29 results about "Immunoglobulin binding" patented technology

The invention relates to the technical field of allergen proteins and antigen epitopes, and discloses an Antarctic krill allergen and an identification method and application of the Antarctic krill allergen, the Antarctic krill allergen and the antigen epitopes are used for identifying the Antarctic krill allergen and the antigen epitopes, and the identification method comprises the steps of Antarctic krill crude protein extraction, Antarctic krill allergen screening and identification. Extracting an antarctic krill map and verifying allergens; analyzing the homology of the euphausia superba and analyzing the conformation of tropomyosin of the euphausia superba; carrying out euphausia superba tropomyosin epitope analysis; and allergens and epitopes of the euphausia superba are applied. According to the invention, the antarctic krill allergen is identified as tropomyosin, eight antigen epitopes of the antarctic krill tropomyosin allergen are ascertained, the stability change rule in the hot working process is analyzed by utilizing the identified antarctic krill allergen and antigen epitopes, and the result shows that the stability of the antarctic krill allergen is greatly improved under the processing condition of 140 DEG C or below. And the conformation of the tropomyosin of the euphausia superba and the binding capacity of the tropomyosin with protein immune globulin E or immune globulin G are kept stable.

An affinity carrier may have improved alkali resistance. An immunoglobulin-binding protein containing a mutant polypeptide chain, as well as an affinity carrier containing a solid-phase carrier to which the immunoglobulin-binding protein is bound, may be a mutant polypeptide chain having an amino acid sequence having at least 85% identity to an amino acid sequence indicated by any of SEQ ID NO: 1-6 and 57-62, having a predetermined mutation, and having immunoglobulin-binding activity.

Immunoglobulin complementarity determining regions ("CDRs"), and immunoglobulin binding domains comprising those CDRs, that bind human lymphocyte antigen 6 family member G6D (LY6G6D), and their use for the preparation of LY6G6D-binding proteins finding use as immunotherapeutics.

Immunoglobulin (Ig) binding proteins having one or more domains having highly hydrophobic amino acids with branched side chains (Iso, Leu, Val), or aromatic amino acids (Tyr, Phe, or Trp) corresponding to position 4 or 6 or 8 of the Ig binding protein of SEQ ID NO: 1 or functionally similar proteins are provided. The disclosed proteins have superior properties for highly efficient purification methods for antibodies (immunoglobulins), for example, the proteins have high binding capacity and high chemical stability. Also provided are affinity matrices that include the disclosed Ig binding proteins, uses of these Ig binding proteins and / or affinity matrices for affinity purification of immunoglobulins, and methods for affinity purification using the disclosed Ig binding proteins.

The present invention relates to mutated immunoglobulin-binding polypeptides. An Fc-binding polypeptide with improved base stability comprising a mutant of an Fc-binding domain of Staphylococcus Protein A (SpA), said mutant being defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 22, SEQ ID NO 51 or EQ ID NO 52, wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO: 4-7 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.

Immunoglobulin complementarity determining regions ("CDRs"), and immunoglobulin binding domains comprising those CDRs, that bind human lymphocyte antigen 6 family member G6D (LY6G6D), for the preparation of multispecific LY6G6D / CD3 binding proteins and their use in a multispecific format with a CD3-binding moiety.

Immunoglobulin complementarity determining regions (“CDRs”), and immunoglobulin binding domains comprising those CDRs, that bind human lymphocyte antigen 6 family member G6D (LY6G6D), and their use for the preparation of LY6G6D-binding proteins finding use as immunotherapeutics.

The application provides a fusion protein PA-G which fuses Ig dominant binding domains of protein A and protein G, and the amino acid sequence of the fusion protein PA-G is as shown in SEQ ID NO. 1. The fusion protein PA-G disclosed by the application has the immunoglobulin binding capacity, has the larger biological characteristic potential than protein A and protein G, has the better affinity and faster binding efficiency for different species and subtypes of immunoglobulins, and through acid and alkali resistance research experiments, it is found that the most important thing of the fusion protein PA-G is that the pH tolerance is wider, and the application prospect and application range are wider.

Immunoglobulin complementarity determining regions ("CDRs"), and immunoglobulin binding domains comprising those CDRs, that bind human lymphocyte antigen 6 family member G6D (LY6G6D), and their use for the preparation of LY6G6D-binding proteins finding use as immunotherapeutics.

The present invention relates to immunoglobulin (Ig) binding proteins comprising one or more domains having highly hydrophobic amino acids with branched side chains (Iso, Leu, Val), or aromatic amino acids (Tyr, Phe, or Trp) corresponding to position 4 or 6 or 8 of the Ig binding protein of SEQ ID NO: 1 or functionally similar proteins. The novel proteins have superior properties for highly efficient purification methods for antibodies (immunoglobulins), for example, the proteins have high binding capacity and high chemical stability. The invention further relates to affinity matrices comprising the Ig binding proteins of the invention. The invention also relates to a use of these Ig binding proteins or affinity matrices for affinity purification of immunoglobulins and to methods of affinity purification using the Ig binding proteins of the invention.

The present invention relates to mutated immunoglobulin-binding polypeptides. An Fc-binding polypeptide with improved base stability comprising a mutant of an Fc-binding domain of Staphylococcus Protein A (SpA), said mutant being defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 22, SEQ ID NO 51 or EQ ID NO 52, wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO: 4-7 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.

The present disclosure provides an improved binding molecule comprising an immunoglobulin binding domain having an affinity for a peptide tag moiety. The binding molecules can be used, for example, as part of bispecific conjugates. The binding molecules exhibit unexpected advantages as part of biopharmaceutical products as compared to known binding molecules with similar binding affinity. The disclosure also provides bispecific conjugates comprising a binding molecule and complexes comprising a bispecific conjugate non-covalently bound to a tag construct comprising a peptide tag moiety and a cargo domain comprising an antigen for delivery of the antigen to an immune cell. The disclosure also provides medical uses of the binding molecules, conjugates and complexes of the disclosure.

The present invention relates to heterologous polypeptide or multimeric proteins and nucleic acids encoding the same comprising at least one immunoglobulin binding domain and at least one immune cell surface polypeptide or protein binding domain. The molecules of the invention can be used as monotherapy or for enhancing standard, current or experimental antibody-based immunotherapy, such as cancer, autoimmunity or pathogenic infections.

To provide a method that enables separation of a multispecific antibody contained in a sample.SOLUTION: A method for separating a multispecific antibody comprises the steps of: bringing a sample containing a multispecific antibody into contact with an antibody adsorbent comprising an insoluble carrier and an immunoglobulin-binding domain of Protein L (FpL) derived from a bacterium of the genus Finegoldia immobilized on the insoluble carrier, thereby adsorbing the antibody onto the adsorbent; and eluting the antibody adsorbed on the adsorbent using an eluent. Therein the eluent contains chloride ions, and the elution step elutes the antibody by a gradient that decreases a chloride ion concentration and a pH of the eluent, thereby solving the problem to be solved.SELECTED DRAWING: Figure 5

Immunoglobulin complementarity determining regions ("CDRs"), and immunoglobulin binding domains comprising those CDRs, that bind human lymphocyte antigen 6 family member G6D (LY6G6D), for the preparation of multispecific LY6G6D / CD3 binding proteins and their use in a multispecific format with a CD3-binding moiety.

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support: b) contacting a liquid sample comprising an immunoglobulin with the separation matrix; c) washing said separation matrix with a washing liquid; d) eluting the immunoglobulin from the separation matrix with an elution liquid, and e) cleaning the separation matrix with a cleaning liquid, wherein the alkali-stabilized Protein A domains comprise mutants of a parental Fc-binding domain of Staphylococcus Protein A (SpA).

The present disclosure relates to non-porous polymer particles having an average particle size of from 1 micron to 10 microns and functionalized with an immunoglobulin binding protein. The functionalized particles of the present disclosure can be used to purify a range of immunoglobulins having affinity for immunoglobulin binding proteins.

The present invention relates to novel engineered artificial immunoglobulin (Ig) binding polypeptides comprising three domains and two linkers. The invention further relates to affinity matrices comprising these artificial Ig binding molecules of the invention. The novel Ig binding proteins are particularly useful for the affinity purification of proteins requiring elution at a higher pH (in particular higher than pH 4.2). The invention also relates to a use of the novel Ig binding proteins or affinity matrices for affinity purification of immunoglobulins and to methods of affinity purification using the novel Ig binding proteins of the invention.

The present invention relates to mutated immunoglobulin-binding polypeptides. An Fc-binding polypeptide with improved base stability comprising a mutant of an Fc-binding domain of Staphylococcus Protein A (SpA), said mutant being defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 22, SEQ ID NO 51 or EQ ID NO 52, wherein at least the asparagine or serine residue at the position corresponding to position 11 in SEQ ID NO: 4-7 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.

The present disclosure provides improved binding molecules comprising an immunoglobulin-binding domain with affinity for a peptide tag moiety. The binding molecules are useful, for example, as part of a bispecific conjugate. They offer unexpected advantages as part of a biopharmaceutical product when compared with known binding molecules with similar binding affinities. Also provided are bispecific conjugates comprising the binding molecules, and complexes comprising the bispecific conjugates non-covalently linked to tag constructs comprising a peptide tag moiety and a cargo moiety comprising an antigen, for antigen delivery to immune cells. Medical uses of the binding molecules, conjugates, and complexes of the present disclosure are also provided.

To provide a method that enables efficient production of a polypeptide containing at least an immunoglobulin-binding domain of Protein L (FpL) originating from Finegoldia bacteria.SOLUTION: A production method comprises the step of culturing a recombinant Escherichia coli containing a polynucleotide encoding a polypeptide including at least an immunoglobulin-binding domain of FpL and expressing the polypeptide, and the step of purifying the polypeptide from a culture of the Escherichia coli, wherein the step includes a purification step using an anion-exchange chromatography and a purification step using a hydrophobic chromatography, wherein the purification step using the hydrophobic chromatography includes a step of equilibrating a hydrophobic chromatography column, a step of adding a sample containing the polypeptide to the column, and a step of recovering the polypeptide, wherein at least one of a solution for equilibrating the column and the sample contains 0.4 mol / L-1.1 mol / L ammonium sulfate.SELECTED DRAWING: Figure 10

Disclosed is a protein which comprises an amino acid sequence derived from an immunoglobulin-binding domain of a protein L of a bacterium belonging to the genus Vincura, said amino acid sequence having at least one or more amino acid substitutions selected from the group consisting of (1) to (5) below. The protein has immunoglobulin binding activity: (1) an amino acid residue equivalent to tyrosine at position 42 of SEQ ID NO: 1 is substituted with histidine; (2) an amino acid residue equivalent to the lysine at position 22 of SEQ ID NO: 1 is substituted with glutamic acid; (3) an amino acid residue corresponding to the lysine at position 38 in SEQ ID NO: 1 is substituted with proline or aspartic acid; (4) an amino acid residue equivalent to tyrosine at position 42 in SEQ ID NO: 1 is substituted with tryptophan or phenylalanine; (5) The amino acid residue equivalent to the asparagine at position 44 in SEQ ID NO: 1 is substituted with proline.

The present invention relates to bifunctional small molecules containing a circulating protein binding moiety (CPBM) linked to a cell receptor binding moiety (CRBM) by a linking group, the CRBM being a membrane receptor of a degrading cell such as a hepatocyte or other degrading cell. In certain embodiments, the (CPBM) is a moiety that binds to immunoglobulin G. In certain embodiments, the (CRBM) is a moiety that binds to an asialoglycoprotein receptor of a hepatocyte (an asialoglycoprotein receptor binding moiety, or an ASGPRBM).

The present invention analyzes an N-linked glycan linked to a protein in a blood-derived sample collected from a subject, and, on the basis of the structure of the N-linked glycan, predicts the structure of a glycan linked to immunoglobulin in the subject's blood after administration when the immunoglobulin has been administered to the subject.

The disclosure relates to binding proteins, including antibodies, that bind to Programmed Death-1 (“PD-1”) and T cell immunoreceptor with Ig and ITIM domains (“TIGIT”). The disclosure also provides compositions comprising such binding proteins and nucleic acid molecules encoding such binding proteins. The disclosure further relates to methods of treating a disorder or condition using such binding proteins.

The invention discloses a PLAG-Tn5 fusion protein as well as a preparation method and application thereof. According to the fusion protein, dominant immunoglobulin binding structural domains of Protein L, Protein A and Protein G are functionally fused with Tn5 transposase, so that IgG antibodies of various genus sources such as mice, rats and rabbits can be efficiently recognized in a broad-spectrum manner, and the problem of existing CUTamp is thoroughly solved; and the problems of poor antibody compatibility, need of using a second antibody, low signal-to-noise ratio and the like caused by insufficient PA / PG-Tn5 affinity in a Tag technology are solved. The invention also provides a low-cost and high-yield preparation method of the fusion protein and a matched preparation process of low-cost and high-efficiency carboxyl nucleic acid purification magnetic beads. The fusion protein and the magnetic beads jointly form the CUTamp which is low in cost, high in efficiency and high in sensitivity. A Tag research system is especially suitable for protein-DNA interaction research of precious low-amount clinical samples such as primary cells and PBMC, and popularization and clinical transformation of the technology are powerfully promoted.