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Artykuły w czasopismach na temat „Recombinant human antibodies”

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Data publikacji: 2 czerwca 2025

Data aktualizacji: 31 lipca 2025

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1

Fuchs, P., S. Dübel, F. Breitling, M. Braunagel, I. Klewinghaus, and M. Little. "Recombinant human monoclonal antibodies." Cell Biophysics 21, no. 1-3 (1992): 81–91. http://dx.doi.org/10.1007/bf02789480.

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Matthews, Ruth C., and James P. Burnie. "Human recombinant antibodies and immunotherapy." FEMS Immunology and Medical Microbiology 9, no. 1 (1994): 1–6. http://dx.doi.org/10.1111/j.1574-695x.1994.tb00466.x.

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DUAN, Tao, Xiao-Fang WANG, Shu-Yuan XIAO, Shu-Yan GU, and Mi-Fang LIANG. "Recombinant Human IgG antibodies against Human Cytomegalovirus." Biomedical and Environmental Sciences 21, no. 5 (2008): 372–80. http://dx.doi.org/10.1016/s0895-3988(08)60057-4.

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Mazov, A. V. ,. "GENERATION AND CHARACTERIZATION OF POLYCLONAL ANTIBODIES SPECIFIC TO HUMAN ESTROGEN RECEPTOR ERα". Biotechnologia Acta 17, № 3 (2024): 59–65. http://dx.doi.org/10.15407/biotech17.03.059.

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Aim. The purpose of the study was to generate and characterize anti-hERα polyclonal antibodies for elucidation of functional relationships between isoforms of estrogen receptor ERα and isoforms of ribosomal protein S6 kinase — S6K1. Methods. cDNA cloning. Expression of recombinant proteins in bacterial system. Affinity purification of His-tag fused recombinant proteins using Ni-NTA chromatography from bacterial lysates. Generation of polyclonal sera by mice immunization. Western blot analysis and immunoprecipitation. Results. cDNA coding for full length hERα was cloned into expression vector p

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5

GRIPPO, VANINA, LETICIA L. NIBORSKI, KARINA A. GOMEZ та MARIANO J. LEVIN. "Human recombinant antibodies againstTrypanosoma cruziribosomal P2βprotein". Parasitology 138, № 6 (2011): 736–47. http://dx.doi.org/10.1017/s0031182011000175.

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SUMMARYPatients with chronic Chagas' Heart Disease (cChHD) develop an antibody response that is suspected to be involved in the cardiac pathogenesis. The response againstTrypanosoma cruziribosomal P proteins is of particular interest, as these antibodies can cross-react with host cardiac receptors causing electrophysiological alterations. To better understand the humoral anti-P response we constructed a single-chain variable fragment library derived from a cChHD patient. The variable heavy and light regions were amplified from bone-marrow RNA and subcloned into the vector pComb3X. The phage li

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6

de Kruif, J., A.-R. van der Vuurst de Vries, L. Clienti, E. Boel, T. Logtenberg, and W. van Ewijk. "New perspectives on recombinant human antibodies." Immunology Today 17, no. 10 (1996): 453–55. http://dx.doi.org/10.1016/0167-5699(96)30057-y.

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Naranjo, Leslie, Fortunato Ferrara, Nicolas Blanchard, et al. "Recombinant Antibodies against Mycolactone." Toxins 11, no. 6 (2019): 346. http://dx.doi.org/10.3390/toxins11060346.

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In the past, it has proved challenging to generate antibodies against mycolactone, the primary lipidic toxin A of Mycobacterium ulcerans causing Buruli ulcer, due to its immunosuppressive properties. Here we show that in vitro display, comprising both phage and yeast display, can be used to select antibodies recognizing mycolactone from a large human naïve phage antibody library. Ten different antibodies were isolated, and hundreds more identified by next generation sequencing. These results indicate the value of in vitro display methods to generate antibodies against difficult antigenic targe

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8

PARIS, N., R. ROBERT, and L. MERCIER. "Monoclonal Antibodies Against Methionyl Recombinant Human Prolactin." Hybridoma 12, no. 1 (1993): 107–13. http://dx.doi.org/10.1089/hyb.1993.12.107.

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Maruyama, Toshiaki, Paul W. H. I. Parren, Anthony Sanchez, et al. "Recombinant Human Monoclonal Antibodies to Ebola Virus." Journal of Infectious Diseases 179, s1 (1999): S235—S239. http://dx.doi.org/10.1086/514280.

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Maruyama, Toshiaki, Paul W. H. I. Parren, Anthony Sanchez, et al. "Recombinant Human Monoclonal Antibodies to Ebola Virus." Journal of Infectious Diseases 179, s1 (1999): S235—S239. https://doi.org/10.5281/zenodo.13446571.

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Maruyama, Toshiaki, Paul W. H. I. Parren, Anthony Sanchez, et al. "Recombinant Human Monoclonal Antibodies to Ebola Virus." Journal of Infectious Diseases 179, s1 (1999): S235—S239. https://doi.org/10.5281/zenodo.13446571.

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12

Maruyama, Toshiaki, Paul W. H. I. Parren, Anthony Sanchez, et al. "Recombinant Human Monoclonal Antibodies to Ebola Virus." Journal of Infectious Diseases 179, s1 (1999): S235—S239. https://doi.org/10.5281/zenodo.13446571.

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13

Maruyama, Toshiaki, Paul W. H. I. Parren, Anthony Sanchez, et al. "Recombinant Human Monoclonal Antibodies to Ebola Virus." Journal of Infectious Diseases 179, s1 (1999): S235—S239. https://doi.org/10.5281/zenodo.13446571.

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14

Maruyama, Toshiaki, Paul W. H. I. Parren, Anthony Sanchez, et al. "Recombinant Human Monoclonal Antibodies to Ebola Virus." Journal of Infectious Diseases 179, s1 (1999): S235—S239. https://doi.org/10.5281/zenodo.13446571.

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Poryazova, Rada, Ginka Cholakova, Alexandra Kapogianni, and Ivanka Tsacheva. "Selection of high-affinity single-chain antibodies to human C3 by phage display." Pharmacia 72 (May 22, 2025): 1–8. https://doi.org/10.3897/pharmacia.72.e150821.

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C3 is the key protein in the activation of the complement system, and it contributes to an effective immune response. However, C3 is also targeted by autoantibodies during the development of autoimmune diseases such as systemic lupus erythematosus, and the autoantigenicity of C3 is still poorly understood. In order to study the molecular aspects of C3 autoantigenicity and the localization of C3 autoepitopes, we selected high-affinity anti-C3 antibodies from the "Griffin 1" phage display library expressing human scFv antibodies. The rounds of phage selection were performed with a gradual decrea

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16

Dechant, Michael, Thomas Beyer, Stefan Lohse, et al. "Recombinant Chimeric IgA1 and IgA2 Antibodies for Tumor Immunotherapy." Blood 110, no. 11 (2007): 4892. http://dx.doi.org/10.1182/blood.v110.11.4892.4892.

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Abstract The therapeutic potential of human IgA antibodies has hardly been explored, although IgA is the most abundantly produced antibody isotype in humans. Here, we describe the generation and functional characterization of human/mouse chimeric IgA antibodies against the epidermal growth factor receptor (EGF-R), which is a validated target antigen for tumor immunotherapy. Human IgG1, IgA1 and IgA2 variants of the C225 antibody were produced in CHO-K1 transfectomas using serum-free, non-adherent culture conditions. Productivity rates of selected IgA producing clones were approximately 5 pg/ce

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17

Sedova, E. S., D. N. Shcherbinin, A. S. Bandelyuk, et al. "Method for obtaining recombinant antibodies produced by a cell line transduced with recombinant adenoviruses." Fine Chemical Technologies 18, no. 1 (2023): 48–64. http://dx.doi.org/10.32362/2410-6593-2023-18-1-48-64.

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Objectives. To develop a technology for obtaining recombinant antibodies in a suspension culture of human HEK293 cells using transduction with recombinant adenovirus serotype 5 (rAd5) carrying genes expressing heavy and light chains of antibodies on the example of two broadspectrum anti-influenza antibodies 27F3 and CR9114.Methods. Ad5-27F3-H, Ad5-CR9114-H, and Ad5-27F3-L recombinant adenoviruses carrying the 27F3 antibody heavy chain gene, CR9114 antibody heavy chain gene, and 27F3 light chain gene, respectively, were generated using the AdEasy™ Adenoviral vector system. To accumulate prepara

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18

Corre, Jean-Philippe, Michèle Février, Jacques Thèze, Moncef Zouali, and Sophie Chamaret. "Anti-idiotypic antibodies to human anti-gp120 antibodies bind recombinant and cellular human CD4." European Journal of Immunology 21, no. 3 (1991): 743–51. http://dx.doi.org/10.1002/eji.1830210330.

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19

Krebs, Barbara, Heather Griffin, Greg Winter, and Stefan Rose-John. "Recombinant Human Single Chain Fv Antibodies Recognizing Human Interleukin-6." Journal of Biological Chemistry 273, no. 5 (1998): 2858–65. http://dx.doi.org/10.1074/jbc.273.5.2858.

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LUSHER, JEANNE M. "Human Antibodies to Recombinant Factor VIII in Hemophiliacs." Journal of Interferon Research 14, no. 4 (1994): 173–74. http://dx.doi.org/10.1089/jir.1994.14.173.

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21

Vola, Roberto, Anna Rivella, Andrew M. Creighton, et al. "Recombinant Anti-Human Melanoma Antibodies Are Versatile Molecules." Journal of Investigative Dermatology 107, no. 2 (1996): 164–70. http://dx.doi.org/10.1111/1523-1747.ep12329566.

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22

Dübel, Stefan, Oda Stoevesandt, Michael J. Taussig, and Michael Hust. "Generating recombinant antibodies to the complete human proteome." Trends in Biotechnology 28, no. 7 (2010): 333–39. http://dx.doi.org/10.1016/j.tibtech.2010.05.001.

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23

Lau, Corinna, Kristin S. Gunnarsen, Lene S. S. Høydahl, et al. "Recombinant anti-human and anti-porcine CD14 antibodies." Immunobiology 217, no. 11 (2012): 1197–98. http://dx.doi.org/10.1016/j.imbio.2012.08.196.

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Misao Ide, Kazue Kaneda, Kenzo Koizumi, et al. "Neutralizing monoclonal antibodies against recombinant human interleukin-2." Journal of Immunological Methods 101, no. 1 (1987): 57–62. http://dx.doi.org/10.1016/0022-1759(87)90216-x.

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Bregenholt, Søren, and John Haurum. "Pathogen-specific recombinant human polyclonal antibodies: biodefence applications." Expert Opinion on Biological Therapy 4, no. 3 (2004): 387–96. http://dx.doi.org/10.1517/14712598.4.3.387.

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26

Nielsen, Lars S., Alexandra Baer, Christian Müller, et al. "Single-Batch Production of Recombinant Human Polyclonal Antibodies." Molecular Biotechnology 45, no. 3 (2010): 257–66. http://dx.doi.org/10.1007/s12033-010-9270-9.

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Adish, Zh B., M. Nurtleu, K. A. Tursunov, K. N. Mukantayev, Y. M. Ramankulov, and K. K. Mukanov. "Obtaining and investigating immunochemical properties of monoclonal antibodies against rCTLA-4 protein." BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 142, no. 1 (2023): 57–67. http://dx.doi.org/10.32523/2616-7034-2023-142-1-57-67.

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Monoclonal antibodies are used to block control points of the tumor development of many oncological pathologies. One of the critical control points of tumor development of several oncological pathologies is the receptor for cytotoxic T-lymphocyte-associated protein 4 (CTLA-4). Monoclonal antibodies against the CTLA-4 receptor are laboratory-derived humanized antibodies. An essential step in the humanization of antibodies is the production of murine hybrid cells producing monoclonal antibodies. This article describes studies of mice monoclonal antibodies against a recombinant human CTLA-4 recep

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Kojic, Snezana, Elisa Medeot, and Georgine Faulkner. "Characterization of antibodies directed against the Ankrd2 human muscle protein." Archives of Biological Sciences 61, no. 4 (2009): 683–91. http://dx.doi.org/10.2298/abs0904683k.

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In order to study the function of the Ankrd2 protein, for which commercial antibodies are not available, we report the production and analysis of polyclonal antibodies to full-length Ankrd2 and its C-terminal and N-terminal regions, as well as a monoclonal antibody to the C-terminus of the protein. Epitope mapping making use of recombinant deletion mutants showed that an epitope located in region 323-333 aa of Ankrd2 is detected by the monoclonal antibody. The high specificity of all four anti-Ankrd2 antibodies for recombinant and endogenous Ankrd2 protein is also demon?strated.

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29

Higo-Moriguchi, Kyoko, Yasushi Akahori, Yoshitaka Iba, Yoshikazu Kurosawa, and Koki Taniguchi. "Isolation of Human Monoclonal Antibodies That Neutralize Human Rotavirus." Journal of Virology 78, no. 7 (2004): 3325–32. http://dx.doi.org/10.1128/jvi.78.7.3325-3332.2004.

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ABSTRACT A human antibody library constructed by utilizing a phage display system was used for the isolation of human antibodies with neutralizing activity specific for human rotavirus. In the library, the Fab form of an antibody fused to truncated cp3 is expressed on the phage surface. Purified virions of strain KU (G1 serotype and P[8] genotype) were used as antigen. Twelve different clones were isolated. Based on their amino acid sequences, they were classified into three groups. Three representative clones—1-2H, 2-3E, and 2-11G—were characterized. Enzyme-linked immunosorbent assay with vir

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Kudryashova, A. M., L. N. Nesterenko, G. A. Generalova, T. Yu Abasheeva, N. A. Mikhailova, and O. V. Borisova. "Characteristics of erythropoietin antibodies in patients treated with recombinant human erythropoietin." Medical Immunology (Russia) 22, no. 1 (2020): 143–52. http://dx.doi.org/10.15789/1563-0625-coe-1879.

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Our aim was to characterize anti-EPO antibodies in serum samples of the patients treated with erythropoietin. 106 serum samples from the patients treated with erythropoietin (EPO) were collected and assayed. 134 serum samples of patients who did not receive EPO were taken for comparative analysis. The anti-EPO antibody detection was performed in ELISA test with rhEPO, by passive capture on ELISA plates, using steptavidin-biotin immunochemical system. Mouse monoclonal antibodies to human IgG, IgG1, IgG2, IgG3 and IgG4 conjugated to horseradish peroxidase were used to detect anti-EPO antibodies,

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Yanuartono, Yanuartono, Hary Purnamaningsih, Alfarisa Nururrozi, Soedarmanto Indarjulianto, and Slamet Raharjo. "Recombinant Human Erythropoietin: Manfaat dalam Bidang Kedokteran." Jurnal Sain Veteriner 37, no. 1 (2019): 49. http://dx.doi.org/10.22146/jsv.48516.

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Recombinant human erythropoietin (rhEPO) is one of the biotechnology-based drugs that are needed by the human medicine and has also been used in the veterinary medicine. Currently RhEPO has been widely used in the world of human medicine for the treatment of anaemia caused by renal failure, cancer, chronic inflammation and AIDS. In veterinary medicine, although there is still not much data on its achievements, rhEPO has also been used for cases of chronic renal failure in dogs and cats. However, since rhEPO is not identical to feline EPO and canine EPO, some patients eventually produce antibod

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Nejatollahi, Foroogh, Samantha J. Hodgetts, Pamela J. Vallely, and James P. Burnie. "Neutralising human recombinant antibodies to human cytomegalovirus glycoproteins gB and gH." FEMS Immunology & Medical Microbiology 34, no. 3 (2002): 237–44. http://dx.doi.org/10.1111/j.1574-695x.2002.tb00630.x.

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Finashutina, Yu P., A. V. Misyurin, T. V. Akhlynina, et al. "PRODUCTION OF PURIFIED HUMAN RECOMBINANT ANTIGEN PRAME AND SPECIFIC MONOCLONAL ANTIBODIES." Russian Journal of Biotherapy 14, no. 3 (2015): 29–36. http://dx.doi.org/10.17650/1726-9784-2015-14-3-29-36.

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Tumor antigens recognized by CTLs have been identified several years ago and are major targets for creating anticancer vaccines. PRAME is an antigen which is highly expressed in various malignant tumors including melanomas and hematopoietic malignancies such as acute and chronic leukemias (AML, CML). Technology for producing recombinant antigen PRAME is based on creating a bacterial producer strain containing cDNA of human PRAME gene. We have obtained two producers of recombinant PRAME protein and its N-half, the synthesis of the target protein in the producers occurs in the inclusion bodies.

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Moreau, Emmanuel, Johan Hoebeke, Daniel Zagury, Sylviane Muller, and Claude Desgranges. "Generation and Characterization of Neutralizing Human Monoclonal Antibodies against Human Immunodeficiency Virus Type 1 Tat Antigen." Journal of Virology 78, no. 7 (2004): 3792–96. http://dx.doi.org/10.1128/jvi.78.7.3792-3796.2004.

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ABSTRACT The human immunodeficiency virus Tat regulatory protein is essential for virus replication and pathogenesis. From human peripheral blood mononuclear cells of three Tat toxoid-immunized volunteers, we isolated five Tat-specific human monoclonal antibodies (HMAbs): two full-length immunoglobulin G (IgG) antibodies and three single-chain fragment-variable (scFv) antibodies. The two IgGs were mapped to distinct epitopes within the basic region of Tat, and the three scFvs were mapped to the N-terminal domain of Tat. The three scFvs were highly reactive with recombinant Tat in Western blott

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35

Yaar, M., A. V. Palleroni, and B. A. Gilchrest. "Normal human epidermis contains an interferon-like protein." Journal of Cell Biology 103, no. 4 (1986): 1349–54. http://dx.doi.org/10.1083/jcb.103.4.1349.

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Interferons have been postulated to participate in growth regulation of normal body tissues and are known to inhibit growth of human epidermal keratinocytes in vitro. Polyclonal antibodies to recombinant human interferon-alpha, purified by passage over an affinity column (Sepharose coupled to the recombinant interferon), used in the indirect immunofluorescent method specifically stained the proliferative (basal) compartment of human epidermis in histological cross-sections of normal skin and in cultured keratinocyte colonies. Extracts prepared from healthy nonvirally infected keratinocyte cult

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Braren, Ingke, Simon Blank, Henning Seismann, et al. "Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries." Clinical Chemistry 53, no. 5 (2007): 837–44. http://dx.doi.org/10.1373/clinchem.2006.078360.

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Abstract Background: Allergen-specific IgE and IgG antibodies play pivotal roles in the induction and progression of allergic hypersensitivity reactions. Consequently, monoclonal human IgE and IgG4 antibodies with defined specificity for allergens should be useful in allergy research and diagnostic tests. We used combinatorial antibody libraries and subsequent recombinant production to make and assess IgE, IgG1, and IgG4 allergen-specific antibodies. Methods: We used phage display to select a synthetic single-chain antibody fragment (scFv) library against 3 different allergens, from bee venom,

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Oliinyk, O. S. "Recombinant single chain variable fragment antibodies (scFv) against Pro(144)-Leu(155) fragment of human protein C." Ukrainian Biochemical Journal 87, no. 2 (2015): 88–94. http://dx.doi.org/10.15407/ubj87.02.088.

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Williamson, Peter, and Ruth Matthews. "Development of neutralising human recombinant antibodies to pertussis toxin." FEMS Immunology & Medical Microbiology 23, no. 4 (1999): 313–19. http://dx.doi.org/10.1111/j.1574-695x.1999.tb01253.x.

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Lofgren, James A., Ralph Schwall, Charles Schmelzer, and Wai Lee T. Wong. "Generation of Polyclonal Antibodies Against Recombinant Human Activin a." Journal of Immunoassay 12, no. 4 (1991): 565–78. http://dx.doi.org/10.1080/01971529108053280.

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Fuchs, Manon, Susanne Kämpfer, Saskia Helmsing, et al. "Novel human recombinant antibodies against Mycobacterium tuberculosis antigen 85B." BMC Biotechnology 14, no. 1 (2014): 68. http://dx.doi.org/10.1186/1472-6750-14-68.

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Krebs, Barbara, Robert Rauchenberger, Silke Reiffert, et al. "High-throughput generation and engineering of recombinant human antibodies." Journal of Immunological Methods 254, no. 1-2 (2001): 67–84. http://dx.doi.org/10.1016/s0022-1759(01)00398-2.

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Williamson, P. "Development of neutralising human recombinant antibodies to pertussis toxin." FEMS Immunology and Medical Microbiology 23, no. 4 (1999): 313–19. http://dx.doi.org/10.1016/s0928-8244(98)00151-5.

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Esposito, G., V. Morea, E. Scarselli, et al. "Recombinant human antibodies specific for hepatitis C virus proteins." Archives of Virology 142, no. 3 (1997): 601–10. http://dx.doi.org/10.1007/s007050050106.

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Koch, Joachim, Mifang Liang, Iris Queitsch, Annette A. Kraus, and Ekkehard K. F. Bautz. "Human recombinant neutralizing antibodies against hantaan virus G2 protein." Virology 308, no. 1 (2003): 64–73. http://dx.doi.org/10.1016/s0042-6822(02)00094-6.

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Bemani, Peyman, Setareh Moazen, Elham Nadimi, and Foroogh Nejatollahi. "Development of Human Recombinant Antibodies Against ROR1 Tumor Antigen." Reports of Biochemistry and Molecular Biology 11, no. 2 (2022): 282–88. https://doi.org/10.61186/rbmb.11.2.282.

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Hackett, John, Jane Hoff-Velk, Alan Golden, et al. "Recombinant Mouse-Human Chimeric Antibodies as Calibrators in Immunoassays That Measure Antibodies toToxoplasma gondii." Journal of Clinical Microbiology 36, no. 5 (1998): 1277–84. http://dx.doi.org/10.1128/jcm.36.5.1277-1284.1998.

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In the present study, we examined the feasibility of using recombinant antibodies containing murine variable regions and human constant regions as calibrators or controls in immunoassays. As a model system, we chose the Abbott IMx Toxo immunoglobulin M (IgM) and Toxo IgG assays designed to detect antibodies to Toxoplasma gondii. Two mouse monoclonal antibodies were selected based on their reactivity to the T. gondii antigens P30 and P66. Heavy- and light-chain variable-region genes were cloned from both hybridomas and transferred into immunoglobulin expression vectors containing human kappa an

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47

Almeida, Raquel, Enzo Ardizzone, Laura Bindschedler, et al. "RB066 and RB067 recognize human CDKN2A-derived peptides by ELISA." Antibody Reports 7, no. 1 (2024): e1580. http://dx.doi.org/10.24450/journals/abrep.2024.e1580.

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Hammond, Philip, Christy Boozer, Mark Branum та ін. "Recombinant human antibodies to IFN-α from the immune repertoires of MG/thymoma donors (83.13)". Journal of Immunology 184, № 1_Supplement (2010): 83.13. http://dx.doi.org/10.4049/jimmunol.184.supp.83.13.

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Abstract A serum titer of autoantibodies to IFN-α has been reported in several autoimmune conditions and in many cases has been shown to neutralize IFN-α. The IFN-α antibody repertoire from 10 patients with autoimmune myasthenia gravis and associated thymoma (MG/T) was characterized. Surface IgG positive memory B-cells from peripheral blood mononuclear cells (PBMC) were cultured in 384-well plates to produce assayable quantities of antibody. Sensitive antibody microarray and AlphaScreen™ binding assays were used to identify antibodies reactive with IFN-α(2a). A range of IFN-α subtype specifici

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Bregenholt, Søren, Allan Jensen, Johan Lantto, Sara Hyldig, and John Haurum. "Recombinant Human Polyclonal Antibodies: A New Class of Therapeutic Antibodies Against Viral Infections." Current Pharmaceutical Design 12, no. 16 (2006): 2007–15. http://dx.doi.org/10.2174/138161206777442173.

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Tiran, Andreas, Rene A. Tio, Esther Oostenveld, et al. "Humoral Immune Response to Human Cytomegalovirus in Patients Undergoing Percutaneous Transluminal Coronary Angioplasty." Clinical Diagnostic Laboratory Immunology 6, no. 1 (1999): 45–49. http://dx.doi.org/10.1128/cdli.6.1.45-49.1999.

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ABSTRACT Possible causal relations between prior human cytomegalovirus (HCMV) infection and atherosclerosis and between HCMV reactivation and restenosis after coronary angioplasty have been suggested. We investigated patterns of antibodies directed to HCMV in 112 patients undergoing percutaneous transluminal coronary angioplasty (PTCA) and in a group of sex- and age-matched controls (blood donors without evidence of atherosclerosis). Levels of antibodies to HCMV were measured by enzyme-linked immunosorbent assay (ELISA) of serum samples drawn before and 5 weeks after PTCA. To further different

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