The application is to antibodies which have been labelled with polyenzymes (multiple enzymes), specifically polyperoxidases, for use in direct immunohistochemical assays of tissues. The antibodies used diagnostically may also be antibodies which are used therapeutically.

Disclosed herein are monoclonal antibodies targeting specific tau epitopes, particularly, microtubule binding domain region 2 or region 4. Also disclosed herein are antibodies or antigen binding fragments thereof that specifically recognize a tau epitope consisting of the amino acid sequence of SEQ ID NO: 9 or 11. Also disclosed herein are methods of detecting tau protein in a subject, comprising performing an assay using the antibodies or antigen binding fragments thereof on the subject or on a biological sample obtained from the subject. Assay kits containing the disclosed antibodies are also provided. Further, methods of treating or preventing a tauopathy in a subject by administering to the subject tau antibodies or antigen-binding fragments thereof are provided.

Disclosed herein are monoclonal antibodies targeting specific tau epitopes, particularly, microtubule binding domain region 2 or region 4. Also disclosed herein are antibodies or antigen binding fragments thereof that specifically recognize a tau epitope consisting of the amino acid sequence of SEQ ID NO: 9 or 11. Also disclosed herein are methods of detecting tau protein in a subject, comprising performing an assay using the antibodies or antigen binding fragments thereof on the subject or on a biological sample obtained from the subject. Assay kits containing the disclosed antibodies are also provided. Further, methods of treating or preventing a tauopathy in a subject by administering to the subject tau antibodies or antigen-binding fragments thereof are provided.

The present invention relates to a fusion protein comprising: —a N-terminal domain which comprises an antibody which is a variable domain of a camelid heavy-chain antibody (VHH) or a single chain variable fragment (scFV) and which is directed against an immunoglobulin and —a C-terminal domain which comprises a polypeptide with a luciferase activity: —having the amino acid sequence SEQ ID NO: 1 or —having at least 80% amino acid sequence identity to the amino acid sequence SEQ ID NO: 1.

The present invention relates to a fusion protein comprising: —a N-terminal domain which comprises an antibody which is a variable domain of a camelid heavy-chain antibody (VHH) or a single chain variable fragment (scFV) and which is directed against an immunoglobulin and —a C-terminal domain which comprises a polypeptide with a luciferase activity: —having the amino acid sequence SEQ ID NO: 1 or —having at least 80% amino acid sequence identity to the amino acid sequence SEQ ID NO: 1.

The present disclosure relates to a dissociation reagent for tumor tissues. The dissociation reagent does not contain collagenase or trypsin but further contains hyaluronidase or a mixture of hyaluronidase and DNase I. The present disclosure also relates to use of the dissociation reagent in dispersing tumor tissues and detecting expression level of molecular markers on cell surface by flow cytometry. The dissociation reagent of the present disclosure does not cause degradation of molecular markers on cell surface such as CD8, PD-1, Tim-3, Lag-3 and the like, thus does not affect downstream assays.

The present disclosure relates to a dissociation reagent for tumor tissues. The dissociation reagent does not contain collagenase or trypsin but further contains hyaluronidase or a mixture of hyaluronidase and DNase I. The present disclosure also relates to use of the dissociation reagent in dispersing tumor tissues and detecting expression level of molecular markers on cell surface by flow cytometry. The dissociation reagent of the present disclosure does not cause degradation of molecular markers on cell surface such as CD8, PD-1, Tim-3, Lag-3 and the like, thus does not affect downstream assays.

Compositions, methods, and kits are disclosed directed at haptens, immunogens and immunoassays for oxycodone and metabolites thereof. The compounds are exemplified by compounds of the Formula I. The method comprises providing in combination in a medium (i) a sample suspected of containing oxycodone and/or oxycodone metabolites, a compound of the Formula I wherein R.sup.4 or R.sup.5 is a label, and an antibody for oxycodone or a metabolite thereof. The medium is examined for the presence of a complex comprising the labeled compound of Formula I where the presence of such as complex indicates the presence of oxycodone or oxycodone metabolite in the sample.

Compositions, methods, and kits are disclosed directed at haptens, immunogens and immunoassays for oxycodone and metabolites thereof. The compounds are exemplified by compounds of the Formula I. The method comprises providing in combination in a medium (i) a sample suspected of containing oxycodone and/or oxycodone metabolites, a compound of the Formula I wherein R.sup.4 or R.sup.5 is a label, and an antibody for oxycodone or a metabolite thereof. The medium is examined for the presence of a complex comprising the labeled compound of Formula I where the presence of such as complex indicates the presence of oxycodone or oxycodone metabolite in the sample.

The disclosure belongs to the field of biotechnology, and in particular to a blocking ELISA kit for detecting an antibody to swine acute diarrhea syndrome coronavirus (SADS-CoV) N protein. The kit includes an enzyme plate coated with SADS-CoV N protein, an HRP-labeled mouse anti-SADS-CoV N protein monoclonal antibody (mAb), a positive serum control, and a negative serum control. The kit may detect positive sera diluted at 1:512, with no cross-reaction with positive sera against porcine epidemic diarrhea virus (PEDV), transmissible gasteroenteritis virus (TGEV) and porcine deltacoronavinis (PDCoV) etc., and the intrabatch and interbatch coefficient of variation is less than 10%. The comparison result with the indirect immunofluorescence test shows that the concordance rate of the blocking ELISA kit of the present disclosure is 99.6%, the Kappa value is 0.91, and the blocking ELISA method established by the present disclosure is highly consistent with IFA.