Abstract: The present disclosure provides compositions and methods for site-specific labeling of antibodies by proximity-based sortase-mediated ligation. The ligation method utilizes a non-canonical isopeptide ligation reaction catalyzed by newly identified variants of S. aureus sortase A. An antibody binding domain (e.g., protein A or protein G) is fused to the variants of SrtA to bring the enzyme into close proximity of an antibody, thereby significantly increases the efficiency of isopeptide bond formation.

Abstract: The present disclosure relates to a class of engineered polypeptides having a binding affinity for interleukin-6, and provides an IL-6 binding polypeptide comprising the sequence EEX3X4AWX7EIH X11 LPNLX16X17X18QX20 X21AFIX25X26LX28X29. The present disclosure also relates to the use of such an IL-6 binding polypeptide as a therapeutic, prognostic and/or diagnostic agent.

Abstract: The present disclosure relates to a class of engineered polypeptides having a binding affinity for interleukin-6, and provides an IL-6 binding polypeptide comprising the sequence EEX3X4AWX7EIH X11 LPNLX16X17X18QX20 X21AFIX25X26LX28X29. The present disclosure also relates to the use of such an IL-6 binding polypeptide as a therapeutic, prognostic and/or diagnostic agent.

Abstract: A protein structure capable of selective interaction with an organic target is provided. The protein structure is a polymer comprising as a repeating structural unit a recombinant fusion protein that is capable of selective interaction with the organic target. The fusion protein is comprising the moieties B, REP and CT, and optionally NT. B is a non-spidroin moiety of more than 30 amino acid residues, which provides the capacity of selective interaction with the organic target. REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein. CT is a moiety of from 70 to 120 amino acid residues and is derived from the C-terminal fragment of a spider silk protein. NT is an optional moiety of from 100 to 160 amino acid residues and is derived from the N-terminal fragment of a spider silk protein. The fusion protein and protein structure thereof is useful as an affinity medium and a cell scaffold material.

Abstract: The present invention relates to a class of engineered polypeptides having a binding affinity for albumin. It also relates to new methods and uses that exploit binding by these and other compounds to albumin in different contexts, some of which have significance for the treatment of disease in mammals including humans.

Abstract: A recombinant fusion protein comprising the moieties Band CT, and optionally REP, wherein B is comprising at least one immunoglobulin fragment, which provides the capacity of selective interaction with an organic target; CT is a moiety of from 70 to 120 amino acid residues and is derived from the C-terminal fragment of a spider silk protein; and REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein.

Abstract: A protein structure capable of selective interaction with an organic target is provided. The protein structure is a polymer comprising as a repeating structural unit a recombinant fusion protein that is capable of selective interaction with the organic target. The fusion protein is comprising the moieties B, REP and CT, and optionally NT. B is a non-spidroin moiety of more than 30 amino acid residues, which provides the capacity of selective interaction with the organic target. REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein. CT is a moiety of from 70 to 120 amino acid residues and is derived from the C-terminal fragment of a spider silk protein. NT is an optional moiety of from 100 to 160 amino acid residues and is derived from the N-terminal fragment of a spider silk protein. The fusion protein and protein structure thereof is useful as an affinity medium and a cell scaffold material.

Abstract: The present invention relates to a class of engineered polypeptides having a binding affinity for albumin. It also relates to new methods and uses that exploit binding by these and other compounds to albumin in different contexts, some of which have significance for the treatment of disease in mammals including humans.

Abstract: The present invention relates to a method for detecting the presence or non-presence of an endotoxin, characterized in that an OmpT protein is brought into contact with a sample suspected of containing an endotoxin and the protease activity of the OmpT protein is assayed. It also relates to a method for detecting early onset of septicaemia using the inventive method and a kit for performing the method.

Abstract: The present invention relates to a nucleic acid molecule or a polypeptide that is selected from a method that includes cell-free expression of nucleic acid molecules immobilized on a sold support system. The present invention also relates to a molecular library that has a solid support system having a plurality of nucleic acid molecules immobilized thereon.

Abstract: A method for the selection of one or more desired polypeptides includes cell free expression of nucleic acid molecules immobilized on a solid support system to produce polypeptides. The solid support carrying system is for biospecific interaction with at least the desired polypeptide or a molecule attached thereto. The method also includes separation of the solid support carrying both the desired polypeptide and the nucleic acid encoding it. Finally, the method optionally includes recovery of the nucleic acid and/or the desired polypeptide, and molecular libraries for use in these methods.

Abstract: A sandwich assay method for detecting the presence of a target molecule in a sample comprising a complex biological fluid is provided. The assay comprises providing a first affinity ligand with affinity for the target molecule, which affinity ligand is capable of being immobilized to a solid support; applying the sample in such a way that binding of a target molecule, if present in the sample, to the first affinity ligand is enabled; applying a second affinity ligand with affinity for the target molecule, the application enabling binding of the second affinity ligand to the target molecule; removing second affinity ligand not bound to target molecule; and detecting the presence of the second affinity ligand, such presence being an indicator of the presence of a target molecule in the sample. The first affinity ligand is immobilized to the solid support at any stage before said detection, and at least one of the first and second affinity ligands is an affinity ligand other than an antibody.

Abstract: The present invention relates to methods of detecting the presence of target molecules in a sample, in particular protein target molecules. In particular, the invention provides a method of detecting the presence of a target molecule in a sample which comprises contacting said sample with a detector protein, said detector protein being a binding partner for said target molecule and being derivatized by two fluorescent reporter groups, the energy transfer between said reporter groups undergoing a detectable change on binding of the target molecule to said detector protein and a detector protein molecule having a binding site for a target molecule and having covalently attached thereto two fluorescent reporter groups, the energy transfer between said reporter groups undergoing a detectable change on binding of the target molecule to said detector protein. The detector protein comprises or consists f a combinatorial protein.

Abstract: The present invention provides a method of producing an insulin C-peptide, which comprises expressing in a host cell a multimeric polypeptide comprising multiple copies of a said insulin C-peptide, and cleaving said expressed polypeptide to release single copies of the insulin C-peptide.

Abstract: The present invention provides a method of producing an insulin C-peptide, which comprises expressing in a host cell a multimeric polypeptide comprising multiple copies of the insulin C-peptide, and cleaving the expressed polypeptide to release single copies of the insulin C-peptide. Also provided are nucleic acid molecules, expression vectors and host cells, for use in such a method and the multimeric insulin C-peptide polypeptide expressed and cleaved in such a method.

Abstract: The present invention relates to a process for improving the immunogenicity of an immunogen, an antigen or a hapten, when it is administered to a host, independently of the mode of administration, characterized in that the said antigen or hapten is coupled covalently to a support molecule in order to form a complex, and in that this support molecule is a polypeptide fragment which is able to bind specifically to mammalian serum albumin. The invention also relates to the use, as a medicament, of the product which can be obtained in this way.

Abstract: A method for obtaining a Staphylococcus carnosus bacterium expressing at its membrane surface a recombinant polypeptide derived from RSV protein G, said polypeptide having a sequence which is a modification of SEQ ID No. 1 and SEQ ID No. 2 (sequence encompassed between residues 130 and 230 of RSV A and RSV B protein G respectively) wherein at least one of position 44 and 57 is serine is disclosed.