127 results about "Immunoglobulin class" patented technology

The present invention relates to a separation matrix comprised of porous particles to which antibody-binding protein ligands have been immobilised, wherein the ligand density is in the range of 5.0-10 mg/ml; the gel phase distribution coefficient of the particles expressed as K_av for a dextran of size 110 kDa is above 0.65 and the median particle diameter is between 65-84 μm. The carbohydrate material is preferably highly cross-linked agarose.

The present invention relates to humanized immunoglobulins having binding specificity for α4β7 integrin, comprising an antigen binding region of nonhuman origin (e.g., rodent) and at least a portion of an immunoglobulin of human origin (e.g., a human framework region, a human constant region). In one embodiment, the humanized immunoglobulin can compete with murine Act-1 for binding to human α4β7 integrin. In a preferred embodiment, the antigen binding region of the humanized immunoglobulin comprises each of the complementarity determining regions of the light and heavy chains of the murine Act-1 antibody.

The present invention relates to antibodies including human antibodies and antigen-binding portions thereof that specifically bind to c-Met, preferably human c-Met, and that function to inhibit c-Met. The invention also relates to human anti-c-Met antibodies and antigen-binding portions thereof. The invention also relates to antibodies that are chimeric, bispecific, derivatized, single chain antibodies or portions of fusion proteins. The invention also relates to isolated heavy and light chain immunoglobulins derived from human anti-c-Met antibodies and nucleic acid molecules encoding such immunoglobulins. The present invention also relates to methods of making human anti-c-Met antibodies, compositions comprising these antibodies and methods of using the antibodies and compositions for diagnosis and treatment. The invention also provides gene therapy methods using nucleic acid molecules encoding the heavy and/or light immunoglobulin molecules that comprise the human anti-c-Met antibodies. The invention also relates to transgenic animals or plants comprising nucleic acid molecules of the present invention.

The present invention relates to immunoglobulin glycoprotein compositions having predominant N-glycan structures on an immunoglobulin glycoprotein which confer a specific effector function. Additionally, the present invention relates to pharmaceutical compositions comprising an antibody having a particular enriched N-glycan structure, wherein said N-glycan structure is GlcNAcMan₅GlcNAc₂.

The present invention relates to chromatography matrices including ligands based on one or more domains of immunoglobulin-binding proteins such as, Staphylococcus aureus Protein A (SpA), as well as methods of using the same.

The invention relates to the generation of immunoglobulin libraries and the identification and production of immunoglobulins having a specific functionality of interest.

The present invention relates to antigen binding proteins to human IL-23, pharmaceutical formulations containing them and to the use of such antigen binding proteins in the treatment and/or prophylaxis of inflammatory diseases such as Rheumatoid Arthritis (RA).

Antigen-binding proteins specific for HLA-A2-restricted Wilms tumor 1 peptide are disclosed. The antigen-binding proteins encompass antibodies in a variety of forms, including full-length antibodies, substantially intact antibodies, Fab fragments, F(ab′)2 fragments, and single chain Fv (scFv) fragments, as well as chimeric antigen receptors. Fusion proteins, such as scFv fusions with immunoglobulin or T-cell receptor domains, incorporating the antigen-binding proteins are provided. Methods of using the antigen-binding proteins in the treatment of hyperproliferative diseases such as cancer are also disclosed.

Novel humanized immunoglobulins and active fragments thereof which are specifically reactive to Fas ligand are provided, and a site on Fas ligand which is important to inhibit apoptosis induced by the Fas-Fas ligand interaction against Fas-expressing cells is demonstrated. The novel humanized immunoglobulins and active fragments thereof which are specifically reactive to Fas ligand are prepared from hybridomas which produce monoclonal antibodies specifically reactive to Fas ligand, via recombinant DNA techniques. The humanized immunoglobulins can inhibit the physiological reactions between Fas ligand and Fas such as apoptosis. Further, identification of the site which is on Fas ligand and responsible for apoptosis induction allows creation of recombinant proteins or peptides which are specifically reactive to the amino acids within the site so as to inhibit apoptosis, and to find new therapeutic or diagnostic agents.

Methods and compositions for the screening and isolation of ligand-binding polypeptides, such as antibodies. In some aspects, methods of the invention enable the isolation of intact soluble antibodies comprising a constant domain. Screening methods that employ genetic packages such as bacteria and bacteriophages enable high through-put identification of ligand binding molecules.

Disclosed herein is a hinge antibody capable of being selectively activated in a target cell or tissue to treat a condition therein. The hinge antibody includes a functional antibody, two inhibitory domains and four cleavable linkers. The functional antibody is capable of treating the condition in an activated state, and has two light chains and two heavy chains. Each inhibitory domain includes a hinge domain of an immunoglobulin and consists of two peptide arms. Each cleavable linker includes a peptide substrate cleavable by an enzyme specifically or highly expressed in the target cell or tissue, and connects one of the peptide arms of the inhibitory domains to the N-terminal of one of the light chains and heavy chains of the functional antibody. Also disclosed herein are methods for preparing and using this hinge antibody.

The invention relates to a chromatography which is used for isolating and purifying immunoglobulin protein and a preparation method and belongs to the preparation technology of isolating and purifying a chromatography medium of the immunoglobulin. The chromatography medium refers to the end of a space arm that is coupled with a double-loop compound molecular which has an imidazol group and a benzene ring as a chromatography medium matrix. The preparation method uses an allylic chromatography medium and a bromide alchoholization reaction of N-bromosuccinimide to get an activated chromatography medium which reacts with the amino of the double-loop compound to complete the coupling of the matrix in dimethyl sulfoxide solution. The chromatography medium has higher dynamic adsorption capacity to the antibody within the ionic strength scope from 0.02 mol/L to 2.0 mol/L and is directly applied to the recycling of the antibody in the solid to liquid; at he same time, the medium has more moderate elution condition and can purify the antibody from serum, ascites, cell culture supernatant and other solid to liquid having the antibody. The chromatography medium has the wide application prospect in the process of antibody preparation.

This invention discloses monoclonal antibody against anti-LCDV immunoglobulin of Paralichthys olivaceus, which is excreted by hybridoma JF-lgM-H (CCTCC-C200631). The method comprises: immunizing Paralichthys olivaceus with LCDV inactivated by formalin to prepare antiserum, purifying Paralichthys olivaceus immunoglobulin, immunizing Balb/c mice as antigen, preparing hybridoma cells by cell engineering method, and screening the monoclonal antibody by immunoassay. Indirect ELISA and indirect immunofluorescent antibody assay show that this monoclonal antibody is located on the heavy chain (7-80 kDa) of the anti-LCDV immunoglobulin. The monoclonal antibody can be used for preparing reagents for detecting LCDV infection in early stage, and evaluating the immune effects of LCDV vaccine inactivated by formalin.

It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity. The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined. Substitution of even a single amino acid within each of the epitopes led to loss of IgE binding. Although the epitopes shared no common amino acid sequence motif, the hydrophobic residues located in the center of the epitope appeared to be most critical to IgE binding.

The application discloses methods for simultaneous detection and quantifying multiple target analytes, including immunoglobulin isotypes and sub-classes, single and multiple protein antibodies within a test sample in a single reaction vessel. The method uses reaction wells as on a multi-well plate, each single well comprising microarrays of: calibration spots, having a predetermined quantity of a target analyte; and capture spots, having multiple agent antibodies, including isotypes and subclasses that specifically bind the target analytes. The captured analytes and the calibration spots are detected with fluorescently labeled antibodies specific for each analyte. The application also discloses methods for detecting and quantifying biomarkers, therapeutic proteins and patient derived antibodies; the use of secondary reagents to determine immunoglobulin classes Ig G, A, M, E and sub-classes including IgG1, IgG2, IgG3, IgG4 and IgA. The intensity of each fluorescent signal allows measurement of a specific immune response to a therapeutic protein and associated analytes.

The invention concerns a method for determining antigen-specific antibodies of a particular immunoglobulin class in a sample by means of an immunoassay in an array format in which various binding partners B_nx are bound on different discrete areas on a support where B_nx in each case contain the various antigens that are able to specifically bind to the antibodies to be detected, by incubating the support with the sample and a binding partner B₂ which carries a label and subsequently detecting the label on the respective discrete areas wherein B₂ specifically binds antibodies of a certain immunoglobulin class that have been bound in an antigen-specific manner.