262 results about "Human immunoglobulin" patented technology

Disclosed are binding molecules which are recombinant polypeptides containing: (i) a binding domain capable of binding a target molecule, and (ii) an effector domain having an amino acid sequence substantially homologous to all or part of a constant domain of a human immunoglobulin heavy chain; characterized in that the binding molecule is capable of binding the target molecule without triggering significant complement dependent lysis, or cell mediated destruction of the target, and more preferably wherein the effector domain is capable of specifically binding FcRn and/or FcγRIIb. These are generally based on chimeric domains which are derived from two or more human immunoglobulin heavy chain CH2 domains domains. In preferred embodiments the regions 233-236, and 327-331, are modified, as are further residues to render the molecule null allotypic. Also disclosed are nucleic acids, host cells, production processes and materials, and uses. Pharmaceutical preparations are also disclosed.

The invention uses the power of display selection methods to screen libraries of human immunoglobulin genes from nonhuman transgenic animals expressing human immunoglobulins. Such screening produces unlimited numbers of high affinity human antibodies to any target of interest.

The invention relates to long-acting and stable oxyntomodulin (OXM). An Fc segment of human immunoglobulin G and the human OXM form fusion protein through a connecting peptide. A method for preparing the fusion protein comprises the following steps of: preparing the human OXM and an Fc segment gene of the human immunoglobulin respectively, and connecting the human OXM and the Fc segment gene of the human immunoglobulin to construct connecting segment-containing recombinant expression vectors; and transforming host cells by using the recombinant expression vectors, culturing the host cells and recovering from cell culture and purifying the host cells to obtain the recombinant fusion protein. The fusion protein can be used for preparing medicaments for treating metabolic diseases such as diabetes and obesity.

Non-human animals, tissues, cells, and genetic material are provided that comprise a modification of an endogenous non-human heavy chain immunoglobulin sequence and that comprise an ADAM6 activity functional in a rodent (e.g., a mouse), wherein the non-human animals rearrange human immunoglobulin light chain gene segments in the context of heavy chain constant regions and express immunoglobulin-like molecules comprising human immunoglobulin light chain variable domains fused to heavy chain constant domains that are cognate with human immunoglobulin light chain variable domains fused to light chain constant domains.

A genetically modified non-human animal is provided, wherein the non-human animal expresses an antibody repertoire capable of pH dependent binding to antigens upon immunization. A genetically modified non-human animal is provided that expresses human immunoglobulin light chain variable domains derived from a limited repertoire of human immunoglobulin light chain variable gene segments that comprise histidine modifications in their germline sequence. Methods of making non-human animals that express antibodies comprising histidine residues encoded by histidine codons introduced into immunoglobulin light chain nucleotide sequences are provided.

A human interleukin 15-Fc fusion protein composed of interleukin 15 and the Fc fragment of human immunoglobulin, which are linked via joining peptide, the nucleic acid ofr coding it, the expression carrier containing said nucleic acid, its composite medicine for preventing and treating microbial infection and its preparing process are disclosed.

This invention describes a novel format of monomeric bispecific fusion protein with immune activating property for clinical therapies. A bispecific fusion protein includes a first targeting domain with a specificity for a first target of interest; a bridging domain derived from a constant region of a light chain or heavy chain of an immunoglobulin, which may be a human immunoglobulin; and a second targeting domain with a specificity for a second target of interest. The bispecific fusion protein may further include a linker fused to the N-terminus or the C-terminus of the bridging domain. The first targeting domain is fused to the bridging domain and the second targeting domain is fused to the bridging domain or the linker. The linker may include a GGGGS sequence. The first target of interest may be CD20, Her2/neu, or EpCAM, and the second targeting domain is a T-lymphocyte activating domain.

The present invention comprises non-human vertebrate cells and non-human mammals having a genome comprising an introduced partially human immunoglobulin region, said introduced region comprising human V_H coding sequences and non-coding V_H sequences based on the endogenous genome of the non-human mammal.

The invention relates to a method for separating and purifying human immunoglobulin from a component I+III of blood plasma, and aims to provide a high-efficiency method for recovering high-purity human immunoglobulin. According to the technical scheme provided by the invention, the method comprises the following steps of: a, fully dissolving component I+III precipitate; b, precipitating with octylic acid and removing lipid and a part of impurity protein to prepare IgG (Immunoglobulin G); c, purifying through anion exchange column chromatography; and d, collecting flow-through liquid, performing membrane nanofiltration, ultrafiltration and concentration, preparing the human immunoglobulin, sterilizing and packaging. The method has the beneficial effects of capability of being operated at the room temperature, simple and short steps, high yield, low energy consumption and high output and is suitable for mass production; comprehensive utilization of the blood plasma is fully realized; the time of the entire production process is shortened; the cost is reduced; extremely considerable economic benefit can be produced; the safety of a product is guaranteed by using two virus inactivation/elimination methods of different mechanisms; the environmental pollution is avoided; and the method has high economic and social values.

The present invention is related with the obtaining of modified antibodies by means of the DNA recombinant technology from the murine monoclonal antibody P3 (MAb P3) produced by the hybridoma cell line deposited under Budapest Treaty with accession number ECACC 94113026 and from its anti-idiotype murine monoclonal antibody 1E10(MAbai 1E10) produced by the hybridoma cell line with deposit number ECACC 97112901, with the objective of achieving monoclonal antibodies which preserve the biological function of specific binding to the antigen of the original antibodies, but being at the same time less immunogenic. The chimeric antibodies of the invention contain the variable domains of the murine immunoglobulin and the constant regions of the human immunoglobulin; and those humanized, besides containing the constant regions of the human immunoglobulins, they are modified in the region of the murine frameworks (FRs) and in particular in those zones that could be in an antigenic site for the T cells, so several positions of the FRS are human as well. These antibodies can be used in the diagnosis and therapy of different types of tumors. The present invention is also related with use of the antibodies for therapeutical and diagnostic purposes.

The invention discloses a recombined human hyaluronidase, a production and purification method and preparations of the recombined human hyaluronidase, a use method and application. Recombined human hyaluronidase PH20 or human hyaluronidase human albumin fusion protein PH20-HSA or human hyaluronidase human immunoglobulin IgG2Fc fragment fusion protein PH20-IgFc is adopted by the recombined human hyaluronidase and used in the mucosa or the surface of the skin. The preparations of the recombined human hyaluronidase can be made into different types such as membrane preparations, spray preparations, lotion and freeze-dried powder spray and used for skin infiltration promotion of beauty nutrient substances, skin mucosa infiltration promotion of surface anesthetic, infiltration promotion of skin disease therapeutic medicine, mucosa infiltration promotion of biological tranquillizer, mucosa skin infiltration promotion of growth factors, mucosa infiltration promotion of hypoglycemic drug, mucosa nasal cavity infiltration promotion of nervous centralis nutrient substances and the like.

The invention relates to a process for preparing human immunoglobulin for intravenous injection, and belongs to the field of biological pharmacy. The precipitate of components II and III in the process for preparing the human immunoglobulin for intravenous injection is treated by a caprylic acid and calcium chloride precipitation method, miscellaneous proteins are removed from the precipitate of the components II and III, and two-step chromatography is performed. Compared with the general caprylic acid precipitation method, the process has the advantages that various blood coagulation factors are effectively removed from a precipitate solution of the components II and III by adding calcium chloride, the stability of the immunoglobulin is improved, and the yield of the product is obviously improved, namely more than 7g of immunoglobulin can be prepared from each liter of blood plasma; upper column chromatographic purification is performed by two ion exchange columns and a chromatographic technology, so that the miscellaneous proteins can be effectively removed, and the purity of the product is over 99.5 percent; and in addition, caprylic acid is added, and viruses are removed and filtered by a DV20 filter element, so that a virus removing effect can be obviously improved, and the safety of clinical medication is improved.

The invention relates to the technical field of biology, and particularly, relates to a recombinant human GLP-1-Fc fusion protein and a preparation method and an application thereof. The invention provides the recombinant human GLP-1-Fc fusion protein, wherein the recombinant human GLP-1-Fc fusion protein comprises two structural function regions which are respectively a recombinant GLP-1 fragment and a human immunoglobulin Fc fragment, and the recombinant GLP-1 fragment has the amino acid sequence shown in SEQID No.1. The recombinant human GLP-1-Fc fusion protein provided by the invention has the homology with an original GLP-1 molecule reaching 97%, and still maintains excellent biological activity and zoology activity.

A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo in comparison to naturally occurring or recombinant native human erythropoietin. In one embodiment of the invention, the protein has a half-life in vivo at least three fold higher than native human erythropoietin. The fusion protein also exhibits enhanced erythropoietic bioactivity in comparison to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human immunoglobulin IgG1. The Fc fragment in the fusion protein includes the hinge region, CH2 and CH3 domains of human immunoglobulin IgG1. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen the risk of an immunogenic response when administered in vivo. In one embodiment the hinge region is a human Fc fragment variant having a non-cysteine residue at amino acid 6. The invention also relates to nucleic acid and amino acid sequences encoding the fusion protein and transfected cell lines and methods for producing the fusion protein. The invention further includes pharmaceutical compositions comprising the fusion protein and methods of using the fusion protein and/or the pharmaceutical compositions, for example to stimulate erythropoiesis in subjects in need of therapy.

The present disclosure provides a fusion protein comprising IL-1 receptor antagonist fused to a hybrid Fc. Particularly the present disclosure relates to a fusion protein comprising IL-1 receptor antagonist fused to a human immunoglobulin hybrid Fc fragment. In one embodiment, the hybrid Fc fragment comprises IgD and IgG4. Also provided is a pharmaceutical composition comprising the present fusion protein, which are useful for treating autoimmune disease including rheumatoid arthritis, inflammatory bowel disease (Crohn's disease, ulcerative colitis), psoriasis and diabetes and the like. The present fusion protein with excellent efficacy and reduced side effects is qualified for clinical development as therapeutic antibodies to treat autoimmune disease.