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: The present invention relates to a method for assessing myocardial infarction comprising the steps of determining the amount of a first biomarker in a sample of a subject, said first biomarker being cMyBPC, determining the amount of a second biomarker in a sample of the subject, wherein said second biomarker is selected from the group consisting of: a BMP10-type peptide (Bone Morphogenic Protein 10-type peptide), FGF23 (Fibroblast growth factor 23), a BNP-type peptide (Brain natriuretic peptide type peptide), GDF-15 (Growth differentiation factor 15), ANG2 (Angiopoietin 2), CRP (C-reactive protein), ESM1 (endothelial cell specific molecule 1), or a lipid biomarker, such as Cholesterol, LDL (Low Density Lipoprotein) or APOAT (Apolipoprotein A-1) comparing the amounts of the biomarkers to references for said biomarkers and/or calculating a score for assessing myocardial infarction based on the amounts of the biomarkers, and assessing said subject based on the comparison and/or the calculation.

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 discloed 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 disclosure relates to specific binding agents binding to different PIVKA-II forms as compared to antibodies known so far in the art. The present disclosure also relates to methods of using the specific binding agents to detect the presence of PIVKA-II.

Abstract: The present invention relates to monoclonal antibodies and antigen binding fragments that specifically bind to ?-1,6-core-fucosylated alpha-fetoprotein (AFP), which is the core component of AFP-L3. Thus, the antibodies and antigen binding fragments provided herein may also be referred to as AFP-L3 antibodies. Also provided are polynucleotides encoding the antibodies or antigen binding fragments of the invention, host cells expressing the antibodies and antigen binding fragments of the invention, methods for producing the antibodies and antigen binding fragments of the invention, and uses of the antibodies and antigen binding fragments of the invention. Also provided herein is a pretreatment agent facilitating the binding of the antibodies and antigen binding fragments of the invention to ?-1,6-core-fucosylated AFP. The present invention further relates to kits comprising the antibodies and antigen binding fragments of the invention and optionally the pretreatment agent of the invention.

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

Abstract: The present invention provides a novel monoclonal antibody specifically binding to L-Thyroxine (T4) and compositions and kits comprising such antibodies. Furthermore, provided are polynucleotides encoding such monoclonal antibodies, host cells expressing said antibodies, methods of producing such antibodies and diagnostic methods using such monoclonal antibodies. The monoclonal antibody of the invention comprises a heavy chain variable domain (VH) comprising V or A in position 33; Y in position 50; W in position 52; I in position 98, G, A or V in position 99; Y in position 100; and I in position 100b; and a light chain variable domain (VL) comprising amino acids H or Y in position 28; N or K in position 29; W in position 32; G or A in position 91; Y, W or F in position 92; S or T in position 93; Y or F in position 95b; N, S, T or Q in position 95c; and H in position 96, wherein the positions of the amino acids in the VH and the VL are indicated according to the Kabat numbering scheme, respectively.

Abstract: The present invention relates to a method for determining the total amount and/or concentration of an analyte in the presence of a binding molecule as well as kits, compositions and uses relating thereto.

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 discloed 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 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 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 present invention relates to a method for assessing atrial fibrillation in a subject, said method comprising the steps of determining the amount of BMP10 in a sample from the subject, and comparing the amount of BMP10 to a reference amount, whereby atrial fibrillation is to be assessed. Moreover, the present invention relates to a method for diagnosing heart failure based on the determination of BMP 10 in a sample from a subject. Further, the present invention relates to a method for predicting the risk of a subject of hospitalization due to heart failure based on the determination of a BMP10-type peptide in a sample from a subject. The present invention further pertains to antibodies which bind to one or more BMP10-type peptides such as NT-proBMP10.

Abstract: The present disclosure relates to specific binding agents binding to different PIVKA-II forms as compared to antibodies known so far in the art. The present disclosure also relates to methods of using the specific binding agents to detect the presence of PIVKA-II.

Abstract: The present disclosure relates to specific binding agents binding to different PIVKA-II forms as compared to antibodies known so far in the art. The present disclosure also relates to methods of using the specific binding agents to detect the presence of PIVKA-II.

Abstract: The present invention concerns an in vitro method for measurement of 25-hydroxyvitamin D, wherein the potentially interfering compound 24,25-dihydroxyvitamin D3 is blocked by a binding agent specifically binding to 24,25-dihydroxyvitamin D3 and not binding to 25-hydroxyvitamin D.

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.