34 results about "Human immunoglobulin" patented technology

To provide a humanized rodent that expresses a heavy chain containing a VL domain. [Solution] A non-human animal, tissue, cell, and genetic material is provided which includes a modification of an endogenous non-human heavy chain immunoglobulin sequence and contains functional ADAM6 activity in a rodent (e.g., mouse), wherein the non-human animal rearranges the human immunoglobulin light chain gene segment in relation to the heavy chain constant domain and expresses an immunoglobulin-like molecule which contains a human immunoglobulin light chain variable domain fused to the heavy chain constant domain and is a cognitive of a human immunoglobulin light chain variable domain fused to the light chain constant domain.

The invention relates to an anti-ovarian antibody chemiluminiscence kit and a preparation method thereof. The kit comprises amino magnetic beads coated with anti-ovarian antibody recombinant protein, anti-human immune globulin labeled by alkaline phosphatase, an anti-ovarian antibody calibrator and a chemiluminiscence substrate. The method has the beneficial effects that the 7-day acceleration stability of the AOAb coated amino magnetic bead is improved to 95% or above, the signal-to-noise ratio is high, the correlation coefficient is greater than 0.999, the test repeatability CV is less than 3.5%, the reagent correlation and the magnetic bead stability can be better improved, and the test result is ensured to be accurate. By optimizing the amino magnetic bead cross-linking agent, 60 clinical samples are tested and compared with the result of a comparison manufacturer, the total coincidence rate is as high as 98%, and false positive can be effectively reduced. Meanwhile, a detection system is formed by matching with a Guilin superior chemiluminescence immunoassay analyzer IA-260, the testing amount per hour reaches 130 tests, and compared with a traditional colloidal gold immunochromatography method and a traditional enzyme-linked immunosorbent assay method, the detection speed is greatly increased, and the result optimization accuracy is greatly improved.

The application discloses a nanobody 3A2 for human adenovirus and a preparation method and application thereof, and belongs to the technical field of biotechnology, and particularly relates to a nanobody 3A2 for human adenovirus and a preparation method and application thereof. The nanobody or antigen-binding fragment containing the nanobody for targeting human adenovirus has three complementarity determining regions CDR1, CDR2 and CDR3; the amino acid sequence of CDR1 is SEQ ID No. 1, the amino acid sequence of CDR2 is SEQ ID No. 2, and the amino acid sequence of CDR3 is SEQ ID No. 3. The nanobody 3A2 is fused with an Fc segment (hFc) of human immunoglobulin to obtain a fusion protein, and the obtained h3A2-hFc can effectively inhibit infection of human adenovirus type 55, and the IC 50 is 0.62 nM.

Provided are human anti-thymocyte globulin (ATG) products, and methods of making and using the same. In particular, the disclosure provides an ungulate-derived polyclonal immunoglobulin, comprising a population of fully human or substantially human immunoglobulins. The population of fully human or substantially human immunoglobulins specifically binds human thymocytes, T cells, B cells, and / or monocytes. Such compositions may be made by immunization of transgenic animals having a human Ig locus with human thymocytes. This method generates polyclonal immunoglobulin with yield, purity, and antigen specificity that enable the use of this product in medical applications.

The application discloses a fusion protein ABD / Fc / IL-2, a coding gene thereof, a preparation method and application, and belongs to the field of biopharmaceuticals. The fusion protein ABD / Fc / IL-2 provided comprises a human serum albumin binding domain ABD, a full-length human immunoglobulin Fc segment and IL-2 or a mutant thereof. The fusion protein can effectively stimulate the proliferation of immune cells in the body, enhance the immunity of the body, and has high biological activity and a long plasma circulation half-life, or has high biological activity, a long plasma circulation half-life and low toxic side effects. The fusion protein can be used for preparing medicines for treating various diseases such as malignant tumors, infectious diseases and low immunity of the body, and can play an important role in the fields of medicine and biopharmaceuticals.

The present application relates to the technical field of biological medicine, and more particularly to a multifunctional antibody K1932 binding human CD19, CD3 and Fc gamma R, wherein the multifunctional antibody is composed of a bivalent Fab fragment specifically recognizing CD19 on the surface of B lymphocyte, a bivalent single-chain antibody recognizing CD3 molecule on the surface of T lymphocyte, and a human immunoglobulin Fc domain binding with Fc receptor, wherein the single-chain antibody recognizing CD3 molecule is connected with the C-terminal of Fab light chain through a connecting peptide Linker1, and the heavy chain and the light chain of the CD3 single-chain antibody are connected by a flexible Linker2; the biological macromolecule with the three functional domains is a highly directional immunotherapy drug, which is suitable for injection administration, can guide T cells to attack CD19-positive B lymphocytes, and the Fc domain is combined with Fc gamma R, so that the in-vivo half-life of the biological macromolecule is adjusted and the unnecessary influence on normal cells is reduced.

This invention relates to the field of irregular antibody detection technology, specifically to an automated washing microfluidic chip for irregular antibody detection. The chip includes a chip body, a membrane, and a detection component comprising a sample application chamber and a detection chamber arranged sequentially away from the center of rotation. The sample application chamber and the detection chamber are connected by a washing channel. The detection component is pre-filled with a washing solution that can fill the detection chamber and the washing channel under centrifugation. The washing solution contains anti-human immunoglobulin that reacts with erythrocyte antigen-antibody complexes. The specific gravity of the washing solution is configured to be greater than the specific gravity of the sample to be tested but less than the specific gravity of the erythrocyte antigen. This configuration solves the problems of cumbersome procedures, excessive time consumption, high operator dependence, and difficulty in standardization caused by multiple manual washing steps required in traditional test tube methods for detecting irregular antibodies. It effectively ensures detection sensitivity and accuracy and reduces the false negative rate.

The purpose of the present invention is to provide, as a platform technique that may serve as preparation for pandemics, a rapid antibody production technique in which a non-human animal having a human antibody gene is used. More specifically, the purpose of the present invention is to provide an immunization method with which it is possible to induce, in a short period of time, a high antigen-binding ability of an antibody or a high antibody titer of an antiserum, and a method for producing a human antibody / antiserum with which it is possible to rapidly produce a wide range of neutralizing antibodies.　(1) An immunization method for rapidly inducing a human monoclonal antibody having a high ability to bind to a desired antigen or a human polyclonal antibody having a high antibody titer, the method comprising a step for immunizing a non-human animal a plurality of times with a desired antigen or a nucleic acid encoding the antigen within 30 days from the first immunization, the non-human animal having a human antibody gene or locus, and the non-human animal being such that an endogenous gene or locus of the non-human animal corresponding to the human antibody gene or locus is disrupted or deleted, or mutated so as to result in a loss of expression or low expression. (2) A method for producing a human antibody against a desired antigen using a non-human animal, the method comprising: an immunization step for immunizing the non-human animal with the antigen or a nucleic acid encoding the antigen; a human immunoglobulin-positive B cell isolation step for isolating B cells that are human immunoglobulin-positive from a tissue of the immunized non-human animal; an antibody base sequence acquisition step for acquiring the base sequences of antibody light-chain mRNA-derived cDNA and antibody heavy-chain mRNA-derived cDNA prepared from the isolated B cells; and an antibody production step for producing an antibody on the basis of the acquired antibody base sequence, the non-h

The application discloses a nanobody 2C10 for human adenovirus and a preparation method and application thereof, and belongs to the technical field of biotechnology, and particularly relates to a nanobody 2C10 for human adenovirus and a preparation method and application thereof. The nanobody or antigen-binding fragment containing the nanobody for targeting human adenovirus has three complementarity determining regions CDR1, CDR2 and CDR3; the amino acid sequence of CDR1 is SEQ ID No. 1, the amino acid sequence of CDR2 is SEQ ID No. 2, and the amino acid sequence of CDR3 is SEQ ID No. 3. The nanobody 2C10 is fused with an Fc segment (hFc) of human immunoglobulin to obtain a fusion protein, and the obtained h2C10-hFc can effectively inhibit infection of human adenovirus type 55, and the IC 50 is 5.33 nM.

The invention discloses a technology for removing viruses from tetanus human immune globulin through a nano film. The process comprises the following steps: pretreating a feed liquid, so that the protein concentration of the feed liquid is 50-60g / L, the pH is 3.8-4.4, and the feed liquid contains 90-110g / L maltose and 50-150mmol / L sodium chloride; then, the feed liquid is subjected to two-stage filtration through a 0.1-micron nylon pre-filtration membrane bag with negative charges and a 20-nm regenerated cellulose (RC) virus removal membrane bag in sequence. According to the process, through optimizing the physical and chemical state of the feed liquid and the synergistic effect of the feed liquid and the functionalized filter membrane, the protein aggregation is effectively inhibited, the membrane pollution is reduced, the virus removal effect is ensured not to be lower than 4log10, the protein load of the RC membrane is remarkably improved to be more than 200L / m, and the product purity is more than or equal to 98%. The invention solves the technical problems of low flux and easy blockage of high-concentration immune globulin in small-aperture virus removal filtration, and is suitable for efficient, safe and large-scale production of blood products.

The invention belongs to the technical field of medical biology, and particularly relates to an EBV (Epstein-Barr Virus) neutralizing antibody-specifically-immune plasma high-throughput screening method and application thereof. EB virus envelope glycoprotein gp350 is selected as a screening target antigen, EBV specific plasma containing a high-titer EBV neutralizing antibody is rapidly screened in a high-throughput mode and used for preparing EBV specific human immune globulin, the titer of the EBV neutralizing antibody is obviously higher than that of listed intravenous gamma-C products, and the content of the EBV neutralizing antibody is about 4-8 times that of the EBV neutralizing antibody with the same concentration. The method provided by the invention can realize large-scale collection of EBV specific plasma through rapid high-throughput screening, reduces the workload of plasma screening, is suitable for large-scale production of EBV specific human immune globulin, and has a good application prospect.

This utility model relates to the technical field of human immunoglobulin preparation devices, and discloses a sampling device for preparing tetanus human immunoglobulin. It includes a sampling cylinder with a low-temperature storage mechanism on its outer wall and an automatic sampling mechanism. The low-temperature storage mechanism includes a first support ring, a supporting outer cylinder fixedly mounted at the bottom of the first support ring, and a second support ring fixedly mounted at the bottom of the supporting outer cylinder. Through the design of the low-temperature storage mechanism, this utility model can store a low-temperature medium in the cavity formed by the first support ring, the supporting outer cylinder, the second support ring, and the copper inner cylinder. The low-temperature medium can pass through the copper inner cylinder to cool the inner cavity of the sampling cylinder, thus achieving the function of low-temperature storage of the sample inside the sampling cylinder. This avoids the problem of sample deterioration during storage due to high ambient temperatures, ensuring the accuracy of biochemical analysis.

The present invention provides antibodies and antigen-binding fragments thereof that specifically bind human immunoglobulin E (IgE) with greater affinity at neutral pH than at acidic pH.

The invention discloses an application of Fc-Elabeta-32 in preparation of a medicine for treating sepsis, and also comprises a preparation method of the Fc-Elabeta-32, and the preparation method comprises the step of fusing an Fc structural domain of human immune globulin IgG with Ela-32 to generate the Fc-Ela-32. The application has the advantages that by preparing and using the Fc-Elabel-32, the survival rate of sepsis mice is remarkably increased in an experiment, the cardiac function is remarkably improved, meanwhile, the myocardial injury index is remarkably reduced, myocardial dysfunction caused by sepsis is relieved, and the Fc-Elabel-32 can be used as a potential treatment medicine for sepsis.

Provided are: an anti-agalactosylated human IgG antibody or an antibody fragment thereof; a method for measuring agalactosylated human IgG in a sample using the anti-agalactosylated human IgG antibody or the antibody fragment thereof; and a measurement reagent for measuring agalactosylated human IgG in a sample.

Provided are human anti-thymocyte globulin (ATG) products, and methods of making and using the same. In particular, the disclosure provides an ungulate-derived polyclonal immunoglobulin, comprising a population of fully human or substantially human immunoglobulins. The population of fully human or substantially human immunoglobulins specifically binds human thymocytes, T cells, B cells, and / or monocytes. Such compositions may be made by immunization of transgenic animals having a human Ig locus with human thymocytes. This method generates polyclonal immunoglobulin with yield, purity, and antigen specificity that enable the use of this product in medical applications.

The application discloses a nanobody 2C7 for human adenovirus and a preparation method and application thereof. The application belongs to the technical field of biotechnology and particularly relates to a nanobody 2C7 for human adenovirus and a preparation method and application thereof. The nanobody or antigen-binding fragment containing the nanobody for targeting human adenovirus has three complementarity determining regions CDR1, CDR2 and CDR3; the amino acid sequence of CDR1 is SEQ ID No. 1, the amino acid sequence of CDR2 is SEQ ID No. 2, and the amino acid sequence of CDR3 is SEQ ID No. 3. The nanobody 2C7 is fused with an Fc segment (hFc) of human immunoglobulin to obtain a fusion protein, and the obtained h2C7-hFc can effectively inhibit infection of human adenovirus type 55, and the IC 50 is 0.52 nM.

The invention relates to a human immunoglobulin product for intravenous injection, which is prepared by virus removal and filtration of a 20nm nano-film, and the nano-filtration protein load is more than 10kg / m < 2 >. The preparation method of the product comprises the following steps: after the intravenous injection human immune globulin stock solution is prepared and before 20nm nano-film virus removal filtration is carried out, adjusting the glycine content in the protein stock solution to 20g / L, adjusting the sodium acetate concentration to 20mmol / L, adjusting the protein content to 58g / L and adjusting the pH value to 4.1, and then carrying out 20nm nano-film virus removal filtration. According to the method disclosed by the invention, the nano-filtration protein load is effectively improved by more than 10kg / m < 2 > protein through the measures of optimizing a stabilizer in a stock solution before filtration of the human immunoglobulin nano-membrane for intravenous injection, adjusting the ionic strength and the like, so that the use efficiency of the nano-filtration membrane is improved, and meanwhile, the virus removal filtration process time of the nano-membrane is also shortened.

The present application relates to the technical field of pharmaceutical chemistry, in particular to a human immunoglobulin E antagonist, a screening method and application. The screening method comprises the following steps: taking IgE as a target, screening drug molecules capable of binding with IgE in a high-throughput FDA drug library; testing the antagonizing efficiency of the drug molecules screened in vitro, and screening molecules capable of antagonizing IgE according to the expected antagonizing efficiency. The present application takes IgE as a target, screens drug molecules capable of binding with IgE in a high-throughput FDA drug library, and verifies the antagonizing efficiency of the drug molecules at the molecular level in vitro, so that a molecule capable of antagonizing IgE is screened, and the antagonizing efficiency of the screened thioctic acid is significantly higher than that of common antagonists.

The invention provides a method for removing IgA (Immunoglobulin A) and IgM (Immunoglobulin M) in human immunoglobulin for intravenous injection. The method comprises the following steps: S1) dissolving plasma component II + III precipitates to obtain a dissolved solution; s2) precipitating and centrifuging the dissolved solution by adopting n-caprylic acid or sodium caprylate to obtain supernate; s3) performing anion exchange column chromatography on the supernate to obtain first flow-through liquid and first washing liquid; s4) mixing the first flow-through liquid with the first washing liquid to obtain a column chromatography collection liquid; s5) performing strong anion membrane chromatography on the column chromatography collection liquid to obtain second flow-through liquid and second washing liquid; s6) mixing the second flow-through liquid and the second washing liquid to obtain a membrane chromatography collection liquid, and S7) sequentially performing first concentration, dialysis, first sterilization, incubation, ultrafiltration and second sterilization on the membrane chromatography collection liquid to obtain the human immunoglobulin for intravenous injection without IgA and IgM. According to the method disclosed by the invention, the IgA and IgM removal efficiency is remarkably improved through a multi-stage purification process.

This invention provides a human anti-thymocyte globulin (ATG) product, as well as a method for producing and using the same. [Solution] This disclosure provides polyclonal immunoglobulins derived from ungulates having a population of fully human or substantially human immunoglobulins. The population of fully human or substantially human immunoglobulins specifically binds to human thymocytes, T cells, B cells, and / or monocytes. Such compositions can be produced by immunizing transgenic animals having the human Ig locus with human thymocytes. This method produces polyclonal immunoglobulins with yield, purity, and antigen specificity that enable the use of this product in medical applications.

The present application belongs to the technical field of blood product preparation, and particularly relates to a preparation method of intravenous human immunoglobulin, comprising the following steps which are sequentially performed: Cohn FIII supernatant is pretreated to obtain a sample I to be loaded; the sample I to be loaded is subjected to first anion exchange chromatography to obtain a first chromatography product; the first chromatography product is pretreated to obtain a sample II to be loaded; the sample II to be loaded is subjected to second anion exchange chromatography to obtain a second chromatography product; the second chromatography product is pretreated to obtain a sample III to be loaded; the sample III to be loaded is subjected to heparin affinity chromatography to obtain a third chromatography product; and the third chromatography product is configured into human immunoglobulin finished product. The technical scheme can solve the technical problems of the existing preparation method of intravenous human immunoglobulin, such as introduction of new materials, poor effect of impurity protein precipitation, high content of anti-A and anti-B, and the like, and has an ideal application prospect.

The invention relates to the technical field of biology, particularly discloses human immune globulin stock solution dry powder as well as a preparation method and application thereof, and belongs to the field of biological pharmacy. The method comprises the following steps: carrying out purification and virus inactivation treatment on an intermediate product containing human immune globulin to obtain a virus-inactivated human immune globulin stock solution; performing ultrafiltration concentration on the human immunoglobulin stock solution, and performing freeze drying to obtain human immunoglobulin stock solution dry powder; and redissolving the dry powder and preparing into a human immune globulin semi-finished product. Wherein the core of the freeze drying process is that a multi-stage gradient sublimation drying procedure is adopted. According to the method, the storage stability of the human immune globulin stock solution is remarkably improved, the effective storage period of the human immune globulin stock solution at the temperature of 2-8 DEG C is prolonged to 13 months or above, key quality indexes are excellent after freeze-dried powder is redissolved, and the technical problems that the storage period of the liquid stock solution is short, and production scheduling is not flexible are solved.

The present invention relates to a stable liquid formulation of a fusion protein having an Fc domain of human immunoglobulin G (IgG) (in particular, a protein in which a soluble extracellular domain of a vascular endothelial growth factor (VEGF) receptor and an Fc domain of human immunoglobulin G (IgG) are fused (e.g. Aflibercept)). The present invention also relates to a composition for stabilizing a protein in which a soluble extracellular domain of a VEGF receptor and an Fc domain of IgG are fused, and a method for stabilizing a protein in which a soluble extracellular domain of a VEGF receptor and an Fc domain of IgG are fused. The present invention can promote stabilization of physiological activity through a stable liquid formulation suitable for intravitreal injection of anti-VEGF-Fc fusion proteins including Aflibercept, and improve the therapeutic effect on various ophthalmic diseases caused by abnormal angiogenesis (e.g., retinal vein occlusion, diabetic macular edema, choroidal neovascularization, and wet age-related macular degeneration, etc.).

This invention discloses a method for preparing a fusion protein of sialic acid-binding immunoglobulin-like lectin 6 extracellular fragment and human immunoglobulin G1-Fc fragment, and its application, belonging to the field of biomedical technology. The fusion protein consists of a functional fragment of the Siglec-6 extracellular region linked to the Fc fragment of human IgG1 via a peptide linker. Its amino acid sequence is selected from one of SEQ ID No. 1, SEQ ID No. 2, or SEQ ID No. 3, or a variant with more than 90% homology to the above sequences and retaining the biological activity of Siglec-6. The preparation method includes: cloning the Siglec-6 fragment and the coding sequence of the Fc fragment, constructing a recombinant expression plasmid and transfecting it into mammalian cells to induce expression, and purifying the target protein by affinity chromatography. The fusion protein vcSig6-Fc of this invention has extremely high structural stability and ligand binding affinity, can significantly inhibit the expression of inflammatory factors and matrix-degrading enzymes in chondrocytes, and shows excellent performance in promoting COL2A1 expression, thus exhibiting good protective effects on articular cartilage and therapeutic effects on rheumatoid arthritis.

The present invention relates to the technical field of irregular antibody detection, particularly to an automatic washing microfluidic chip for irregular antibody detection, the automatic washing microfluidic chip comprises a chip main body and a film, and further comprises: a detection assembly, the detection assembly comprises a sample adding cavity and a detection cavity which are sequentially arranged away from a rotation center, and the sample adding cavity and the detection cavity are communicated through a washing flow channel, a washing solution capable of filling the detection cavity and the washing runner under the centrifugal action is preset in the detection assembly, the washing solution contains anti-human immune globulin which is subjected to immune reaction with a red blood cell antigen-antibody compound, and the specific gravity of the washing solution is configured to be larger than that of a sample to be detected and smaller than that of red blood cell antigens. The problems of tedious flow, too long time consumption, strong operator dependence and difficulty in standardization caused by multiple manual washing steps in the process of detecting irregular antibodies by a traditional test tube method are solved, the detection sensitivity and accuracy are effectively ensured, and the false negative rate is reduced.

The application provides a method for detecting ADCP activity of human immunoglobulin products in the field of infectious diseases, and belongs to the technical field of immunological detection. The method comprises the steps of target cell screening, effector-target ratio optimization, and test product concentration gradient optimization, and provides an accurate and intuitive biological activity detection method for antibody-dependent cell-mediated phagocytosis of immunoglobulin products, so that accurate detection of the biological activity of antibody-dependent cell-mediated phagocytosis of human immunoglobulin products is realized. The detection method is intuitive, precise and accurate, fills the blank of the detection of antibody-dependent cell-mediated phagocytosis of human immunoglobulin products, and has important significance for improving the quality control and clinical application of human immunoglobulin products.

The present invention provides antibodies and antigen-binding fragments thereof that specifically bind human immunoglobulin E (IgE) with greater affinity at neutral pH than at acidic pH.

The present application relates to a kind of from IgG chromatography waste material preparation rich in IgA and IgM human immunoglobulin, belong to the technical field of blood products.The method comprises the following steps: (1) Fractogel EMD TMAE anion exchange chromatography eluate is treated with ultrafiltration;(2) the filtrate obtained after ultrafiltration is subjected to affinity chromatography, and eluate is collected;(3) the eluate obtained in step (2) is subjected to ultrafiltration after ultrafiltration, and is subjected to pasteurization inactivation;(4) ultrafiltration and preparation are carried out according to specified concentration;(5) sterile filtration, dispensing, obtain finished product.The present application uses waste eluate as raw material, and rich in IgA and IgM human immunoglobulin can be obtained after ultrafiltration by one-step affinity chromatography.The prepared immunoglobulin contains IgM 19%-25%, IgA 15%-20%, IgG 55%-66%, and the purity can reach more than 95%.

The utility model belongs to the technical field of sampling for preparation of immune globulin, and particularly relates to a sampling device for preparation of rabies human immune globulin, which comprises a sampling tank, a storage tank arranged in the sampling tank, a limit ring fixedly mounted on the inner wall of the storage tank, a mounting rack arranged at the top of the limit ring, a filter screen fixedly mounted in the mounting rack, and a filter screen arranged in the filter screen. A limiting rod is fixedly mounted on the top of the mounting frame and located on one side of the filter screen, an inserting groove is formed in the top of the sampling tank and located on one side of the limiting rod, one end of the limiting rod extends into the inserting groove, and limiting blocks are symmetrically and fixedly mounted on the inner wall of the inserting groove and located on the top of the limiting rod. The feeding pipe is fixedly installed on one side of the sampling tank and located above the filtering net, the filtering net can be conveniently taken out by a worker to be cleaned and disinfected, operation is easy, fast and convenient, the feeding pipe can be conveniently disassembled and installed by the worker, and the situation that impurities left in the feeding pipe affect next sampling preparation is avoided.