17 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.

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.

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.

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 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.

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 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 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.