds comprising fusion proteins comprising a MIC-1 protein or an analogue thereof at the C-terminus of the fusion protein and a functional variant of human serum albumin at the N-terminus of the fusion protein connected via a peptide linker. The compounds of the invention have MIC-1 activity. The invention also relates to pharmaceutical compositions comprising such compounds and pharmaceutically acceptable excipients, as well as the medical use of the compounds.

Abstract: The invention is related to a method for purification of recombinant proteins using highly basic proteins from thermophilic bacteria as purification tags for use in a cation-exchange chromatography purification step. The basic proteins may be ribosomal proteins. The recombinant proteins are expressed in eukaryotic or prokaryotic host cells. The purification tag will typically have a pl above about 9 and comprise from about 15 to about 250 amino acid residues.

Abstract: The invention is related to processing enzyme comprising an N-terminally attached tag derived from highly basic proteins from thermophilic bacteria. The processing enzymes are useful for modifying proteins. They can be produced in high yields and can be effectively separated from the modified protein after use.

Abstract: The invention is related to processing enzyme comprising an N-terminally attached tag derived from highly basic proteins from thermophilic bacteria. The processing enzymes are useful for modifying proteins. They can be produced in high yields and can be effectively separated from the modified protein after use.

Abstract: The invention is related to processing enzyme comprising an N-terminally attached tag derived from highly basic proteins from thermophilic bacteria. The processing enzymes are useful for modifying proteins. They can be produced in high yields and can be effectively separated from the modified protein after use.

Abstract: The invention is related to a method for purification of recombinant proteins using highly basic proteins from thermophilic bacteria as purification tags for use in a cation-exchange chromatography purification step. The basic proteins may be ribosomal proteins. The recombinant proteins are expressed in eukaryotic or prokaryotic host cells. The purification tag will typically have a pl above about 9 and comprise from about 15 to about 250 amino acid residues.

Abstract: The invention is related to a method for purification of recombinant proteins using highly basic proteins from thermophilic bacteria as purification tags for use in a cation-exchange chromatography purification step. The basic proteins may be ribosomal proteins. The recombinant proteins are expressed in eukaryotic or prokaryotic host cells. The purification tag will typically have a pl above about 9 and comprise from about 15 to about 250 amino acid residues.

Abstract: The invention is related to processing enzyme comprising an N-terminally attached tag derived from highly basic proteins from thermophilic bacteria. The processing enzymes are useful for modifying proteins. They can be produced in high yields and can be effectively separated from the modified protein after use.

Abstract: The invention is related to processing enzyme comprising an N-terminally attached tag derived from highly basic proteins from thermophilic bacteria. The processing enzymes are useful for modifying proteins. They can be produced in high yields and can be effectively separated from the modified protein after use.

Abstract: The invention is related to processing enzyme comprising an N-terminally attached tag derived from highly basic proteins from thermophilic bacteria. The processing enzymes are useful for modifying proteins. They can be produced in high yields and can be effectively separated from the modified protein after use.

Abstract: The invention is related to a method for purification of recombinant proteins using highly basic proteins from thermophilic bacteria as purification tags for use in a cation-exchange chromatography purification step. The basic proteins may be ribosomal proteins. The recombinant proteins are expressed in eukaryotic or prokaryotic host cells. The purification tag will typically have a pl above about 9 and comprise from about 15 to about 250 amino acid residues.

Abstract: The present invention relates to a novel combination of methods that enables identification of proteins secreted from intracellular bacteria regardless of the secretion pathway. The invention further provides proteins that are identified by these methods. Secreted proteins are known to be suitable candidates for inclusion in immunogenic compositions and/or diagnostic purposes. The invention also provides peptide epitopes (T-cell epitopes) from the identified secreted proteins, as well as nucleic acid compounds that encode the proteins. The invention further comprises various applications of the proteins or fragments thereof, such as pharmaceutical and diagnostic applications.