7 results about "Immunoglobulin Variable Region" patented technology

It provides an improved immunoglobulin variable domain. [Solution] A VH domain comprising: (i) the amino acid residue at position 112 is either K or Q, and / or; (ii) the amino acid residue at position 89 is T, and / or; (iii) the amino acid residue at position 89 is L, the amino acid residue at position 110 is either K or Q, and (iv) in each of (i) to (iii), the amino acid at position 11 is preferably V, and the VH domain contains a C-terminal extension (X)n [wherein n is 1 to 10, preferably 1 to 5, for example 1, 2, 3, 4, or 5, and each X is a (preferably native) amino acid residue, independently selected from alanine (A), glycine (G), valine (V), leucine (L), or isoleucine (I), preferably independently selected from the group consisting of these].

Provided is a method for producing an antibody and the antibody produced by the method. The method includes immunizing an animal transplanted with stems cell with differentiation potential using an antigen and obtaining an antigen-specific antibody. The stem cells with differentiation potential are derived from a donor animal carrying one or more human immunoglobulin variable region gene segments. The method solves problems in the prior art including long transportation time and high costs associated with live transgenic animals used for producing human antibodies due to policy and quarantine requirements. When producing antibody against a target antigen having high homology with a transgenic animal, an immunosuppressed animal with a target antigen-encoding gene knockout is used as a transplantation recipient, which solves the problem in the prior art where transgenic animals have difficulty generating antibodies against homologous regions of the target antigen between humans and transgenic animals.

Disclosed in the present disclosure is genetically modified mice in which immunoglobulin loci are modified to insert gene segments of a human immunoglobulin variable region. The mice can be bred normally and produce human-mouse chimeric antibodies including a human variable region and a mouse constant region. The present disclosure also provides a method for preparing the genetically modified mice and use of the mice.

The present disclosure belongs to the field of immunology, and relates to a stable antibody preparation. The stable antibody preparation includes a therapeutically effective amount of an antibody molecule, a tonicity agent, a buffer agent, a filler and a surfactant, and the preparation has a pH of 4.5-5.5. The antibody molecule can specifically bind to both IL-5 and IL-4 Ra, and includes at least two immunoglobulin variable domains, which are divided into a first immunoglobulin variable domain capable of specifically binding to IL-4 Ra molecule and a second immunoglobulin variable domain n capable of specifically binding to IL-5. The antibody in the antibody preparation substantially retains the physical and chemical stability, and integrity thereof during storage.

The invention discloses a PEDV (Porcine Epidemic Diarrhea Virus) sIgA detection reagent, a PEDV sIgA detection method and application. The reagent comprises a first probe and a second probe. The first probe comprises a first binding element and a first fluorescent reporter molecule which are coupled with each other, and the first binding element comprises a PEDV S2 protein capable of being combined with a variable region of PEDV sIgA or a stabilizing mutant of a functional fragment of the PEDV S2 protein. The second probe comprises a second binding element and a second fluorescence reporter molecule which are coupled with each other, and the second binding element comprises an anti-porcine IgA antibody capable of being bound with a PEDV sIgA constant region. The first fluorescent reporter molecule and the second fluorescent reporter molecule form a fluorescence resonance energy transfer (FRET) pair. Compared with the prior art, the detection reagent provided by the invention can realize rapid, homogeneous and high-throughput quantitative detection of PEDV sIgA, and the detection sensitivity, the specificity and the signal-to-noise ratio of the detection reagent are greatly improved.

Genetically modified non-human animals are provided that express an immunoglobulin variable domain that comprises at least one histidine, wherein the at least one histidine is encoded by a substitution of a non-histidine codon in the germline of the animal with a histidine codon, or the insertion of a histidine codon in a germline immunoglobulin nucleic acid sequence. Immunoglobulin genes comprising histidines in one or more CDRs, in an N-terminal region, and / or in a loop 4 region are also provided. Immunoglobulin variable domains comprising one or more histidines (e.g., histidine clusters) substituted for non-antigen-binding non-histidine residues. Non-human animals that are progeny of animals comprising modified heavy chain variable loci (V, D, J segments), modified light chain variable loci (V, J segments), and rearranged germline light chain genes (VJ sequences) are also provided. Non-human animals that make immunoglobulin domains that bind antigens in a pH-sensitive manner are provided.

Improved immunoglobulin single variable domains that bind to serum albumin are provided. [Solution] An immunoglobulin single variable domain has specific CDR1, CDR2, and CDR3 (by Abm) and has seven or fewer, for example, five or fewer "amino acid differences" from a specific amino acid sequence, whereby (i) position 89 is T; or (ii) position 89 is L and position 11 is V; or (iii) position 89 is L and position 110 is K or Q; or (iv) position 89 is L and position 112 is K or Q; or (v) position 89 is L, position 11 is V, and position 110 is K or Q; or (vi) position 89 is L, position 11 is V, and position 112 is K or Q; or (vii) position 11 is V and position 110 is K or Q; or (vii) position 11 is V and position 110 is K or Q; or (vii) position 11 is V and position 112 is K or Q.