Abstract: The present invention relates to a method of determining an analyte in a sample, said method comprising (a) contacting said sample with (i) a binding compound binding to said analyte, said binding compound comprising a binding agent and a first partner of an affinity pair (first affinity partner); and (ii) a second partner of the affinity pair (second affinity partner) coupled to a solid surface, to an indicator, and/or to a second binding agent; and (b) determining said analyte based on complexes formed in step (a); wherein one of said first affinity partner and said second affinity partner is a polypeptide comprising the amino acid sequence of SEQ ID NO:1 or a sequence at least 50% identical thereto, and wherein the other of said first affinity partner and said second affinity partner is a polypeptide comprising the amino acid sequence of SEQ ID NO:2 or a sequence at least 50% identical thereto.

Abstract: The present invention relates to monoclonal antibodies binding to the nucleocapsid protein of SARS-CoV-2 virus, nucleic acids encoding said antibody, host cells producing the same, compositions and kits comprising said antibodies, as well as methods of detecting SARS-CoV-2 virus in a sample comprising using said antibodies.

Abstract: The present invention relates to bacterial pilus protein complex FimGt-DsF stabilized protein complexes for producing phagemids or filamentous phages, and methods for use of these.

Abstract: The present invention relates to an antibody or an antigen binding fragment thereof that specifically binds to ?-1,6-core-fucosylated prostate specific antigen (PSA) and partial sequences thereof comprising the ?-1,6-core-fucose residue. The antibodies and antigen binding fragments significantly discriminate between core-fucosylated PSA or core-fucosylated PSA partial sequences and other glycosylated PSA species and partial sequences thereof lacking the core-fucose residue, including aglycosylated PSA, as well as core-fucosylated glycan in other contexts. The present invention further relates to nucleic acid molecules encoding the light chain variable region or the heavy chain variable region of the antibody of the invention, as well as vectors comprising said nucleic acid molecules.

Abstract: Herein is reported a polypeptide-polynucleotide-complex as therapeutic agent and its use as tool for the targeted delivery of an effector moiety. The polynucleotide part of the complex is essentially resistant to proteolytic and enzymatic degradation in vivo. Additionally the polypeptide part specifically binds to a compound or structure such as a tissue or organ, a process or a disease. Thus, one aspect as reported herein is a polypeptide-polynucleotide-complex comprising a) a polypeptide specifically binding to a target and conjugated to a first member of a binding pair, b) a polynucleotide linker conjugated at its first terminus to the second member of the binding pair, and c) an effector moiety conjugated to a polynucleotide that is complementary to at least a part of the polynucleotide linker.

Abstract: The current invention reports a method for producing an antibody comprising the steps of a) providing a plurality of hybridoma cells each expressing an antibody, b) determining the time dependent amount of said antibody bound to the respective antigen by surface plasmon resonance at different temperatures and different antibody concentrations, c) calculating with the time dependent amount determined in b) based on equations (II) to (XIII) at least the thermodynamic parameters (i) standard association binding entropy (?S°‡ass), (ii) standard dissociation binding entropy (?S°‡diss), (iii) standard binding entropy (?S°), (iv) free standard binding enthalpy (?G°), (v) standard dissociation free binding enthalpy (?G°‡diss), (vi) standard association free binding enthalpy (?G°‡ass), (vii) ?T?S°, (viii) dissociation rate constant kd, (ix) equilibrium binding constant KD, and (x) association rate constant ka, d) selecting a hybridoma cell producing an antibody with at least two of the following: i) a standard associa

Abstract: The present invention relates to a monoclonal antibody, or fragment thereof, which binds to CSF-1R (Colony stimulating factor 1 receptor), in particular to human CSF-1R. The present invention further relates to the in vitro use of the monoclonal antibody, or fragment thereof, of the present invention for the detection of CSF-1R in a sample. Further encompassed by the present invention is a complex comprising the monoclonal antibody, or fragment thereof, of the present invention and CSF-1R such as the human CSF-1R polypeptide.

Abstract: The present report relates to hybridizing single-stranded (ss-) oligonucleotides which entirely consist of locked nucleic acid (LNA) monomers. The present document shows hybridization experiments with pairs of entirely complementary ss-oligonucleotides which fail to form a duplex within a given time interval. The present report provides methods to identify such incompatible oligonucleotide pairs. In another aspect, the present report provides pairs of complementary ss-oligonucleotides which are capable of rapid duplex formation. The present report also provides methods to identify and select compatible oligonucleotide pairs. In yet another aspect the present report provides use of compatible oligonucleotide pairs as binding partners in binding assays, e.g. receptor-based assays.

Abstract: The present invention relates to an improved variant monoclonal antibody binding to cardiac troponin T and having a better KD than the parent monoclonal antibody 11-7

Abstract: The present invention relates to a monoclonal antibody capable of binding to biotin. In one embodiment the monoclonal antibody according to the invention also does not bind to a biotin moiety on a biotinylated molecule, wherein the biotin moiety is attached to the molecule via the carbon atom of the carboxyl function of the valeric acid moiety of biotin. Also disclosed is a method for generation of an antibody as disclosed herein. The monoclonal antibody according to the invention is of specific use in a method for measuring an analyte in a sample, wherein a (strept)avidin/biotin pair is used to bind a biotinylated analyte specific binding agent to a (strept)avidin coated solid phase.

Abstract: The present invention relates to a monoclonal antibody capable of binding to biotin. In one embodiment the monoclonal antibody according to the invention also does not bind to a biotin moiety on a biotinylated molecule, wherein the biotin moiety is attached to the molecule via the carbon atom of the carboxyl function of the valeric acid moiety of biotin. Also disclosed is a method for generation of an antibody as disclosed herein. The monoclonal antibody according to the invention is of specific use in a method for measuring an analyte in a sample, wherein a (strept)avidin/biotin pair is used to bind a biotinylated analyte specific binding agent to a (strept)avidin coated solid phase.

Abstract: The present invention relates to a monoclonal antibody capable of binding to biotin. In one embodiment the monoclonal antibody according to the invention also does not bind to a biotin moiety on a biotinylated molecule, wherein the biotin moiety is attached to the molecule via the carbon atom of the carboxyl function of the valeric acid moiety of biotin. Also disclosed is a method for generation of an antibody as disclosed herein. The monoclonal antibody according to the invention is of specific use in a method for measuring an analyte in a sample, wherein a (strept)avidin/biotin pair is used to bind a biotinylated analyte specific binding agent to a (strept)avidin coated solid phase.

Abstract: In one aspect, the present disclosure provides a system and method for the identification and characterization of a transglutaminase. Further, the present disclosure provides transglutaminase enzymes for forming isopeptide bonds, methods of forming isopeptide bonds in the presence of transglutaminases, and substrate tags for use with transglutaminases. In another aspect, the present disclosure provides glutamine-containing substrates (or Q-tag substrates) that are more resistant to proteases/clipping and therefore, more stable, than other Q-tag substrates, and their uses in substrate tags for cross-linking to an amine-donor tag via an isopeptide bond mediated by a microbial transglutaminase.

Abstract: According to one aspect, the present disclosure provides a method of identifying a substrate of a transglutaminase using a peptide array comprising a plurality of peptides. The method includes the steps of contacting the peptides in the peptide array with the transglutaminase, allowing the transglutaminase to bind to the peptides, and identifying the substrate of the transglutaminase.

Abstract: In one aspect, the present disclosure provides a system and method for the identification and characterization of a transglutaminase. Further, the present disclosure provides transglutaminase enzymes for forming isopeptide bonds, methods of forming isopeptide bonds in the presence of transglutaminases, and substrate tags for use with transglutaminases. In another aspect, the present disclosure provides glutamine-containing substrates (or Q-tag substrates) that are more resistant to proteases/clipping and therefore, more stable, than other Q-tag substrates, and their uses in substrate tags for cross-linking to an amine-donor tag via an isopeptide bond mediated by a microbial transglutaminase.

Abstract: The present report relates to hybridizing single-stranded (ss-) oligonucleotides which entirely consist of locked nucleic acid (LNA) monomers. The present document shows hybridization experiments with pairs of entirely complementary ss-oligonucleotides which fail to form a duplex within a given time interval. The present report provides methods to identify such incompatible oligonucleotide pairs. In another aspect, the present report provides pairs of complementary ss-oligonucleotides which are capable of rapid duplex formation. The present report also provides methods to identify and select compatible oligonucleotide pairs. In yet another aspect the present report provides use of compatible oligonucleotide pairs as binding partners in binding assays, e.g. immunoassays.

Abstract: A bivalent binding agent having a first monovalent binder that binds to a polypeptide epitope of a target polypeptide, a second monovalent binder that binds to a posttranslational polypeptide modification on the target polypeptide and a linker. Further disclosed are methods for the detection of a posttranslationally modified target polypeptide, for making the disclosed bivalent binding agent, and for use of the disclosed bivalent binding agent in histological staining procedures.

Abstract: Provided are nanopore-based methods, compositions, and systems for assessing analyte-ligand interactions and analyte concentration in a fluid solution. The compositions include an analyte detection complex that is associated with a nanopore to form a nanopore assembly, the analyte detection complex including an analyte ligand. As a first voltage is applied across the nanopore assembly, the analyte ligand is presented to an analyte in the solution. As a second voltage that is opposite in polarity to the first voltage is applied across the nanopore assembly, the analyte binds to the analyte. By comparing the total number of analyte-ligand binding pairs to a control binding count, the concentration of the analyte can be determined. In other examples, further increasing the second voltage can result in dissociation of the analyte-ligand pair, from which a dissociation voltage—and hence a dissociation constant—can be determined.

Abstract: The present invention relates to a novel monoclonal antibody that specifically binds to a conformation dependent epitope on human thymidine kinase 1 (hTK-1; SEQ ID NO:1), to methods for quantifying hTK-1 employing the antibody and to the use of the anti-hTK-1 antibody in quantifying hTK-1.

Abstract: The present invention relates to a novel method of generating libraries of polynucleotides encoding a framework region and at least one adjacent complementarity determining region (CDR) of an antibody of interest. These libraries are suitable for use in affinity maturation procedures in order to obtain maturated antibodies with improved characteristics compared to the parent antibody.