7 results about "Elisa assay" patented technology

This invention discloses an antibody that specifically recognizes Toxoplasma gondii surface antigens and its applications. The invention utilizes hybridoma technology to establish a hybridoma cell line by fusing Balb / C mouse spleen cells with SP2 / 0 cells. Monoclonal antibodies were prepared from these cells using in vitro culture and in vivo ascites induction methods, yielding the monoclonal antibody SH12-S7. This invention provides clinical and research institutions with an antibody that specifically recognizes Toxoplasma gondii surface antigens. It can be used for ELISA assays to detect clinical samples, for immunohistochemical assays to diagnose pathological specimens, and provides a convenient research tool for toxoplasmosis research departments. It has broad application value in the diagnosis and detection of definitive host infections and provides technical support for epidemiological investigations and evaluation of control effects of Toxoplasma gondii.

This invention utilizes a machine learning model to analyze the crystal structure of the PEDV Nsp5 protein. Through virtual peptide screening technology, a peptide sequence with potential affinity for the target protein, YKKLHK(162860), was artificially synthesized in a solid phase. Using artificially expressed PEDV Nsp5 protein, the peptide was screened using an ELISA assay. The affinity constant between the peptide and the target protein was determined using surface plasmon resonance (SPR) assays. The cytotoxicity of peptide 162860 was tested using a CCK-8 assay kit. Its inhibitory activity against viral infection was tested using quantitative real-time PCR and indirect immunofluorescence assays. The results showed that the 162860 sequence significantly inhibited PEDV infection.

Immunoglobulin light Chain "AL" amyloidosis is the most common form of systemic amyloidosis, accounting for approximately 70% of the diagnosed cases in developed countries. As there are treatments available, e.g., based on antibody C11-1F4, and in development for AL amyloidosis, there is a need in for more accurate methods for quality control of c11-1F4 antibodies or antigen-binding fragment thereof. Immunoassays, methods, and kits for testing the specificity of 11-1F4 antibodies are provided. The immunoassays, methods, and kits are more than 10 times more sensitive than the ELISA protocol that is routinely used for evaluation of c11-1F4 binding to LEN peptide.

The invention provides an ELISA (Enzyme-Linked Immunosorbent Assay) detection method of an anti-CD3 antibody. The detection method provided by the invention can accurately detect the anti-CD3 antibody impurity in the cell preparation product, avoids the medication risk, and is beneficial to improving the safety of the cell preparation product.

Methods, systems, and kits are provided for standardizing lectin reagents and measuring galactose-deficient IgA1 (Gd-IgA1) as a biomarker for IgA nephropathy. The invention includes a method for standardizing test batches of lectin reagents by comparing binding activity to reference batches using calibration standards, with acceptance criteria based on analytical recovery within thresholds. A stabilized reference standard comprising enzymatically modified or recombinantly produced Gd-IgA1 exhibits parallelism with natural serum samples and enables reproducible quantification across runs. The invention further provides a lectin-based ELISA assay kit for quantitative measurement of Gd-IgA1 in biological samples, particularly serum, using standardized N-acetylgalactosamine (GalNAc)-specific lectins such as biotinylated Helix pomatia agglutinin (HPA) or Helix aspersa agglutinin (HAA). Clinical applications include diagnosing IgA nephropathy, risk stratification, monitoring disease progression, assessing treatment response, and screening kidney transplant donors. The standardization methodology is broadly applicable to validating binding reagents for detecting diverse biomarkers, peptides, and proteins in diagnostic assays.

The application belongs to the technical field of biotechnology and relates to the field of veterinary diagnosis, and particularly discloses a liquid-phase blocking ELISA kit for porcine Senecavirus neutralizing antibody, which contains porcine Senecavirus single-domain antibody and matched detection reagents, and the porcine Senecavirus single-domain antibody can also be an antigen-binding fragment of the single-domain antibody, the single-domain antibody is selected from one or more groups in 52 groups, the heavy chain variable region of each group of single-domain antibodies or antigen-binding fragments contains CDR-1, CDR-2 and CDR-3, the amino acid sequences of the heavy chain variable region CDR-1 (VH-CDR-1) of the 52 groups of single-domain antibodies or antigen-binding fragments are respectively shown in SEQ ID NO. 1-SEQ ID NO. 52, the amino acid sequences of the heavy chain variable region CDR-2 (VH-CDR-2) are respectively shown in SEQ ID NO. 53-SEQ ID NO. 104, and the amino acid sequences of the heavy chain variable region CDR-3 (VH-CDR-3) are respectively shown in SEQ ID NO. 105-SEQ ID NO. 156. The kit can quickly detect the SVA neutralizing antibody level in serum, has high sensitivity, good specificity and stable results, and can be better applied to SVA vaccine efficacy evaluation.

Methods, systems, and kits are provided for standardizing lectin reagents and measuring galactose- deficient IgAl (Gd-IgAl) as a biomarker for IgA nephropathy. The invention includes a method for standardizing test batches of lectin reagents by comparing binding activity to reference batches using calibration standards, with acceptance criteria based on analytical recovery within thresholds. A stabilized reference standard comprising enzymatically modified or recombinantly produced Gd-IgAl exhibits parallelism with natural serum samples and enables reproducible quantification across runs. The invention further provides a lectin-based ELISA assay kit for quantitative measurement of Gd-IgAl in biological samples, particularly serum, using standardized N-acetylgalactosamine (GalNAc)-specific lectins such as biotinylated Helix pomatia agglutinin (HP A) or Helix aspersa agglutinin (HAA). Clinical applications include diagnosing IgA nephropathy, risk stratification, monitoring disease progression, assessing treatment response, and screening kidney transplant donors. The standardization methodology is broadly applicable to validating binding reagents for detecting diverse biomarkers, peptides, and proteins in diagnostic assays.