35 results about "Human Immunoglobulin G" patented technology

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.

The invention relates to a liquid pharmaceutical composition comprising human immunoglobulins G (IgGs), comprising at least 200 mM, preferably 250 mM±50 mM, of glycine and between 20 and 100 mg/l of a non-ionic detergent, and having a pH of less than or equal to 4.8.

The invention relates to an interferon fusion protein, preparation thereof and application thereof. The interferon fusion protein is a fusion protein formed by connecting an Fc fragment of the human immunoglobulin G and the human interferon, or connecting the human interferon and the Fc fragment of the human immunoglobulin through a connecting peptide. The preparation of the fusion protein comprises the following steps of: preparing an interferon gene and an Fc fragment gene of the human immunoglobulin G respectively, connecting the interferon gene and the Fc fragment gene and then constructing a recombinant expression vector which contains the connecting fragment; and transforming host cells by using the recombinant expression vector, culturing the host cells, recovering the recombinant fusion protein from cell culturing substances and purifying the recovered product to obtain the recombinant fusion protein. The fusion protein in the invention can be applied in the preparation of antivirus medicaments, antitumor medicaments and immune adjusting medicaments.

The invention relates to a human immunoglobulin G composition characterized in that the human immunoglobulin G concentration is at least 230 g/l, which is of use in particular for subcutaneous administration.

A stable liquid formulation includes a fusion protein having an Fc domain of a human immunoglobulin G (IgG), in particular, a protein in which an Fc domain of a human immunoglobulin G (IgG) and a soluble extracellular domain of a vascular endothelial growth factor (VEGF) receptor are fused (e.g., aflibercept)). A composition for stabilizing a protein and a method for stabilizing a protein in which an Fc domain of an IgG and a soluble extracellular domain of a VEGF receptor are fused are disclosed. The present invention improves therapeutic effects on various ophthalmic diseases (e.g., retinal vein occlusion, diabetic macular edema, choroidal neovascularization and wet age-related macular degeneration, etc.) caused by abnormal angiogenesis, while pursuing stabilization of bioactivity through a stable liquid formulation suitable for intravitreal injection of an anti-VEGF-Fc fusion protein including aflibercept.

The invention discloses a liquid chip kit for detecting a lung cancer autoantibody. The kit includes: microspheres coupling antigen proteins, a biotin labeled second antibody, streptavidin-phycoerythrin, a reaction buffer and a dilution buffer solution. The antigen proteins are at least two of p62, NY-ESO-1, p53 and CAGE, wherein the microspheres coupling different antigen proteins have different color codes. The second antibody is anti-human immunoglobulin G. The liquid chip kit for detecting the lung cancer autoantibody provided in the invention realizes joint detection of four antibodies in serum on a liquid chip technology platform, and takes the p62 antibody, the NY-ESO-1 antibody, the p53 antibody and the CAGE antibody as marks, has high detection accuracy, and provides a new idea for early diagnosis of lung cancer.

The invention provides a novel I-type human immunodeficiency virus (HIV-1) infection enzyme test-free reagent kit. The reagent kit comprises A, HIV-1gp41 protein, B, a blank enzyme linked plate, C, acid eluent, D, goat anti-human immunoglobulin G (IgG) marked with horseradish peroxidase, E, tetramethyl benzidine (TMB) color development solutions and F, stop solutions.

The invention, which belongs to the technical field of medical in-vitro diagnostics, relates to a human urine immunoglobulin G detection kit based on latex-enhanced immunoturbidimetry, thereby solvinga problem of providing a human urine immunoglobulin G content detection kit having advantages of wide detection linear range, high detection accuracy, and high detection stability. The kit comprisesan R1 reagent, an R2 reagent and a calibrator. The R1 reagent includes a buffer solution, NaCl and a preservative. The R2 reagent includes a buffer solution, an antibody-coupling latex microsphere, aprotective agent and a preservative; and the antibody is the goat anti-human immunoglobulin polyclonal antibody or a rabbit anti-human immunoglobulin polyclonal antibody. The calibrator is formed by aplurality of solution; each solution includes human immunoglobulin G, a buffer solution and a preservative; and the concentrations of the human immunoglobulin G in different solutions are different.The kit has advantages of wide detection linear range, high detection accuracy, and high detection stability.

The invention discloses a preparation method of a redox probe for marking an h-IGg (Human-Immunoglobulin G) impedance immunosensor. The preparation method comprises the following steps of: dropping an absolute ethyl alcohol solution containing beta-mercaptoethylamine into an absolute ethyl alcohol solution in which 3,5-dibromosalicylaldehyde is dissolved, performing water-bath heating, recrystallizing and drying in vacuum so as to obtain beta-mercaptoethylamine shrinkage 3,5-dibromosalicylaldehyde Schiff base; preparing the absolute ethyl alcohol and N,N-dimethylformamide into a mixture solvent in a volume ratio of 2:1, dropwise adding an N,N-dimethylformamide solution containing nickel acetate into the mixture solvent of the beta-mercaptoethylamine shrinkage 3,5-dibromosalicylaldehyde Schiff base, performing water-bath heating, recrystallizing and drying in vacuum so as to obtain a beta-mercaptoethylamine shrinkage 3,5-dibromosalicylaldehyde Schiff base complex; dissolving the beta-mercaptoethylamine shrinkage 3,5-dibromosalicylaldehyde Schiff base complex into the absolute ethyl alcohol, and further adding into nanogold sol. The redox probe is simple to prepare and has the advantages of low detection limit, good stability, good reproducibility and the like when being used for marking the h-IGg impedance immunosensor to detect the h-IGg content.

The invention discloses characteristic spectrums of lung cancer and pulmonary nodule proteis as well as construction methods and application of the characteristic spectrums. The methods comprise the following steps of extracting total protein from the plasma of a lung cancer/pulmonary nodule patient group and a healthy control group respectively, carrying out enzymolysis by trypsase, carrying out iTRAQ (isobaric Tags for Relative and Absolute Quantification) labeling, carrying out two-dimensional liquid chromatographic and tandem mass spectrometric detection, and carrying out relative quantitative analysis, so that the characteristic spectrums of the proteins related to the lung cancer/pulmonary nodule are obtained, wherein in the characteristic spectrum of the protein related to the lung cancer, the protein with expression differences in the lung cancer patient group and the healthy control group is up-regulated protein (SAA1 (Serum Amyloid A 1), SERPINA1 (Alpha-1-Antitrypsin), CRP (C-Reactive Protein), IGHG4 (Human Immunoglobulin G 4) and a CFH (Complement Factor H)); in the in the characteristic spectrum of the protein related to the pulmonary nodule, the protein with expression differences in the pulmonary nodule patient group and the healthy control group is up-regulated protein (the SERPINA1 and the CRP) and down-regulated protein (the SAA1, the IGHG4 and the CFH). The characteristic spectrums are used for facilitating the research of the biological natures of the lung cancer and the pulmonary nodule, and have important significance for the normative typing of the lung cancer and the pulmonary nodule.

A method for increasing the therapeutic efficacy of a human immunoglobulin G class 1 (IgG1) antibody, includes: mutating the human CH1γ1 domain from the antibody, to restore the pairing between CH1 and CL domains that is typical of the other IgG subclasses, or by substituting the human CH1γ1 domain by the CH1 domain from a human IgG2 (CH1γ2), IgG3 (CH1γ3) or IgG4 (CH1γ4); the antibody obtained by such method, includes a) a light chain including the following amino acid sequences: i) the Light Chain Variable Region (LCVR) specific from an antigen; and ii) a human kappa (κ) Constant (CL) domain; and b) a heavy chain including the following amino acid sequences: i) the Heavy Chain Variable Region (HCVR) specific from the antigen; ii) the CH2 and CH3 domains from a human IgG1; and iii) the CH1 domain from a human IgG1, mutated to restore pairing between CH1 and CL domains.

Disclosed is a procalcitonin (PCT) detection kit, which comprises a magnetic particle separation reagent, a PCT detection antibody, an enzyme conjugate, a photogenic substrate, a PCT standard substance, and an enzyme diluent for diluting the enzyme conjugate. The magnetic particle separation reagent contains a magnetic particle coupled protein molecule, which is anti-rat human immunoglobulin G; the PCT detection antibody is an anti-rat IgG antibody; and the enzyme conjugate anti-rat human IgG labeled by horse radish peroxidase. According to the invention, an indirect coating mode that anti-rat human immunoglobulin G is coupled with magnetic particles, and a PCT monoclonal antibody combines with the anti-rat human immunoglobulin G is adopted. Through such mode, the dosage of the PCT monoclonal antibody is lowered, so that cost is reduced. The detection sensitivity is obviously improved by adding the concentration of anti-rat human immunoglobulin G of coupled magnetic particles.

The invention belongs to the field of electrochemical biosensors, and particularly relates to a preparation method of an anti-pollution electrochemical biosensor based on temperature-sensitive westernblot gel. The preparation method comprises the following steps: polishing a glassy carbon electrode in an alumina suspension, carrying out ultrasonic treatment, and washing with ethanol and water insequence; respectively weighing acrylamide, N, N-methylene diacrylamide, ammonium persulfate, isopropyl acrylamide, transferrin or human immunoglobulin G and tetramethylethylenediamine, and uniformlydispersing in a phosphoric acid buffer solution to obtain a mixed solution; dropwise adding the prepared mixed solution to the surface of the pretreated GCE, carrying out free radical polymerization reaction in a nitrogen environment, and washing the surface of the electrode with water. The prepared biosensor is excellent in anti-pollution performance, and the anti-pollution performance is improved by 1-3 times; the detection sensitivity is high; the preparation method is simple and easy to operate.

The invention provides a hydrophobic cyclic peptide ligand capable of being used for separating and purifying human immunoglobulin G. The hydrophobic cyclic peptide ligand is obtained through a computer simulation bionic design method, and the bionic design method takes an amino acid sequence Ser383-Asn389 on a CH3 binding region on a SpA and hIgG-Fc fragment as a simulation system. Hydrophobic cyclic peptide ligands which can be specifically combined with hIgG are determined through LeDock molecular docking, FlexX molecular docking and Amber molecular dynamics simulation screening, and the cyclic peptide ligand chromatographic medium is adopted to perform purification research on hIgG from a human serum sample, so that purity as high as 96% and recovery rate as high as 92% can be obtained; the hydrophobic cyclic peptide ligand sequence is -[HWG-C-AKTE]-, -[YF-C-WRHE]-, [-WV-C-LHHYF]-, -[PYF-C-TIE]- and -[FY-C-DEHL]-, wherein the peptide ligand with the best effect is -[HWG-C-AKTE]-.