50results about "Serum immunoglobulins" patented technology

This invention proposes a method for preparing an antigen-specifically enriched, complete equine IgG(T) antitoxin formulation. The steps include: diluting hyperimmune equine plasma after multiple immunizations, adjusting the pH with a first acid solution, centrifuging to remove impurities, adding a second acid solution to cause non-immunoglobulin precipitation, obtaining a crude polyclonal equine IgG solution; constructing an IdeZ2 expression plasmid with an N-terminal His tag in a pET-28a(+) vector, and then transforming it into BL21(DE3) E. coli to obtain purified IdeZ2; adding purified IdeZ2 to the crude polyclonal equine IgG solution for cleavage reaction to obtain the IgG(T) component; polishing and purifying the IgG(T) component to obtain an intermediate IgG(T) formulation solution; contacting the intermediate IgG(T) formulation solution with the target toxin antigen for specific affinity binding to obtain an antigen-specifically enriched, complete equine IgG(T) antitoxin formulation. This equine IgG(T) antitoxin formulation, after targeted purification and background optimization, specifically alleviates the contradiction between persistence and safety in existing different molecular forms.

This invention provides a specific detection method for *Daphnia magna* in nearshore marine aquatic ecosystem assessment. Based on obtaining the species-specific antigenic protein and key immunogenic peptides of *Daphnia magna*, a highly specific monoclonal antibody was successfully prepared and purified, and a colloidal gold side-flow chromatography rapid detection test strip was prepared using this antibody. The amino acid sequence of the antigenic protein is SEQ ID NO:1 or SEQ ID NO:2. This invention, by screening for the *Daphnia magna* species-specific antigen and its corresponding monoclonal antibody, combined with paired antibodies prepared from the full-length protein, and using them to develop a colloidal gold rapid immunoassay product, achieves for the first time high-throughput, rapid on-site screening of this species, significantly improving the efficiency and accuracy of marine ecological monitoring, ship ballast organism inspection, and aquaculture environmental assessment.

The present application relates to the field of biomedical detection, specifically to a SPINK1 specific ELISA detection kit for aging detection, the kit contains polyclonal antibodies specific to SPINK1 protein and a color developing reaction system for assisting detection; the kit is also configured with E. coli derived recombinant SPINK1 protein with a purity of more than 99% as a standard for concentration calibration; the specific reagent list supplied in the kit includes horseradish peroxidase labeled antibody, blocking solution, washing buffer, the color developing reaction system is composed of 3,3',5,5'-tetramethylbenzidine solution, and the termination solution for interrupting the color developing chemical reaction is independently packaged. Through prokaryotic expression technology and targeted optimization of core induction conditions, combined with protein affinity chromatography purification process based on imidazole elution mechanism, the present application successfully realizes high-efficiency soluble expression of SPINK1 protein in E. coli vector and obtains recombinant protein with a purity of more than 99%.

Disclosed are monoclonal antibodies and antigen binding fragments thereof that specifically bind to Nipah virus (NiV) F or G protein. In several examples, the antibodies and antigen binding fragments are cross-reactive with other Henipavirus F or G proteins, such as Hendra virus (HeV) F or G proteins. Also disclosed is the use of these antibodies and antigen binding fragments for inhibiting a Henipavirus infection, such as a NiV and / or HeV infection. In addition, disclosed are methods for detecting Henipavirus, such as NiV or HeV in a biological sample, using the disclosed antibodies and antigen binding fragments.

This invention provides the application of gonococcal ferritin in the preparation of anti-gonococcal products, relating to the field of antibody technology. The application of gonococcal ferritin subunits in the preparation of antibodies against gonococcal ferritin inhibits gonococcal infection by intervening in the iron metabolism pathway of gonococci, without inducing classic drug resistance mutations. This overcomes the limitations of existing technologies that rely on antibiotics, achieving broad-spectrum inhibition of drug resistance lineages. It solves the technical problem in existing technologies where multidrug / pan-drug resistance of gonococci leads to complete failure of antibiotic treatment, and the lack of therapeutic targets targeting its core survival mechanisms.

The application belongs to the field of marine biotechnology, and specifically discloses a preparation method of a long oyster insulin-like peptide receptor (ILPR) polyclonal antibody and application thereof. The method is characterized by the following steps: specific antigen epitopes of the long oyster ILPR protein are screened through bioinformatics analysis, a pET32a-ILPR recombinant plasmid is constructed and induced to express in Escherichia coli; the purified recombinant protein is used as an immunogen to immunize New Zealand white rabbits, and rabbit antisera are collected after four times of booster immunization; specific polyclonal antibodies are purified by using antigen affinity chromatography technology, and can specifically recognize the ILPR protein in long oyster tissues. The antibody prepared by the application has high specificity and sensitivity, and provides an important biological tool for studying the insulin signal transduction pathway, growth regulation and energy metabolism mechanism of long oysters.

This invention relates to a high-titer prealbumin antibody purification method and its application, belonging to the field of biotechnology. The method utilizes Protein A affinity chromatography to capture total IgG from antiserum, followed by purification using an affinity chromatography column prepared by targeted conjugation of a specific sequence peptide. The antibody purified by this method achieves a titer of 1:256,000 in ELISA detection, with a half-maximal effective concentration (EC50). 50 The antibody concentration was 3.2 ng / mL, exhibiting extremely high affinity and reactivity. When used in a double-antibody sandwich chemiluminescent immunoassay, it achieved a detection limit of 0.08 µg / mL, a wide dynamic range (0.08–400 µg / mL), and a titer retention rate as high as 88% after accelerated storage at 37°C for 14 days, demonstrating significantly better stability than antibodies prepared by traditional methods. This invention provides a highly active and stable core antibody raw material for the preparation of high-performance immunodiagnostic reagents.

This invention relates to an anti-phospholipase A2 receptor polyclonal antibody, its preparation method, and its application. The preparation method includes immunizing animals with phospholipase A2 receptor protein as an antigen and collecting serum; separating and purifying the serum to obtain the anti-phospholipase A2 receptor polyclonal antibody; the amino acid sequence of the phospholipase A2 receptor protein includes the sequence shown in SEQ ID NO.1. This invention designs specific antigens for the preparation of polyclonal antibodies, enabling efficient preparation of polyclonal antibodies that specifically recognize the phospholipase A2 receptor. It has also been found that polyclonal antibodies prepared using eukaryotically expressed antigens, compared to those prepared using prokaryotically expressed or peptide-derived antigens, can more stably and efficiently construct an anti-PLA2R-associated membranous nephropathy (PLA2R MN) animal model.

The present disclosure provides an ophthalmic formulation comprising: one or more pharmaceutically acceptable excipients; a pharmaceutically active compound capable of reducing the amount or deleterious effects of autoantibodies on the ocular surface, such as IgG; in particular, the present disclosure provides an ophthalmic formulation wherein the pharmaceutically active compound is capable of treating a clinical condition selected from the group consisting of inflammatory, infectious and immunological ocular surface or intraocular diseases that can cause symptoms of ocular discomfort, keratitis, dry eye disease, formation of symblepharon, shortening of the anterior chamber depth, lid margin / conjunctival keratinization, subconjunctival fibrosis, retinal gliosis and glaucoma.

The present invention provides for a separation matrix for purification of antibodies or antibody fragments comprising at least one VH3 chain, said separation matrix comprising a VH3 binding ligand coupled to a porous support. Also provided is a method for isolation of antibodies or antibody fragments comprising at least one VH3 chain using the above-mentioned separation matrix. Additionally, there is provided a method for separation of bispecific antibodies or antibody fragments comprising one VH3 chain from variants of the antibody or antibody fragment comprising two VH3 chains or no VH3 chain, using the above-mentioned separation matrix.

Provided are methods of making a chimeric thymus in a subject, including implanting a donor thymic functional unit tissue graft, wherein the donor thymic functional unit tissue graft includes thymic epithelial cells (TEC) and dendritic cells. The chimeric thymus is useful to induce a dual immunologic tolerance to both donor tissue antigens and tissue antigens of the subject.

The application belongs to the technical field of biotechnology, and particularly discloses a synthetic peptide antigen of porcine circovirus type 2 Cap protein, a polyclonal antibody and application thereof. In order to solve the technical defects of low specificity and inaccurate detection of the amino acid sequence of the synthetic peptide antigen in the prior art, the application provides a synthetic peptide antigen of PCV2 Cap protein, a polyclonal antibody and application thereof. The application obtains an amino acid sequence of an antigen peptide by performing antigen peptide prediction on PCV2 Cap protein, and the applicant synthesizes the antigen peptide by using an Fmoc solid phase method, and immunizes a New Zealand white rabbit with the obtained antigen peptide to prepare a polyclonal antibody of Cap protein, the antibody can effectively react with a transiently expressed Cap protein and a Cap protein in PCV2b-infected PK15 cells, and provides a powerful tool for detection and biological function research of the PCV2 Cap protein.

The application provides an antigen epitope peptide and a paralichthys olivaceus mucin Muc13 specific antibody prepared by the antigen epitope peptide, determines a B cell epitope from the paralichthys olivaceus Muc13 protein through antigen epitope screening, and the sequence is PGTTEEPDPTAGSPP. After the epitope is coupled with a KLH carrier protein, the epitope is used for immunizing New Zealand white rabbits, and a rabbit-derived anti-paralichthys olivaceus Muc13 specific antibody is successfully obtained. The antibody can specifically recognize the Muc13 protein in paralichthys olivaceus mucosa tissue and Muc13 positive mucous cells, and provides a key detection means for in-depth exploration of the function mechanism of mucous cells in the fish mucosa immune response process.

A monolithic implantable device for delivery of an antibody is provided. The implantable device comprises a polymer matrix within which is dispersed a pharmaceutical formulation that includes one or more therapeutic agents and optionally, one or more excipients. The therapeutic agents contain an antibody and the polymer matrix contains a hydrophobic polymer. Within a time period of 35 days, the device exhibits a cumulative weight-based release ratio of the antibody of from about 20% to about 60%.

The present invention provides an improved manufacturing process for producing a bispecific antibody product comprising at least two binding domains. The process comprises at least a process comprising a step of refolding a construct, wherein one or more domains comprise disulfide bonds, and wherein the construct is contacted with a refolding buffer to refold the construct into its native form, the buffer comprising (i) an oxidizing and / or reducing agent at a concentration of at least 0.1 mM, and (ii) a chaotropic agent at a concentration > 1 M, and wherein the pH of the refolding buffer corresponds to + / - 4.5 of the pi value of the first domain or + / - 4.0 of the pi value of the entire construct.

This invention relates to the field of bioengineering technology, specifically to a method for preparing neutrophil gelatinase-associated lipid transport protein and its antibody. Specifically, using pET23a(+) as the expression vector, the NGAL gene with six His tags fused to its N-terminus under promoter control is introduced into *E. coli* for induced expression. After purification using a Ni Focurose 6FF column and a molecular sieve column, tag-free NGAL protein with a purity ≥95% is obtained. Subsequently, the NGAL protein is used to repeatedly immunize Japanese rabbits, and serum is collected after each immunization. Qualified serum is screened using a two-dimensional agar diffusion assay, and then purified using the aforementioned antigen to prepare an antigen affinity purification column, yielding a highly active NGAL polyclonal antibody. The high-purity recombinant NGAL of this invention not only possesses activity but is also low-cost, not limited by raw materials, and can be mass-produced, possessing potential and wide-ranging application value in clinical and in vitro diagnostics.

The application provides an antigen epitope polypeptide and a paralichthys ovatus mucin Muc5b specific antibody prepared by the antigen epitope polypeptide, a B cell antigen epitope of the paralichthys ovatus Muc5b protein is screened, the amino acid sequence of the B cell antigen epitope is shown as NDKQRSKQCEDYQVV, a New Zealand white rabbit is immunized after the antigen epitope is coupled with a KLH carrier protein, and a rabbit anti-paralichthys ovatus Muc5b specific antibody is prepared. The antibody can specifically recognize the Muc5b protein in paralichthys ovatus mucosa tissue and positive mucous cells, and provides a key detection tool for in-depth exploration of the function mechanism of mucous cells in the paralichthys ovatus mucosa immune response process.

The present invention provides methods of reducing yellow color in an Fc-containing molecule sample, such as in an elution pool. Said methods are useful in manufacturing of therapeutic antibodies.

The application relates to the technical field of biological medicine, and particularly discloses a monoclonal antibody combined with human CD4 and a preparation method and application thereof. The antibody is obtained by combining single B cell sorting, gene cloning and mammalian cell expression technology after rabbit immunization of a CD4 polypeptide antigen. The antibody has high affinity and good specificity, and can effectively recognize CD4 positive T cells in human peripheral blood. The antibody is verified by ELISA and flow cytometry, and has high titer, low background and a signal-to-noise ratio superior to that of existing mouse-derived antibodies. Further, the amino acid sequences of the light chain and the heavy chain variable region of the antibody are obtained, so that controllability and repeatability of antibody expression are realized. The antibody can be widely applied to scenes such as immunodetection, HIV auxiliary diagnosis, T cell subgroup research and antibody engineering development, and has important scientific research and industrial values.

This invention provides a human anti-thymocyte globulin (ATG) product, as well as a method for producing and using the same. [Solution] This disclosure provides polyclonal immunoglobulins derived from ungulates having a population of fully human or substantially human immunoglobulins. The population of fully human or substantially human immunoglobulins specifically binds to human thymocytes, T cells, B cells, and / or monocytes. Such compositions can be produced by immunizing transgenic animals having the human Ig locus with human thymocytes. This method produces polyclonal immunoglobulins with yield, purity, and antigen specificity that enable the use of this product in medical applications.

The application provides a pig getah virus positive serum and a preparation method and application, and belongs to the technical field of animal virology. The application provides a preparation method of a pig getah virus positive serum, wherein a CDCD pig is used as a host, neutralizing antibody titer obtained through multiple immunization of high-concentration antigen is greater than or equal to 1:512; the serum does not have cytotoxicity affecting cell culture; the CDCD pig is a pig free from maternal antibody interference, which is obtained through caesarean section, isolated feeding and artificial feeding; the positive serum does not detect pig pseudorabies virus, swine fever virus, porcine circovirus type 2, pig foot-and-mouth disease virus, bovine viral diarrhea virus, porcine infectious gastroenteritis virus, porcine epidemic diarrhea virus, porcine rotavirus, porcine parvovirus, porcine Japanese encephalitis virus antibody, and has the characteristics of high titer and no cytotoxicity.

The present invention generally pertains to methods of cultivating cells and producing a recombinant protein of interest, such as dupilumab. In particular, the present invention pertains to the use of a fixed seed schedule to determine the expansion time of seed train unit operations for improved cell growth and protein titer. The protein produced by the fixed seed schedule, such as dupilumab, can be later subjected to lipase activity reduction methods.

The present application belongs to the technical field of blood product preparation, and particularly relates to a preparation method of intravenous human immunoglobulin, comprising the following steps which are sequentially performed: Cohn FIII supernatant is pretreated to obtain a sample I to be loaded; the sample I to be loaded is subjected to first anion exchange chromatography to obtain a first chromatography product; the first chromatography product is pretreated to obtain a sample II to be loaded; the sample II to be loaded is subjected to second anion exchange chromatography to obtain a second chromatography product; the second chromatography product is pretreated to obtain a sample III to be loaded; the sample III to be loaded is subjected to heparin affinity chromatography to obtain a third chromatography product; and the third chromatography product is configured into human immunoglobulin finished product. The technical scheme can solve the technical problems of the existing preparation method of intravenous human immunoglobulin, such as introduction of new materials, poor effect of impurity protein precipitation, high content of anti-A and anti-B, and the like, and has an ideal application prospect.

The invention provides a method of manufacturing an IgM-containing composition depleted of anti-A and / or anti-B immunoglobulin from human plasma. An IgM-containing composition derived from human plasma having 5% or more IgM of the total immunoglobulin is contacted with a macroporous chromatography resin coupled with a ligand comprising GalNAcα1-3(Fucα1-2)Galβ1-4Glc- and / or Galα1-3(Fucα1-2)Galβ1-4Glc-. The flow-through is recovered.

Provided is a product production method which includes: a step of culturing a cell which produces a product and is contained in a cell suspension accommodated in a culture vessel; a separation treatment step of extracting the cell suspension from the culture vessel and separating the cell suspension by a tangential filtration method using a separation membrane; a step of returning a return liquid to the culture vessel; a step of supplying a fresh medium into the culture vessel; and a step of collecting the product, and in which with respect to a live cell concentration Nc, a pore diameter Dp of the separation membrane, a filtration area S of the separation membrane, and a volume Vf of a primary side flow path of the separation membrane, a number density Nd of fine particles having a particle size of 8 Dp to 30 Dp other than live cells in the cell suspension satisfies Nc ≤ Nd ≤ S / (32 × π × Vf × Dp2).