32 results about "Immunoglobulin Variable Region" patented technology

The present invention provides methods for producing mutationally-altered immunoglobulins and compositions containing such mutationally-altered immunoglobulins, wherein the mutationally-altered immunoglobulins have at least one mutation that alters the pattern of glycosylation in a variable region and thereby modifies the affinity of the immunoglobulin for a preselected antigen. The methods and compositions of the invention provide immunoglobulins that possess increased affinity for antigen. Such glycosylation-altered immunoglobulins are suitable for diagnostic and therapeutic applications.

The present invention provides an isolated protein comprising an immunoglobulin variable region comprising at least two cysteine residues positioned within framework region (FR) 2 and/or at least two cysteine residues positioned within framework region (FR3), wherein if at least two of the cysteine residues in FR2 and/or FR3 are not conjugated to a compound then an intra-framework disulphide bond is capable of forming between the cysteine residues. Preferably the protein comprises an immunoglobulin heavy chain variable region (V_H) and an immunoglobulin light chain variable region (V_L), wherein at least one of the variable regions comprises the two cysteine residues. The present invention also provides conjugates of the protein and another compound.

The present invention is based, at least in part, on the discovery that strategic modifications of non-human donor antibody CDR residue(s) can be used to humanize antibodies. Such modifications modulate the 3D structural fit between donor antibody CDRs and human acceptor antibody framework regions that comprise the variable domains of a CDR-grafted antibody. Whereas prior art methods of humanization have relied on making framework substitutions (in which selected human framework residues are backmutated to the corresponding amino acid residue present in the non-human donor antibody), the instant invention is based, at least in part, on a method of humanizing antibodies in which selected CDR residues, and optionally adjacent FR residues, are changed in order to accommodate differences in FR amino acid sequences between donor and acceptor antibodies.

The present invention provides an isolated protein comprising an immunoglobulin variable region comprising at least two cysteine residues positioned within framework region 1 such that if at least two of the cysteine residues are not conjugated to another compound a disulphide bond forms between the cysteine residues. Preferably the protein comprises an immunoglobulin heavy chain variable region and an immunoglobulin light chain variable region, wherein at least one of the variable regions comprises the two cysteine residues. The present invention also provides a protein that binds to TAG72. The present invention also provides conjugates of the protein and another compound.

The invention provides a bifunctional fusion molecule comprising: a first functional domain comprising a first immunoglobulin variable region, a second immunoglobulin variable region and a linker for connecting the first and second variable regions; a second functional domain comprising a moiety for binding to an antigenic agent; wherein the first and second functional domains are linked; and wherein the first functional domain specifically binds to a surface molecule of a professional antigen-presenting cell, and uses thereof.

This invention provides variable region gene of anti-human CD19 Mouse IgE ELISA, which has the nucleotide sequence of SEQ ID NO. 1 and SEQ ID NO. 2 as well as the amino acid sequence of SEQ ID NO. 3 and SEQ ID NO. 4. The mono-clone anuibody of this invention has the characteristic that identify B lymphocyte tumour cell membrane CD19 antigen but not identify other tissue and cell composition. The in vitro indicates that this antibody can selectively kill the B-ALL cell, so this kind of antibody has broad potential application prospect in curing B lymphocytes malignant tumor, including leukaemia, lymphoma. It can be applied to the medicine that curing B lymphocytes malignant tumor.

The invention relates to an antibody library. An immune globulin light chain variable region VL gene sequence is inserted between Xba and Sac restriction enzyme cutting sites of a Pcomb3 vector. An immune globulin heavy chain variable region VH gene sequence is inserted between Spe and Xho endo restriction enzyme cutting sites. The antibody library is characterized in that two gene fragments comprise the possible combination of antibody variable region light chain and heavy chain, and the antibody library can realize affinity enrichment with an avian influenza virus antigen, and can be applied to avian influenza immunodetection. The antibody library has the advantages that a high affinity antibody can be acquired without animal immunity; a preparation period is short; the antibody library is a phage antibody library which is constructed by taking mice natural immune globulin variable region light chain and heavy chain genes as sources, theoretically contains all possible antibodies in a mice, and is a specificity antibody library which can directly acquire different avian influenza viruses through screening; and the screening has the advantages of high efficiency, high flux, large selection base and high specificity, thus the phage antibody library has a wide application prospect in the aspect of the disease detection of avian influenza and other animals.

The invention discloses a staphylococcus aureus-specific egg yolk immunoglobulin (IgY) variable region single-chain antibody. The specific egg yolk immunoglobulin variable region antibody has a nucleotide sequence shown by SEQ ID No:2 and an amino acid sequence shown by SEQ ID No:1. The single-chain antibody has relatively strong binding capacity with staphylococcus aureus, namely that the screened antibody has an obvious inhibition effect on the growth of staphylococcus aureus, and the inhibition effect and inhibition behavior are similar to those of penicillin and streptomycin, so that the single-chain antibody has a perfect application prospect in preparation of staphylococcus aureus antibody drugs or detection reagents. Moreover, the single-chain antibody has high specificity to staphylococcus aureus, and thus the laboratory early diagnosis and clinical treatment level of the staphylococcus aureus can be improved.

The purpose of the present invention is to provide: a mutant immunoglobulin kappa chain variable region-binding peptide characterized by the acid dissociation pH of an immunoglobulin kappa chain variable region-containing protein being shifted to the neutral side compared to prior to the introduction of a mutation; an affinity separation matrix comprising the peptide as a ligand; and a method forproducing a kappa chain variable region-containing protein using the affinity separation matrix. Another purpose of the present invention is to provide DNA that encodes the peptide, a vector containing the DNA, and a transformant that is transformed by the vector. The problem addressed by the present invention is solved by using a peptide into which a mutation has been introduced at an appropriatesite as an affinity ligand for a kappa chain variable region binding domain of protein L derived from a Peptostreptococcus magnus strain.

NKp46-binding immunoglobulin variable regions, and proteins such as antibodies and multispecific proteins that comprise the variable regions are provided. The proteins can bind and specifically redirect NK cells to lyse a target cell of interest. The proteins have utility in the treatment of disease, notably cancer or infectious disease.

The invention provides a primer group for amplifying a B lymphocyte immune repertoire and an application of the primer group. The primer group comprises a group of forward primers and a group of reverse primers. The forward primers comprise a linker sequence 1, a bar code sequence 1 and a specific sequence aiming at an immunoglobulin variable region complementation determining region 3, which areconnected in sequence from a 5' end to a 3' end, wherein the specific sequence aiming at the immunoglobulin variable region complementary determining region 3 is shown as any one of SEQ ID NO. 1 to SEQ ID NO. 12; and the reverse primers sequentially comprise a linker sequence 2, a bar code sequence 2 and a specific sequence aiming at an immunoglobulin gene constant region from the 5' end to the 3'end. The primer group is used for amplifying B lymphocytes of an IgAN patient and a normal control group, library information is collected, and the length and diversity changes of CDR3 of the IgAN patient are analyzed through sequencing.