43 results about "IgG binding" patented technology

The invention involves viral vectors that can be used to transduce a target cell, i.e., to introduce genetic material into the cell. The targets of interest are eukaryotic cells and particularly human cells. The transduction can be done in vivo or in vitro. More particularly the invention concerns viral vectors that have chimeric envelope proteins and contain the IgG-binding domain of protein A. These vectors when used in conjunction with antibodies targeting a particular cell are particularly useful for gene therapy.

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.

Antibodies to FcRn are provided which are non-competitive inhibitors of IgG binding to FcRn. The antibodies may be polyclonal or monoclonal or antigen binding fragment thereof. These antibodies are useful for reducing the concentration of pathogenic IgGs in individuals and therefore used as a therapeutic tool in autoimmune and alloimmune conditions.

The present invention relates to site-specific labeling of antibodies or fragments thereof with one or more reporter group(s) in a way that does not affect antigen binding. The method for labeling antibodies and/or fragments thereof, comprises the following steps a) providing an IgG binding protein, which comprises α-helix structures, with a photoactivatable group and at least one label; b) forming a mixture of said IgG binding protein and the antibodies and/or fragments to be labeled; and c) UV illuminating said mixture for site-specific labeling of said antibodies and/or fragments thereof. The IgG binding protein is preferably the Z domain of Protein A.

The invention discloses a recombinant Protein A protein and a preparation method of an affinity chromatography medium. The protein is a mutant of parent immune globulin-binding protein as defined by SEQ ID No 1 and SEQ ID No 2; and the preparation method of the affinity chromatography medium comprises the following steps: S1, synthesizing genes of the recombinant Protein A protein, S2, respectively constructing expression vectors by using the genes synthesized in the S1, S3, culturing, expressing and purifying to obtain a recombinant Protein A solution with a corresponding sequence of SEQ ID, and S4, preparing the affinity chromatography medium by using the recombinant Protein A. The preparation method has the advantages that the chemical stability of the Protein A in alkali liquor is greatly improved by redesigning an amino acid sequence, so that the Protein A with a specific binding effect on an antibody is provided, the Protein A has good chemical stability under an alkaline condition, the binding load of the recombinant Protein A and affinity chromatography medium is remarkably improved, in-place cleaning under 0.5-1.0 M NaOH can be tolerated, and the IgG binding load is 60-90 mg/ml.

The present invention describes diagnosis and treatment of antibody-mediated inflammatory auto-immune diseases. The biochemical mechanisms underlying such disorders are described as characteristic molecular markers and antibody-mediated ligand-receptor interactions. Specifically, the activation of T-cells by disease specific IgG binding to the IGF-1 receptor is shown to underlie thyroid associated ophthalmopathy associated with Graves' disease and rheumatoid arthritis. Diagnostics for detection of disease are provided, as are therapeutics based on the determination of the mechanisms underlying a particular pathology.

The invention relates to the technical field of immunology, in particular to IgG epitope peptide of whey allergen beta-lactoglobulin. The invention provides an IgG binding epitope of beta-lactoglobulin, and the epitope aims at the epitope of specific cow milk whey allergen of Chinese population, and has great significance on the molecular mechanism of cow milk allergy, the screening of protease for guiding directional breaking of the epitope and the development of low-allergy whey protein products based on the epitope.

The present invention relates to an IgG-binding compound, which more specifically has affinity for human IgGs of κ-type and functional derivatives thereof. More specifically, the compound according to the invention comprises an N,N-alkylated urea moiety located between an aromatic part and another part, which is a linear or cyclic substituted or unsubstituted aliphatic group. The compound binds to a pocket-shaped binding site present on all human IgG κ-Fabs, which site is located between the two domains (CH1 and CL) of its constant part. Accordingly, the compound according to the invention is a ligand for human IgGs of κ-type, and consequently, the invention also relates to a separation matrix for affinity chromatography, which matrix comprises said compound, as well as to other uses of the compound.

The present invention provides an IgG-binding peptide which can be used for the purification of IgG and has excellent stability, e.g., alkali stability. The present invention also provides a method for purifying IgG using the IgG-binding peptide. Specifically, the present invention relates to a solid-phase support including an IgG-binding peptide, an IgG separation column including the solid-phase support, a kit including the solid-phase support or the column, and a method for purifying IgG using the solid-phase support or the column.

The invention provides a multispecies universal detection protein with green fluorescence activity and application of the universal detection protein. The universal detection protein is characterizedin that the detection protein comprises a streptococcus protein G (SPG) segment and a fluorescent protein; and an IgG binding segment of an SPG gene is reconstructed, only a C3 region where the protein G can be specifically bound with the Fc terminal of an antibody IgG is retained, the C3 region is divided into three groups of C3, C3-D-C3 and C3-D-C3-D-C3, all the groups are connected to EGFP, anda prepared recombinant protein has the fluorescence activity and dual activity of binding to antibodies of different species. Disclosed evolutionary immunoglobulin binding molecules can widely bind to total IgG and IgG of different subclasses in humans and many animals in a wide spectrum mode, and compared with immunoglobulin binding molecules in the prior art, the binding force of the evolutionary immunoglobulin binding molecules is also higher than that of the existing immunoglobulin binding molecules.

The invention provides a novel coronavirus antibody detection kit as well as a preparation method and application thereof. The kit comprises an IgG binding molecule, an anti-IgM antibody, fluorescently-labeled novel coronavirus S1 protein, fluorescently-labeled novel coronavirus N protein, an hIgG antibody positive standard substance of the S1 protein, an hIgG antibody positive standard substanceof the N protein, an hIgM antibody positive standard substance of the S1 protein, an hIgM antibody positive standard substance of the N protein, a negative control hIgG antibody sample and a negativecontrol hIgM antibody sample, wherein the IgG binding molecule and the anti-IgM antibody are loaded on nanoparticles with different particle sizes. The kit disclosed by the invention is used for detecting novel coronavirus antibodies, can be used for quickly detecting novel coronavirus neutralizing antibodies in serum within 12 h, and has the advantages of small dosage of a to-be-detected sample,good specificity, high sensitivity, good repeatability, simplicity in operation, low laboratory requirement and high safety.

Provided is a peptide that specifically or selectively binds to human IgG. This peptide comprises an amino acid sequence consisting of 13 to 17 amino acid residues and is capable of binding to human IgG, wherein the amino acid sequence is represented by formula I: (X_1-3)-C-(X₂)-H-R-G-(Xaa1)-L-V-W-C-(X_1-3), wherein, X each independently represents any amino acid residue except cysteine, C represents a cysteine residue, H represents a histidine residue, R represents an arginine residue, G represents a glycine residue, Xaa1 represents a glutamic acid residue or an asparagine residue, L represents a leucine residue, V represents a valine residue, and W represents a tryptophan residue.

The present invention relates to a human IgG binding pocket comprised of a first interacting surface, which originates from an IgG κ light chain, and a second interacting surface, which originates from an IgG heavy chain, which amino acids are strictly conserved between human IgGs of κ-type. The invention also embraces an isolated and purified polypeptide, which comprises said binding pocket. Further, the invention relates to various methods of using the novel binding pocket, such as in screening for identification of chemical entities capable of selective binding thereof, and in other experimental and/or virtual methods for design and/or identification of chemical entities capable of selective binding thereof.

The invention discloses a protein A variant, and particularly relates to a protein A variant with high alkali resistance and high IgG binding affinity. The invention also discloses application of the protein A variant.

Disclosed herein are recombinant polypeptides comprising one or more homologous amino acid repeats fused to an IgG binding domain. The recombinant polypeptide can bind to a therapeutic antibody and act as a delivery vehicle to increase the retention time of the therapeutic antibody and reduce systemic-related side effects of the therapeutic antibody. Also disclosed herein are pharmaceutical compositions comprising a recombinant polypeptide that binds to a therapeutic antibody; and methods of administering them to a patient to treat cancer.