9 results about "Alpha globulin" patented technology

The present disclosure provides methods of determining whether a subject treated for hypertension should continue hypertension treatment. In exemplary embodiments, the method comprises measuring the level of at least two of the following in a urine sample obtained from the subject: (i) Alpha-1 microglobulin (aim); (ii) kidney injury molecule (KIM-1); and (iii) Chitinase-3-like protein (YKL-40); wherein the subject should continue the hypertension treatment, when the levels are decreased or unchanged, relative to a control level, and wherein the subject should discontinue or decrease the hypertension treatment, when the levels are increased, relative to a control level. Related methods, kits, assay systems, systems comprising machine readable instructions, computer-readable storage media, and methods implemented by a processor in a computer are furthermore provided herein.

The purpose of the present invention is to provide, as a platform technique that may serve as preparation for pandemics, a rapid antibody production technique in which a non-human animal having a human antibody gene is used. More specifically, the purpose of the present invention is to provide an immunization method with which it is possible to induce, in a short period of time, a high antigen-binding ability of an antibody or a high antibody titer of an antiserum, and a method for producing a human antibody / antiserum with which it is possible to rapidly produce a wide range of neutralizing antibodies.　(1) An immunization method for rapidly inducing a human monoclonal antibody having a high ability to bind to a desired antigen or a human polyclonal antibody having a high antibody titer, the method comprising a step for immunizing a non-human animal a plurality of times with a desired antigen or a nucleic acid encoding the antigen within 30 days from the first immunization, the non-human animal having a human antibody gene or locus, and the non-human animal being such that an endogenous gene or locus of the non-human animal corresponding to the human antibody gene or locus is disrupted or deleted, or mutated so as to result in a loss of expression or low expression. (2) A method for producing a human antibody against a desired antigen using a non-human animal, the method comprising: an immunization step for immunizing the non-human animal with the antigen or a nucleic acid encoding the antigen; a human immunoglobulin-positive B cell isolation step for isolating B cells that are human immunoglobulin-positive from a tissue of the immunized non-human animal; an antibody base sequence acquisition step for acquiring the base sequences of antibody light-chain mRNA-derived cDNA and antibody heavy-chain mRNA-derived cDNA prepared from the isolated B cells; and an antibody production step for producing an antibody on the basis of the acquired antibody base sequence, the non-h

The present application relates to the field of biotechnology, in particular to a preparation method of human type III collagen.The present application first attempts to use beta-lactoglobulin as a guide protein in the construction of a human type III collagen expression system, and relies on the characteristics of the expression system to produce high-yield beta-lactoglobulin, thereby achieving high-yield human type III collagen.The present application also provides a fusion protein composed of beta-lactoglobulin as a guide protein and human type III collagen, and a method for producing human type III collagen using the fusion protein.It has been verified that the present application successfully prepares human type III collagen with natural amino acid sequences and skin care effects, and the yield is more than 15g / L, thereby achieving high-yield human type III collagen with skin care effects under the premise of ensuring safety.

This invention discloses a β-lactoglobulin mutant, its preparation method, and its application, relating to the field of genetic engineering technology. The amino acid sequence of the β-lactoglobulin mutant is shown in SEQ ID NO.1. The preparation method is as follows: designing forward primers, reverse primers, forward mutation primers, and reverse mutation primers; using wild-type β-Lg plasmid as a template, obtaining a mutant DNA fragment using overlap extension PCR technology; ligating the mutant DNA fragment into an empty vector and transforming it into competent E. coli cells for culture and identification to obtain a recombinant plasmid; transforming the recombinant plasmid into competent E. coli cells, culturing, lysing, collecting the cell supernatant, purifying, and obtaining the β-lactoglobulin mutant. This invention, through structural modification of β-lactoglobulin, improves its binding to specific IgE antibodies, enhances the immunogenicity of β-lactoglobulin allergens, and improves the sensitivity and specificity of its allergen-specific IgE antibody detection results.

The present disclosure provides a method for degrading a target protein, comprising: contacting an IL-2Rβγ positive cell with a multispecific binding protein, wherein the multispecific binding protein comprises: a) a first cell surface binding moiety that specifically binds to a CD122 (IL-2Rβ) subunit and / or a CD132 (IL-2Rγ) subunit, on the surface of the IL-2Rβγ positive cell, wherein the first cell surface binding moiety comprises at least one immunoglobulin domain or a fragment thereof; and b) a second binding moiety that is operatively linked to the first cell surface binding moiety and that specifically binds to the target protein, wherein specific binding of the multispecific binding protein to the IL-2Rβ subunit and / or the IL-2Rγ subunit facilitates the internalization of the target protein into the IL-2Rβγ positive cell. The present disclosure also provides multispecific binding proteins and methods of using the multispecific binding proteins to treat disease.

This invention provides a method for preparing immobilized lipase using composite-modified protein amyloid protofibrils. The method first prepares β-lactoglobulin amyloid protofibrils by controlling pH and hydrothermal conditions, then polymerizes them into COF protofibrils via TFB and DB condensation. An immobilized carrier is obtained by composite modification with sulfopropyl betaine and pentamalloylmannose to adsorb and immobilize the lipase. In this invention, sulfopropyl betaine anchors to the carrier surface through electrostatic, hydrogen bonding, and hydrophobic interactions, forming a hydration film to prevent pore blockage and enhance the carrier's resilience. Pentamalloylmannose permeates the pores to form a stable interpenetrating structure, giving the carrier a high specific surface area and stability. Furthermore, it stabilizes the loaded lipase through multiple interactions, preventing conformational damage and detachment of the enzyme, while simultaneously creating a stable microenvironment for the lipase, inhibiting oxidation and denaturation inactivation. The immobilized lipase prepared by this invention exhibits high catalytic activity, excellent substrate mass transfer efficiency, and good reusability, and can efficiently catalyze oleic acid esterification reactions.

This disclosure provides compositions (e.g., pharmaceutical compositions) for delivering anti-HIV antibody agents, as well as related technologies (e.g., their components and / or methods). In addition, this disclosure provides polynucleotides encoding multiple immunoglobulin chains of anti-HIV antibody agents.

This invention discloses a recombinant β-lactoglobulin, its engineered Pichia pastoris strain, and anhydride modification method and applications, belonging to the field of biotechnology. This invention simultaneously knocks out the vacuolar protease PEP4 gene and the extracellular metalloproteinase YPS1 gene of Pichia pastoris, introduces an expression vector pPIC9K-BLG containing a codon-optimized β-lactoglobulin gene, and replaces the signal peptide with a secretion-enhancing signal peptide 0030 to obtain a recombinant plasmid. The recombinant plasmid is electroporated with competent Pichia pastoris cells, and then the folding system is transformed into a high-copy strain to obtain an engineered Pichia pastoris strain that secretes and expresses recombinant β-lactoglobulin, with the accession number CCTCC NO: M20251654. This invention also provides an anhydride modification method for the recombinant β-lactoglobulin, and the resulting modified protein has anti-HPV activity and can be used to prepare agents for the prevention and treatment of HPV infection.