Abstract: The present disclosure is directed at an antibody conjugate having an antibody and a tag, wherein one or more element(s) present in the antibody exhibit an isotope ratio which differs from the naturally occurring isotope ratio of the one or more element(s), wherein the amount of the isotope which is less-common in nature, is increased to at least 4% of the atoms of the respective element in the antibody, as well as uses thereof.

Abstract: The present disclosure is directed at an antibody conjugate having an antibody and a tag, wherein one or more element(s) present in the antibody exhibit an isotope ratio which differs from the naturally occurring isotope ratio of the one or more element(s), wherein the amount of the isotope which is less-common in nature, is increased to at least 4% of the atoms of the respective element in the antibody, as well as uses thereof.

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: Herein is reported a fusion polypeptide according to formula I NH2—S2—X1—S1—COOH??(formula I) wherein X1 comprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide, S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and — denotes a peptide bond, wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein X1 is inserted in place of the insert-in-flap-domain of the second polypeptide.

Abstract: Herein is reported a fusion polypeptide according to formula I NH2—S2—X1—S1—COOH??(formula I) wherein X1 comprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide, S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and — denotes a peptide bond, wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein X1 is inserted in place of the insert-in-flap-domain of the second polypeptide.

Abstract: Isolated antibodies that specifically bind to an epitope comprised in the stretch of amino acids ranging from amino acid 76 to amino acid 84 of human insulin-like growth factor-1 precursor (SEQ ID NO:1). Use of the novel antibodies for the sensitive and specific detection of insulin-like growth factor-1, in some embodiments while in the presence of high excess concentration of insulin-like growth factor-2, for example in a bodily fluid sample.

Abstract: The invention concerns a fusion polypeptide including several molecules of folding helper polypeptides, including one multimerization domain, in particular Skp, and at least one molecule of SlyD or SlpA, wherein no further target polypeptide sequences are fused to the fusion polypeptide. The invention further concerns an immunoassay and the use of the fusion polypeptide in an immunoassay for reduction of interferences or minimizing false positive results or for stabilizing proteinaceous assay reagents. Further the invention concerns a reagent kit for use in an immunoassay comprising the fusion polypeptide.

Abstract: Herein is reported a fusion polypeptide according to formula I NH2—S2—X1—S1—COOH??(formula I) wherein X1 comprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide, S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and — denotes a peptide bond, wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein X1 is inserted in place of the insert-in-flap-domain of the second polypeptide.

Abstract: Novel glucose oxidase (GOx) variants are disclosed that have the substitutions of T30V and I94V set forth in SEQ ID NO:1, and additionally at least one further amino acid substitution in the enzyme sequence in any of the positions S53; A137; A173; A332; F414 and V560. The GOx variants herein exhibit specificity for glucose and significantly reduced oxygen consumption rates and/or increased enzyme activity for electron mediators other than oxygen. Also provided are assay devices incorporating at least one of the GOx variants herein for improved blood glucose measurements.

Abstract: The invention concerns a fusion polypeptide comprising several molecules of folding helper polypeptides, comprising one multimerization domain, in particular Skp, and at least one molecule of SlyD or SlpA, wherein no further target polypeptide sequences are fused to said fusion polypeptide. The invention further concerns an immunoassay and the use of said fusion polypeptide in an immunoassay for reduction of interferences or minimizing false positive results or for stabilizing proteinaceous assay reagents. Further the invention concerns a reagent kit for use in an immunoassay comprising said fusion polypeptide.

Abstract: Compositions, devices, kits and methods are disclosed for assaying glucose with a glycosylated, modified flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH), variant thereof or an active fragment thereof, where at least one asparagine residue at positions N2, N168 and N346 of mature, wild-type A. oryzae FAD-GDH according to SEQ ID NO:2 is substituted by one or more amino acids not suitable for glycosylation, thereby eliminating or inactivating, respectively, a potential glycosylation site at this position.

Abstract: Herein is reported a fusion polypeptide according to formula I NH2—S2—X1—S1—COOH??(formula I) wherein X1 comprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide, S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and — denotes a peptide bond, wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein X1 is inserted in place of the insert-in-flap-domain of the second polypeptide.

Abstract: Isolated antibodies that specifically bind to an epitope comprised in the stretch of amino acids ranging from amino acid 76 to amino acid 84 of human insulin-like growth factor-1 precursor (SEQ ID NO:1). Use of the novel antibodies for the sensitive and specific detection of insulin-like growth factor-1, in some embodiments while in the presence of high excess concentration of insulin-like growth factor-2, for example in a bodily fluid sample.

Abstract: Isolated antibodies that specifically bind to an epitope comprised in the stretch of amino acids ranging from amino acid 76 to amino acid 84 of human insulin-like growth factor-1 precursor (SEQ ID NO:1). Use of the novel antibodies for the sensitive and specific detection of insulin-like growth factor-1, in some embodiments while in the presence of high excess concentration of insulin-like growth factor-2, for example in a bodily fluid sample.

Abstract: Herein is reported a fusion polypeptide according to formula (I): NH2—S2—X1—S1—COOH, wherein X1 comprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide, S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and denotes a peptide bond, wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein X1 is inserted in place of the insert-in-flap-domain of the second polypeptide.

Abstract: Novel glucose oxidase variants are disclosed that have besides the two substitutions T30V and I94V according to SEQ ID NO:1, additionally at least one further amino acid substitution in the polypeptide sequence in any of the positions S53; A137; A173; A332; F414 and V560. The glucose oxidase variants herein exhibit specificity for glucose and significantly reduced oxygen consumption rates and/or increased enzyme activity for electron mediators other than oxygen. Also provided are assay devices incorporating at least one of the GOx variants herein for improved blood glucose measurements.

Abstract: Compositions, devices, kits and methods are disclosed for assaying glucose with a glycosylated, modified flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH), variant thereof or an active fragment thereof, where at least one asparagine residue at positions N2, N168 and N346 of mature, wild-type A. oryzae FAD-GDH according to SEQ ID NO:2 is substituted by one or more amino acids not suitable for glycosylation, thereby eliminating or inactivating, respectively, a potential glycosylation site at this position.

Abstract: Herein is reported a fusion polypeptide according to formula (I): NH2—S2—X1—S1—COOH, wherein X1 comprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide, S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and denotes a peptide bond, wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein X1 is inserted in place of the insert-in-flap-domain of the second polypeptide.

Abstract: The disclosure concerns the enzymatic synthesis of stable analogues of nicotinamide adenine dinucleotide NAD/NADH and nicotinamide adenine dinucleotide phosphate NADP/NADPH, the so-called “carba-NADs”, i.e. analogues of NAD/NADH or NADP/NADPH, respectively, comprising a carbacyclic sugar instead of ribose.

Abstract: Isolated antibodies that specifically bind to an epitope comprised in the stretch of amino acids ranging from amino acid 76 to amino acid 84 of human insulin-like growth factor-1 precursor (SEQ ID NO:1). Use of the novel antibodies for the sensitive and specific detection of insulin-like growth factor-1, in some embodiments while in the presence of high excess concentration of insulin-like growth factor-2, for example in a bodily fluid sample.