Journal articles: 'Recombinant monoclonal antibody'

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Siegel, D. L. "Recombinant monoclonal antibody technology." Transfusion Clinique et Biologique 9, no. 1 (January 2002): 15–22. http://dx.doi.org/10.1016/s1246-7820(01)00210-5.

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Liu, Hongcheng, Georgeen Gaza-Bulseco, and Chris Chumsae. "Glutamine deamidation of a recombinant monoclonal antibody." Rapid Communications in Mass Spectrometry 22, no. 24 (December 30, 2008): 4081–88. http://dx.doi.org/10.1002/rcm.3831.

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Eltarhoni, Khadiga, Faddy Kamel, Katrina Ihebunezie, Pasha Nisar, and Mikhail Soloviev. "Therapeutic Antibodies in Cancer Treatment in the UK." International Journal of Molecular Sciences 23, no. 23 (November 23, 2022): 14589. http://dx.doi.org/10.3390/ijms232314589.

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The growing understanding of the molecular mechanisms of carcinogenesis accelerated the development of monoclonal therapeutic antibodies to specifically target multiple cancer pathways. Recombinant protein therapeutics now constitute a large proportion of yearly approved medicines. Oncology, autoimmune diseases and to a smaller degree the prophylaxis of organ transplant rejection are their main application areas. As of the date of this review, 37 monoclonal antibody products are approved for use in cancer treatments in the United Kingdom. Currently, the antibody therapeutics market is dominated by monoclonal immunoglobulins (IgGs). New types of recombinant antibody therapeutics developed more recently include bispecific recombinant antibodies and other recombinantly produced functional proteins. This review focuses on the approved therapeutic antibodies used in cancer treatment in the UK today and describes their antigen targets and molecular mechanisms involved. We provide convenient links to the relevant databases and other relevant resources for all antigens and antibodies mentioned. This review provides a comprehensive summary of the different monoclonal antibodies that are currently in clinical use primarily in malignancy, including their function, which is of importance to those in the medical field and allied specialties.

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Brichta, J., M. Hnilova, and T. Viskovic. "generation of hapten-specific recombinant antibodies: antibody phage display technology: a review." Veterinární Medicína 50, No. 6 (March 28, 2012): 231–52. http://dx.doi.org/10.17221/5620-vetmed.

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Production of antibodies has been revolutionized by the development of modern molecular biology methods for the expression of recombinant DNA. Phage display technology represents one of the most powerful tools for production and selection of recombinant antibodies and has been recognized as a valuable alternative way for the preparation of antibodies of a desired specificity. In comparison to poly- and monoclonal antibodies, recombinant antibodies using the phage display technology can be prepared faster, in more automatic process and with reduced consumption of laboratory animals. This review summarizes current trends of phage display technology with focus on the generation of hapten-specific recombinant antibodies and gives the examples of successful applications of phage display in the environmental analysis of low molecular weight compound.

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Lubkin, Margaret, Matthew Shallice, Julie Nyhus, Louis Leong, and Birte Aggeler. "Recombinant Rabbit Monoclonal Antibodies to Study Apoptosis and Apoptotic Pathways (132.4)." Journal of Immunology 184, no. 1_Supplement (April 1, 2010): 132.4. http://dx.doi.org/10.4049/jimmunol.184.supp.132.4.

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Abstract Flow cytometry a tool for studying apoptosis and apoptotic pathways. Using monoclonal antibodies for flow cytometry leads to high specificity for the detection of the target epitope of interest, limiting the use of flow cytometry to available mouse monoclonal antibodies. Here we present high quality recombinant rabbit monoclonal antibodies that do not rely on hybridoma cell lines, but are made with a proprietary recombinant technology to obtain cloned antibodies. These rabbit monoclonals were compared to other available antibodies to demonstrate high specificity and affinity to their targets. We examined lot-to-lot consistency using the same antibody for flow cytometry, western blot and immunocytochemistry. In this study two rabbit monoclonal antibodies involved in apoptotic pathways, Cleaved Caspase-3[Asp175] and p53[pS15] were examined. The p53 antibody is the phosphorylated form of p53 [pS15], which in turn induces p53 Upregulated Modulator of Apoptosis (PUMA), the result being apoptosis through mitochondrial degradation. We performed western blot, and immunocytochemistry studies to show high specificity for both antibodies as well as obtain spatial resolution within the cell.

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Boonham, N., and I. Barker. "Virus Strain Discrimination Using Recombinant Antibodies." Disease Markers 16, no. 1-2 (2000): 95–97. http://dx.doi.org/10.1155/2000/815852.

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Most routine testing for plant viruses is currently carried out using monoclonal and polyclonal antibodies. Traditional methods of antibody production however can be time consuming and require the use of expensive cell culture facilities. Recombinant antibody technology however is starting to make an impact in this area, enabling the selection of antibody fragments in a few weeks compared with the many months associated with traditional methods and requires only basic microbiological facilities. Single chain Fv antibody fragments (scFv) have been selected from a synthetic phage-antibody library by affinity selection with purifiedPotato virus Y, ordinary strain (PVYO). The scFv selected was specific for PVY and detected 7 out of 9 isolates of PVYOwhilst it did not detect 15 isolates from the closely related necrotic strains PVYNand PVYNTN. In ELISA the scFv could be used to detect virus at concentrations of 50 ng/ml in plant sap and was shown to have similar limits of detection as commercially available PVY monoclonal antibodies. These results highlight the potential of the technology for the selection of strain specific antibodies with an affinity and assay sensitivity similar to traditional monoclonal antibodies and their use in viral diagnostics.

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Ambrogelly, Alexandre, Stephen Gozo, Amit Katiyar, Shara Dellatore, Yune Kune, Ram Bhat, Joanne Sun, et al. "Analytical comparability study of recombinant monoclonal antibody therapeutics." mAbs 10, no. 4 (March 20, 2018): 513–38. http://dx.doi.org/10.1080/19420862.2018.1438797.

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Schrader, John W., and Gary R. McLean. "Multispecificity of a recombinant anti-ras monoclonal antibody." Journal of Molecular Recognition 31, no. 2 (November 8, 2017): e2683. http://dx.doi.org/10.1002/jmr.2683.

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Greunke, Kerstin, Edzard Spillner, Ingke Braren, Henning Seismann, Sabine Kainz, Ulrich Hahn, Thomas Grunwald, and Reinhard Bredehorst. "Bivalent monoclonal IgY antibody formats by conversion of recombinant antibody fragments." Journal of Biotechnology 124, no. 2 (July 2006): 446–56. http://dx.doi.org/10.1016/j.jbiotec.2005.12.032.

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Ewers, Helge. "Open-source recombinant monoclonal secondary nanobodies." Journal of Cell Biology 217, no. 3 (February 14, 2018): 809–11. http://dx.doi.org/10.1083/jcb.201802025.

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Secondary antibodies are everyday reagents in biomedical research that are generated in animals. In this issue, Pleiner et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201709115) describe several single domain antibody fragments against antibodies from mouse and rabbit, so-called nanobodies that are easily produced recombinantly, and characterize their use in Western blotting, enzyme-linked immunosorbent assay, and immunofluorescence assays.

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Gong, Siqi, Seijal Gautam, Joshua D. Coneglio, Hanna B. Scinto, and Ruth M. Ruprecht. "Antibody Light Chains: Key to Increased Monoclonal Antibody Yields in Expi293 Cells?" Antibodies 11, no. 2 (May 18, 2022): 37. http://dx.doi.org/10.3390/antib11020037.

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When constructing isogenic recombinant IgM–IgG pairs, we discovered that μ heavy chains strongly prefer partnering with λ light chains for optimal IgM expression in transiently cotransfected Expi293 cells. When μ chains were paired with κ light chains, IgM yields were low but increased by logs—up to 20,000 X—by using λ chains instead. Switching light chains did not alter epitope specificity. For dimeric IgA2, optimal expression involved pairing with λ chains, whereas light-chain preference varied for other immunoglobulin classes. In summary, recombinant IgM production can be drastically increased by using λ chains, an important finding in the use of IgM for mucosal immunoprophylaxis.

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Aki, Yuichi, Yuta Katsumata, Hirofumi Kakihara, Koichi Nonaka, and Kenshu Fujiwara. "4-(2,5-Dimethyl-1H-pyrrol-1-yl)-N-(2,5-dioxopyrrolidin-1-yl) benzamide improves monoclonal antibody production in a Chinese hamster ovary cell culture." PLOS ONE 16, no. 4 (April 22, 2021): e0250416. http://dx.doi.org/10.1371/journal.pone.0250416.

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There is a continuous demand to improve monoclonal antibody production for medication supply and medical cost reduction. For over 20 years, recombinant Chinese hamster ovary cells have been used as a host in monoclonal antibody production due to robustness, high productivity and ability to produce proteins with ideal glycans. Chemical compounds, such as dimethyl sulfoxide, lithium chloride, and butyric acid, have been shown to improve monoclonal antibody production in mammalian cell cultures. In this study, we aimed to discover new chemical compounds that can improve cell-specific antibody production in recombinant Chinese hamster ovary cells. Out of the 23,227 chemicals screened in this study, 4-(2,5-dimethyl-1H-pyrrol-1-yl)-N-(2,5-dioxopyrrolidin-1-yl) benzamide was found to increase monoclonal antibody production. The compound suppressed cell growth and increased both cell-specific glucose uptake rate and the amount of intracellular adenosine triphosphate during monoclonal antibody production. In addition, the compound also suppressed the galactosylation on a monoclonal antibody, which is a critical quality attribute of therapeutic monoclonal antibodies. Therefore, the compound might also be used to control the level of the galactosylation for the N-linked glycans. Further, the structure-activity relationship study revealed that 2,5-dimethylpyrrole was the most effective partial structure of 4-(2,5-dimethyl-1H-pyrrol-1-yl)-N-(2,5-dioxopyrrolidin-1-yl) benzamide on monoclonal antibody production. Further structural optimization of 2,5-dimethylpyrrole derivatives could lead to improved production and quality control of monoclonal antibodies.

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Zonneveld, Anton-Jan van, Harry Veerman, Just P. J. Brakenhoff, Lucien A. Aarden, Jean-Francois Cajot, and Hans Pannekoek. "Mapping of Epitopes on Human Tissue-Type Plasminogen Activator with Recombinant Deletion Mutant Proteins." Thrombosis and Haemostasis 57, no. 01 (1987): 082–86. http://dx.doi.org/10.1055/s-0038-1651067.

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SummaryAn antigen assay based on a monoclonal antibody directed against the light chain of tissue-type plasminogen activator (t-PA) was developed to quantify seven recombinant (r) t-PA deletion mutant proteins. These recombinant proteins were then employed to map different epitopes on t-PA which interact with a panel of twenty-three monoclonal anti-t-PA antibodies. Twenty were directed against domains on the heavy chain, two against the “finger” domain, three against the “epidermal growth factor-like” domain, five against the kringle 1 domain, and ten against the kringle 2 domain. Only three monoclonal anti-t-PA antibodies interact with the light chain. The finding that the epitopes of each of the monoclonals could be determined with the deletion mutant proteins supports the hypothesis of autonomous folding of structural domains and emphasizes the validity of the use of the recombinant t-PA-deletion mutant proteins for structure-function studies.

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Vancutsem, E., F. Echahidi, K. Van Geel, G. Muyldermans, O. Soetens, and A. Naessens. "Production of Recombinant Antigens of Ureaplasma parvum Serotypes 3 and 6 for Development of a Serological Assay." Clinical and Vaccine Immunology 15, no. 3 (December 19, 2007): 447–51. http://dx.doi.org/10.1128/cvi.00379-07.

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ABSTRACT Recombinant antigens of Ureaplasma parvum serotypes 3 and 6 were produced in order to develop a serological assay for Ureaplasma antibody detection. The genes of the multiple banded antigen (MBA) were amplified by PCR and cloned in a pTrcHis TOPO plasmid. Purified recombinant proteins were evaluated in Western blotting and enzyme-linked immunosorbent assay (ELISA) with monoclonal antibodies and human sera. Our approach was successful in the production of the recombinant MBAs (rMBAs) for serotypes 3 and 6. The antigens tested positive with serotype-specific monoclonal antibodies in Western blotting and in ELISA. Prominent reactions were detected with the rMBAs and their homologous monoclonal antibodies. Strong cross-reactions were visible in ELISA between rMBA 3 and the monoclonal antibodies from the other U. parvum serotypes. A weak cross-reaction was seen with rMBA 3 and the monoclonal antibody from serotype 4. rMBA 6 showed cross-reaction only with the monoclonal antibody from U. parvum serotype 1. Fifty-one percent of the sera obtained from culture-positive women reacted with one or both rMBAs. Only three (15%) of the sera from culture-negative women reacted with the rMBA. The positive reactions were observed only with rMBA 6. These preliminary tests showed the potential usefulness of the rMBAs produced for detecting an antibody response against Ureaplasma antigens.

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De Logu, Alessandro, R. Anthony Williamson, Roman Rozenshteyn, Fernando Ramiro-Ibañez, Cindy D. Simpson, Dennis R. Burton, and Pietro Paolo Sanna. "Characterization of a Type-Common Human Recombinant Monoclonal Antibody to Herpes Simplex Virus with High Therapeutic Potential." Journal of Clinical Microbiology 36, no. 11 (1998): 3198–204. http://dx.doi.org/10.1128/jcm.36.11.3198-3204.1998.

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We report the characterization of a type-common human recombinant monoclonal antibody previously isolated by antigen selection from a phage-displayed combinatorial antibody library established from a herpes simplex virus (HSV)-seropositive individual. Competition with well-characterized murine monoclonal antibodies and immunodetection of gD truncations revealed that this antibody recognizes the group Ib antigenic site of glycoprotein D, a highly conserved and protective type-common determinant. To our knowledge, this is the first human group Ib monoclonal antibody ever described. The antibody also displayed first-order neutralization kinetics and a high neutralization rate constant, was capable of completely inhibiting syncytium formation by a fusogenic strain of HSV type 1, and efficiently neutralized low-passage clinical isolates of both HSV serotypes. Taken together with our earlier observations of the in vivo antiviral activities of this human recombinant antibody in animal models of HSV infection, the present results support the high therapeutic potential of this antibody.

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Wang, Dongdong, Christine Nowak, Bruce Mason, Amit Katiyar, and Hongcheng Liu. "Analytical artifacts in characterization of recombinant monoclonal antibody therapeutics." Journal of Pharmaceutical and Biomedical Analysis 183 (May 2020): 113131. http://dx.doi.org/10.1016/j.jpba.2020.113131.

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Mayani, Mukesh, Carlos D. M. Filipe, Michael D. McLean, J. Christopher Hall, and Raja Ghosh. "Purification of transgenic tobacco-derived recombinant human monoclonal antibody." Biochemical Engineering Journal 72 (March 2013): 33–41. http://dx.doi.org/10.1016/j.bej.2012.12.007.

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Gaza-Bulseco, Georgeen, and Hongcheng Liu. "Fragmentation of a Recombinant Monoclonal Antibody at Various pH." Pharmaceutical Research 25, no. 8 (May 13, 2008): 1881–90. http://dx.doi.org/10.1007/s11095-008-9606-3.

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Kim, Eun-Jung, Gyu-Min Im, Chang-Soo Lee, Yun-Gon Kim, Byoung Joon Ko, Hee-Jin Jeong, and Byung-Gee Kim. "Generation of Monoclonal Antibodies for Sensitive Detection of Pro-Inflammatory Protein S100A9." Applied Sciences 11, no. 10 (May 19, 2021): 4659. http://dx.doi.org/10.3390/app11104659.

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The calcium-binding protein S100A9 regulates inflammatory processes and the immune response. It is overexpressed in a variety of inflammatory and oncologic conditions. In this study, we produced a recombinant human S100A9 (hS100A9) antigen with high yield and purity and used it to generate a hybridoma cell culture-based monoclonal anti-hS100A9 antibody. We selected five anti-hS100A9 antibodies from cell supernatants that showed high antigen binding efficiency and identified the nucleotide sequences of three antibodies: two with high effective concentration values and one with the lowest value. The antigen and antibody development procedures described herein are useful for producing large amounts of monoclonal antibodies against hS100A9 and other antigens of interest. The nucleotide sequences of the anti-hS100A9 monoclonal antibody revealed herein will be helpful in the generation of recombinant antibodies or antibody fragments against hS100A9.

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Mohammadian, Omid, Masoumeh Rajabibazl, Hadi Bayat, and Azam Rahimpour. "Transient Expression of a Recombinant Monoclonal Antibody in HEK293T Cells." Pharmaceutical Sciences 24, no. 3 (September 23, 2018): 207–12. http://dx.doi.org/10.15171/ps.2018.30.

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Background: Monoclonal antibodies (mAbs) are considered the most important and financially successful category of the biopharmaceuticals. Extensive optimization of the expression vector, host system and culture parameters are required for the successful production of active monoclonal antibodies in mammalian cells. In this regards, transient expression enables rapid and cost-effective production of recombinant proteins for initial characterization. Methods: In the present study, an internal ribosome entry site (IRES) based bicistronic expression system has been evaluated for the transient expression of an anti-CD52 monoclonal antibody in mammalian cells. The IRES based bicistronic vector was generated through sequential cloning of the Light chain (LC), IRES, and Heavy chain (HC) in an intermediate vector and transfer of the resulting fragment to the expression vector. Transfection of the HEK293T cells was performed and antibody expression was analyzed in cell culture supernatant. Results: Restriction enzyme analysis indicated successful cloning of the antibody coding unit in the expression vector. Analysis of EGFP expression indicated successful transfection of the HEK293T cells. Production levels of 220 µg/L of antibody were achieved in HEK293T cells during three days of culture. Conclusion: Our results show the convenience and efficiency of the bicistronic expression system for transient expression of the whole monoclonal antibodies in mammalian cells.

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Yurkov, S. G., S. P. Zhivoderov, A. Y. Koltsov, R. A. Khamitov, N. V. Stratonova, and N. A. Litvinova. "Evaluation of the Virus Elimination and Inactivation at Different Stages of the Model Biotechnological Process for the Production of a Drug Based on the Monoclonal Antibody Fab-Fragment." Biotekhnologiya 37, no. 1 (2021): 69–80. http://dx.doi.org/10.21519/0234-2758-2021-37-1-69-80.

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Virus safety insuring is one of the most serious problems in the development of biotechnological drugs produced using animal cell lines. Quantitative assessment of virus removal and inactivation is an integral approach to show the reliability of the target compound production. In this work, the model experiments have been carried out on the purification of the monoclonal antibody recombinant Fab-fragment from viruses of various origins and properties: xenotropic murine leukemia virus (X-MuLV), pseudorabies virus (PRV), Reo-3 virus and encephalomyocarditis virus (EMCV). It was shown that two methods, acidification to pH 3.2 and nanofiltration, made it possible to reduce the virus infectivity to levels undetectable in cell cultures (according to TCID50). The developed multistage purification process of the target protein provided an overall decrease in viral clearance to the following values: X-MuLV≥10.17lg, PRV≥13.98lg, Reo-3≥8.09lg and EMCV≥4.98lg. These results confirm that the developed technology ensures the virus safety during the production of a monoclonal antibody recombinant Fab-fragment by CHO cell line. These results confirm virus safety of production technology of recombinant monoclonal antibody Fab-fragment produced in CHO cell line. virus safety, virus elimination, virus inactivation, nanofiltration, Fab-fragment, monoclonal antibody, CHO cell line

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Lyubarskaya, Yelena, Damian Houde, James Woodard, David Murphy, and Rohin Mhatre. "Analysis of recombinant monoclonal antibody isoforms by electrospray ionization mass spectrometry as a strategy for streamlining characterization of recombinant monoclonal antibody charge heterogeneity." Analytical Biochemistry 348, no. 1 (January 2006): 24–39. http://dx.doi.org/10.1016/j.ab.2005.10.003.

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Batista, Cassiano Martin, Lia Carolina Soares Medeiros, Iriane Eger, and Maurilio José Soares. "mAb CZP-315.D9: An Antirecombinant Cruzipain Monoclonal Antibody That Specifically Labels the Reservosomes ofTrypanosoma cruziEpimastigotes." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/714749.

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Reservosomes are large round vesicles located at the posterior end of epimastigote forms of the protozoanTrypanosoma cruzi, the etiological agent of Chagas disease. They are the specific end organelles of the endocytosis pathway ofT. cruzi, and they play key roles in nutrient uptake and cell differentiation. These lysosome-like organelles accumulate ingested macromolecules and contain large amounts of a major cysteine proteinase (cruzipain or GP57/51 protein). Aim of this study was to produce a monoclonal antibody (mAb) against a recombinantT. cruzicruzipain (TcCruzipain) that specifically labels the reservosomes. BALB/c mice were immunized with purified recombinant TcCruzipain to obtain the mAb. After fusion of isolated splenocytes with myeloma cells and screening, a mAb was obtained by limiting dilution and characterized by capture ELISA. We report here the production of a kappa-positive monoclonal IgG antibody (mAb CZP-315.D9) that recognizes recombinant TcCruzipain. This mAb binds preferentially to a protein with a molecular weight of about 50 kDa on western blots and specifically labels reservosomes by immunofluorescence and transmission electron microscopy. The monoclonal CZP-315.D9 constitutes a potentially powerful marker for use in studies on the function of reservosomes ofT. cruzi.

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Desogus, Alessandra, Roberto Burioni, Angela Ingianni, Francesca Bugli, Raffaello Pompei, and Giovanni Fadda. "Production and Characterization of a Human Recombinant Monoclonal Fab Fragment Specific for Influenza A Viruses." Clinical Diagnostic Laboratory Immunology 10, no. 4 (July 2003): 680–85. http://dx.doi.org/10.1128/cdli.10.4.680-685.2003.

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ABSTRACT A human recombinant monoclonal Fab fragment that specifically recognizes all the influenza A virus strains tested was produced in transformed Escherichia coli using the phage display technique. No strain of influenza B virus reacted with it. It was purified after four cycles of panning and by a single passage through an immunoaffinity column. About 1 mg of pure monoclonal antibody was obtained from 1 liter of culture medium in 3 working days. The Fab fragment reacted with a viral 27-kDa protein, which could reasonably be a matrix protein. Indirect immunofluorescence tests performed on virus-infected MDCK cells showed that this Fab fragment was at least equally efficient as other commercial monoclonal antibody-based systems in detecting influenza A viral infections. The potential advantages of human recombinant Fabs on murine monoclonal antibodies are discussed.

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Zheng, Ling, Shucheng Zhang, Charles Wood, Sanjay Kapil, Graham E. Wilcox, Thomas A. Loughin, and H. C. Minocha. "Differentiation of Two Bovine Lentiviruses by a Monoclonal Antibody on the Basis of Epitope Specificity." Clinical Diagnostic Laboratory Immunology 8, no. 2 (March 1, 2001): 283–87. http://dx.doi.org/10.1128/cdli.8.2.283-287.2001.

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ABSTRACT Bovine immunodeficiency virus (BIV) and Jembrana disease virus (JDV) are bovine lentiviruses that are closely related genetically. A recombinant fusion protein containing the capsid protein of BIV expressed in Escherichia coli was used to immunize mice and produce monoclonal antibodies. Six hybridomas specific for BIV capsid protein were identified, and one antibody, designated 10H1, was characterized further. Competitive binding assays were performed to analyze the topography of antigenic determinants by enzyme-linked immunosorbent assay and demonstrated the existence of at least three distinct antigenic determinants on capsid protein. The monoclonal antibody reacted specifically with both BIV capsid and the recombinant fusion protein in Western immunoblot analyses. However, it did not react with the recombinant capsid fusion protein of JDV, indicating that BIV contains at least one unique epitope in the capsid protein that is absent in JDV. Further mapping of the epitope by chemical cleavage analysis identified that the epitope is located at the 6.4-kDa N terminus of the 29-kDa capsid protein. This monoclonal antibody assay will be valuable for distinguishing the two closely related lentiviruses by Western blotting.

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Orlandi, R., M. Cattaneo, F. Troglio, M. Campiglio, I. Biunno, and S. Ménard. "Production of a Monoclonal Antibody Directed against the Recombinant SEL1L Protein." International Journal of Biological Markers 17, no. 2 (April 2002): 104–11. http://dx.doi.org/10.1177/172460080201700205.

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SEL1L, highly similar to the C. elegans sel-1 gene, is a recently cloned human gene whose function is under investigation. SEL1L is differentially expressed in tumors and normal tissues and seems to play a role in tumor growth and aggressiveness. We used the recombinant N-terminus of the SEL1L protein to immunize a Balb/c mouse and produce a monoclonal antibody. A hybridoma secreting an antibody specifically reacting on the SEL1L recombinant fragment was selected. This monoclonal antibody, named MSel1, recognizes the SEL1L protein by Western blotting, immunofluorescence and immunohistochemistry on normal and tumor cells. MSel1 is able to recognize SEL1L even on archival tumor specimens and is therefore particularly appropriate to study SEL1L involvement in tumor progression.

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Koo, Kai, Peggy M. Foegeding, and Harold E. Swaisgood. "Construction and Expression of a Bifunctional Single-Chain Antibody against Bacillus cereusSpores." Applied and Environmental Microbiology 64, no. 7 (July 1, 1998): 2490–96. http://dx.doi.org/10.1128/aem.64.7.2490-2496.1998.

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ABSTRACT The variable-region genes of monoclonal antibody againstBacillus cereus spores were cloned from mouse hybridoma cells by reverse transcription-PCR. The heavy- and light-chain variable-region genes were connected by a 45-base linker DNA to allow folding of the fusion protein into a functional tertiary structure. For detection of protein expression, a 10-amino-acid strep tag (biotin-like peptide) was attached to the C terminus of recombinant antibody as the reporter peptide. The single-chain antibody construct was inserted into the expression vector and expressed in Escherichia coliunder the control of the T7 RNA polymerase-T7 promoter expression system. The expressed single-chain antibody was detected on Western blots by using a streptavidin-conjugated enzyme system. This small recombinant antibody fragment (ca. 28,000 Da by calculation) hadB. cereus spore binding ability and antigen specificity similar to those of its parent native monoclonal antibody.

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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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KOLB, ANDREAS F., and STUART G. SIDDELL. "Expression of a Recombinant Monoclonal Antibody From a Bicistronic mRNA." Hybridoma 16, no. 5 (October 1997): 421–26. http://dx.doi.org/10.1089/hyb.1997.16.421.

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van Duijnhoven, Hans L. P., Torik A. Y. Ayoubi, Erika D. J. Timmera, Anneke A. M. Braks, Anton J. M. Roebroek, Gerard J. M. Martens, and Wim J. M. van de Ven. "Development of a monoclonal antibody against recombinant neuroendocrine 7B2 protein." FEBS Letters 255, no. 2 (September 25, 1989): 372–76. http://dx.doi.org/10.1016/0014-5793(89)81125-1.

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KAMIHIRA, MASAMICHI, ICHIROU KAWAKUBO, MASAYUKI TANIGUCHI, SHINJI IIJIMA, and TAKESHI KOBAYASHI. "Production and characterization of monoclonal antibody to recombinant .ALPHA.-amylase." Journal of Chemical Engineering of Japan 21, no. 4 (1988): 357–62. http://dx.doi.org/10.1252/jcej.21.357.

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Liu, Hongcheng, Christine Nowak, Mei Shao, Gomathinayagam Ponniah, and Alyssa Neill. "Impact of cell culture on recombinant monoclonal antibody product heterogeneity." Biotechnology Progress 32, no. 5 (August 3, 2016): 1103–12. http://dx.doi.org/10.1002/btpr.2327.

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Beck, Alain, Christine Nowak, Deborah Meshulam, Kristina Reynolds, David Chen, Dennis B. Pacardo, Samantha B. Nicholls, et al. "Risk-Based Control Strategies of Recombinant Monoclonal Antibody Charge Variants." Antibodies 11, no. 4 (November 20, 2022): 73. http://dx.doi.org/10.3390/antib11040073.

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Since the first approval of the anti-CD3 recombinant monoclonal antibody (mAb), muromonab-CD3, a mouse antibody for the prevention of transplant rejection, by the US Food and Drug Administration (FDA) in 1986, mAb therapeutics have become increasingly important to medical care. A wealth of information about mAbs regarding their structure, stability, post-translation modifications, and the relationship between modification and function has been reported. Yet, substantial resources are still required throughout development and commercialization to have appropriate control strategies to maintain consistent product quality, safety, and efficacy. A typical feature of mAbs is charge heterogeneity, which stems from a variety of modifications, including modifications that are common to many mAbs or unique to a specific molecule or process. Charge heterogeneity is highly sensitive to process changes and thus a good indicator of a robust process. It is a high-risk quality attribute that could potentially fail the specification and comparability required for batch disposition. Failure to meet product specifications or comparability can substantially affect clinical development timelines. To mitigate these risks, the general rule is to maintain a comparable charge profile when process changes are inevitably introduced during development and even after commercialization. Otherwise, new peaks or varied levels of acidic and basic species must be justified based on scientific knowledge and clinical experience for a specific molecule. Here, we summarize the current understanding of mAb charge variants and outline risk-based control strategies to support process development and ultimately commercialization.

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Chargelegue, Daniel, Pascal M. W. Drake, Patricia Obregon, Alessandra Prada, Neil Fairweather, and Julian K.-C. Ma. "Highly Immunogenic and Protective Recombinant Vaccine Candidate Expressed in Transgenic Plants." Infection and Immunity 73, no. 9 (September 2005): 5915–22. http://dx.doi.org/10.1128/iai.73.9.5915-5922.2005.

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ABSTRACT Vaccine development has been hampered by difficulties in developing new and safe adjuvants, so alternative technologies that offer new avenues forward are urgently needed. The goal of this study was to express a monoclonal recombinant immune complex in a transgenic plant. A recombinant protein consisting of a tetanus toxin C fragment-specific monoclonal antibody fused with the tetanus toxin C fragment was designed and expressed. Immune complex formation occurred between individual fusion proteins to form immune complex-like aggregates that bound C1q and FcγRIIa receptor and could be targeted to antigen-presenting cells. Unlike antigen alone, the recombinant immune fusion complexes were highly immunogenic in mice and did not require coadministration of an adjuvant (when injected subcutaneously). Indeed, these complexes elicited antibody titers that were more than 10,000 times higher than those observed in animals immunized with the antigen alone. Furthermore, animals immunized with only 1 μg of recombinant immune complex without adjuvant were fully protected against lethal challenge. This the first report on the use of a genetic fusion between antigen and antibody to ensure an optimal expression ratio between the two moieties and to obtain fully functional recombinant immune complexes as a new vaccine model.

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Brena, Sonia, Miren J. Omaetxebarría, Natalia Elguezabal, Jonathan Cabezas, María D. Moragues, and José Pontón. "Fungicidal Monoclonal Antibody C7 Binds to Candida albicans Als3." Infection and Immunity 75, no. 7 (April 23, 2007): 3680–82. http://dx.doi.org/10.1128/iai.01840-06.

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ABSTRACT Monoclonal antibody (MAb) C7 reacted with a >200-kDa component from the Candida albicans cell wall identified by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry as Als3. It also bound the recombinant N terminus of Als3. Binding of MAb C7 to Als3 may explain the biological activities exerted by the MAb on C. albicans.

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Ginsburg, David, Paula L. Bockenstedt, Elizabeth A. Allen, David A. Fox, Paul A. Foster, Zaverio M. Ruggeri, Theodore S. Zimmerman, et al. "Fine Mapping of Monoclonal Antibody Epitopes on Human von Willebrand Factor Using a Recombinant Peptide Library." Thrombosis and Haemostasis 67, no. 01 (1992): 166–71. http://dx.doi.org/10.1055/s-0038-1648400.

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SummaryA recombinant human von Willebrand factor (vWF) cDNA fragment library was constructed in λgtll for the localization of anti-vWF monoclonal antibody epitopes. Twelve of 21 monoclonal antibodies screened identified epitopes expressed in λgtll as β-galactosidase fusion proteins. By sequence analysis, these antigenic determinants were localized to segments ranging from 17 to 105 amino acids in length. Four epitopes apparently shared by more than one antibody were identified, suggesting the presence of immuno-dominant epitopes within vWF. Monoclonal antibody C3, which blocks factor VIII (FVIII) binding to vWF, bound to the same epitope previously identified by a second monoclonal antibody which also blocks this function, suggesting that this region may be at or near the vWF/FVIII binding domain. Three antibodies recognize the same region within the vWF A2 repeat. Mutations near this region appear to be responsible for Type IIA von Willebrand’s disease. The co-localization of these antibodies suggests that this domain might be exposed on the surface of vWF, consistent with its apparent increased sensitivity to plasma proteases.

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Liu, Dong, Mandy Tseng, Linda F. Epstein, Lydia Green, Brian Chan, Brian Soriano, Desiree Lim, et al. "Evaluation of recombinant monoclonal antibody SVmab1 binding to NaV1.7 target sequences and block of human NaV1.7 currents." F1000Research 5 (November 25, 2016): 2764. http://dx.doi.org/10.12688/f1000research.9918.1.

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Identification of small and large molecule pain therapeutics that target the genetically validated voltage-gated sodium channel NaV1.7 is a challenging endeavor under vigorous pursuit. The monoclonal antibody SVmab1 was recently published to bind the NaV1.7 DII voltage sensor domain and block human NaV1.7 sodium currents in heterologous cells. We produced purified SVmab1 protein based on publically available sequence information, and evaluated its activity in a battery of binding and functional assays. Herein, we report that our recombinant SVmAb1 does not bind peptide immunogen or purified NaV1.7 DII voltage sensor domain via ELISA, and does not bind NaV1.7 in live HEK293, U-2 OS, and CHO-K1 cells via FACS. Whole cell manual patch clamp electrophysiology protocols interrogating diverse NaV1.7 gating states in HEK293 cells, revealed that recombinant SVmab1 does not block NaV1.7 currents to an extent greater than observed with an isotype matched control antibody. Collectively, our results show that recombinant SVmab1 monoclonal antibody does not bind NaV1.7 target sequences or specifically inhibit NaV1.7 current.

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Burrin, J. M., J. L. Paterson, P. S. Sharp, and T. H. Yeo. "Monoclonal and polyclonal antibodies compared for radioimmunoassay of somatomedin-C in patients with acromegaly or hypopituitarism." Clinical Chemistry 33, no. 9 (September 1, 1987): 1593–96. http://dx.doi.org/10.1093/clinchem/33.9.1593.

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Abstract We used a synthetic recombinant analog of somatomedin-C (Sm-C) to directly compare the performance of polyclonal and monoclonal antibodies for measuring Sm-C in serum of normal persons and in acromegalic or hypopituitary patients. Mean concentrations of Sm-C in healthy adults were 181 (SD 42) micrograms/L as measured with the monoclonal antibody, 194 (SD 61) micrograms/L with the polyclonal antibody. Both antisera gave excellent discrimination between acromegalics and normals. However, the assay with the polyclonal antibody was more sensitive than that with the monoclonal antibody (lower detection limits: 5 vs 100 micrograms/L) and thus better suited for quantifying Sm-C in samples from hypopituitary patients.

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Woźniakowski, Grzegorz, and Elżbieta Samorek-Salamonowicz. "In Vitro Replication of Recombinant Marek’S Disease Viruses Constructed from Field Strains Lacking Meq and Vtr Oncogenes." Bulletin of the Veterinary Institute in Pulawy 57, no. 2 (June 1, 2013): 141–47. http://dx.doi.org/10.2478/bvip-2013-0027.

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Abstract The study describes construction of five recombinant very virulent (vv) and very virulent plus (vv+) strains lacking meq and viral telomerase (vTR). Deletion of both copies of meq and vTR was achieved by Red E/T recombination in GS1783 E. coli cells. The constructed bacterial artificial chromosome (BAC) clones reconstituted in chicken embryo fibroblasts were examined by immunofluorescence assay to compare the features of recombinant strains with wild-type viruses. The results demonstrated that recombinant BAC strains caused slightly reduced cytophatic effect and decreased level of the fluorescence obtained from the monoclonal antibody in comparison to the parental viruses. Generation of recombinant BAC clones may provide more detailed information on the function of Marek's disease virus oncogenes and the potential use of recombinants for the preparation of the new vaccine against Marek’s disease.

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Alves, Bryce, Mary Anne Jelinek, Yanan Lu, Melissa Ritland, Patricia Velasco, Xi Zhao, Eddie Adams, and Joseph Fernandez. "Single B cell isolation and cloning from rabbits to generate recombinant antibodies." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 159.53. http://dx.doi.org/10.4049/jimmunol.204.supp.159.53.

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Abstract For decades the method for generating antibodies with high avidity and affinity relied upon monoclonal antibody generation from immunized mice or polyclonal antibodies from rabbits. Both methods have their shortcomings. The murine immune system—specifically the high degree of immunological tolerance—prevents robust humoral responses to antigens that closely reasonable self-antigens in the mouse. Additionally, the cost and time necessary to generate a monoclonal antibody from mice can be prohibitively expensive, particularly if multiple attempts at hybridoma generation are required. A work around is to generate polyclonal antibodies in rabbits. Rabbits are further evolutionarily removed from humans than mice and mount a stronger immunological response to immunized human proteins or antigens. Unfortunately, the source of polyclonal antibodies from each rabbit is finite. To combat this problem, here we describe the development of a method to isolate single rabbit plasma B cells after immunization. Once isolated the VH and VL regions of the antibody are sequenced and the sequences are cloned into a recombinant rabbit IgG and IgK backbone that enables the recombinant expression of the single cell-derived, cloned rabbit antibodies. In doing so we have harnessed the immunological response of the rabbit host while eliminating the supply problem of finite reactive serum volumes and the cost of traditional murine monoclonal antibody generation.

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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 (April 1, 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 virus-like particles (VLP-VP2/6 and VLP-VP2/6/7) and recombinant VP4 protein produced from baculovirus recombinants indicated that 1-2H and 2-3E bind to VP4 and that 2-11G binds to VP7. The neutralization epitope recognized by each of the three human antibodies might be human specific, since all of the antigenic mutants resistant to mouse monoclonal neutralizing antibodies previously prepared were neutralized by the human antibodies obtained here. After conversion from the Fab form of an antibody into immunoglobulin G1, the neutralizing activities of these three clones toward various human rotavirus strains were examined. The 1-2H antibody exhibited neutralizing activity toward human rotaviruses with either the P[4] or P[8] genotype. Similarly, the 2-3E antibody showed cross-reactivity against HRVs with the P[6], as well as the P[8] genotype. In contrast, the 2-11G antibody neutralized only human rotaviruses with the G1 serotype. The concentration of antibodies required for 50% neutralization ranged from 0.8 to 20 μg/ml.

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Baharudeen, Zamrina, Rahmah Noordin, Lim Theam Soon, Dinesh Balachandra, Nor Suhada Anuar, Fatin Hamimi Mustafa, and Anizah Rahumatullah. "Isolation and Production of Human Monoclonal Antibody Proteins against a Toxocara canis Excretory–Secretory Recombinant Antigen." Pathogens 11, no. 11 (October 25, 2022): 1232. http://dx.doi.org/10.3390/pathogens11111232.

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Toxocariasis is a widespread zoonotic parasitic disease with a significant socioeconomic impact, particularly on underprivileged communities. Limitations of existing diagnostic tools and vague presenting symptoms may lead to misdiagnosis, thus underestimating the actual global impact of the disease. The present study describes the isolation and production of novel recombinant monoclonal antibodies against Toxocara canis recombinant TES-26 antigen (rTES-26) utilizing a human helminth scFv phage display library. The isolated antibody clones were characterized based on their gene sequences and binding characteristics. Three clones representing unique gene families (clone 48: IgHV3-LV1; clone 49: IgHV3-LV3; clone 50: IgHV6-LV3) were isolated, but only clones 48 and 49 showed successful insertion of the full-length scFv antibody sequence after sub-cloning. Both clones produced antibody proteins of good solubility and satisfactory yield and purity. Binding assays via Western blot and ELISA using rTES-26 and Toxocara canis native protein showed that both monoclonal antibodies were highly specific and sensitive to the target antigen. A preliminary antigen detection ELISA showed the diagnostic potential of the monoclonal antibody proteins. The proteins can also be useful in studying host–parasite interactions and therapeutic applications.

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Braren, Ingke, Simon Blank, Henning Seismann, Susanne Deckers, Markus Ollert, Thomas Grunwald, and Edzard Spillner. "Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries." Clinical Chemistry 53, no. 5 (May 1, 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, bovine milk, and apple. The scFv obtained were converted into IgG1, IgG4, and IgE antibody formats and assessed for their biochemical properties by ELISA, immunoblotting, and fluorescence-activated cell sorting. Results: Two different antibody formats for each IgG1, IgG4, and IgE antibody were produced in mammalian cells as disulfide-linked and glycosylated Ig, which were usable in allergen-specific ELISA assays and immunoblots. In addition, the recombinant IgE antibodies mediated the binding of allergens to HEK-293 cells transfected with the high-affinity IgE receptor, and this binding was blocked by corresponding IgG antibodies. Conclusions: The use of synthetic libraries for the generation of allergen-specific recombinant IgE and IgG antibodies should have broad applications in allergological research and diagnosis.

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May, Kenneth F., Bettina Franz, Christopher Harvey, F. Stephen Hodi, Glenn Dranoff, and Kai Wucherpfennig. "Isolation of human anti-MICA antibody from cancer patients responding to immunotherapies." Journal of Clinical Oncology 30, no. 15_suppl (May 20, 2012): 2502. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.2502.

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2502 Background: Immunotherapy is a promising modality for the treatment of cancer, and elucidating the mechanism of action is crucial to guiding patient selection and developing future immunotherapeutic strategies. Engagement of the immune molecule NKG2D by the cancer antigen MICA is important for immune surveillance of many cancers. Tumors can evade immune surveillance by shedding cell surface MICA, which leads to dampening of anti-tumor immunity. Investigations by our laboratory revealed that patients responding to immunotherapy can mount antibody responses targeting MICA, which permits re-engagement of immunity. Methods: Patients with advanced cancer treated at our institution with immunotherapies (tumor cell vaccination, ipilimumab) were identified, including several with long-term clinical remissions. Plasma was analyzed for MICA reactivity to three distinct MICA alleles, and rare memory B cells reactive to MICA were isolated using tetramerized MICA protein. Immunoglobulin heavy and light chain variable domains were sequenced with single cell RT-PCR to generate recombinant monoclonal antibody. Results: Plasma from patients treated with immunotherapy revealed considerable inter-patient variation in reactivity to MICA. Patients with marked plasma reactivity (including several with sustained clinical remissions) were selected for isolation of rare memory B cells reactive to MICA. From these cells, we have generated a recombinant fully-human MICA-reactive monoclonal antibody that exhibits binding to a variety of MICA alleles. Conclusions: We have developed novel methods to analyze anti-MICA antibody responses and isolate rare memory B cells from cancer patients who gained significant clinical benefit from immunotherapy. This has facilitated the generation of fully human recombinant anti-MICA monoclonal antibody. To our knowledge, this is the first example of a specific antibody reactive to a cancer antigen isolated from a cancer patient responding to immunotherapy. As these antibody responses likely played a role in tumor destruction, these results inform the development of new antibody-based immunotherapies targeting the NKG2D-MICA pathway.

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Saijo, Masayuki, Marie-Claude Georges-Courbot, Philippe Marianneau, Victor Romanowski, Shuetsu Fukushi, Tetsuya Mizutani, Alain-Jean Georges, Takeshi Kurata, Ichiro Kurane, and Shigeru Morikawa. "Development of Recombinant Nucleoprotein-Based Diagnostic Systems for Lassa Fever." Clinical and Vaccine Immunology 14, no. 9 (July 18, 2007): 1182–89. http://dx.doi.org/10.1128/cvi.00101-07.

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ABSTRACT Diagnostic systems for Lassa fever (LF), a viral hemorrhagic fever caused by Lassa virus (LASV), such as enzyme immunoassays for the detection of LASV antibodies and LASV antigens, were developed using the recombinant nucleoprotein (rNP) of LASV (LASV-rNP). The LASV-rNP was expressed in a recombinant baculovirus system. LASV-rNP was used as an antigen in the detection of LASV-antibodies and as an immunogen for the production of monoclonal antibodies. The LASV-rNP was also expressed in HeLa cells by transfection with the expression vector encoding cDNA of the LASV-NP gene. An immunoglobulin G enzyme-linked immunosorbent assay (ELISA) using LASV-rNP and an indirect immunofluorescence assay using LASV-rNP-expressing HeLa cells were confirmed to have high sensitivity and specificity in the detection of LASV-antibodies. A novel monoclonal antibody to LASV-rNP, monoclonal antibody 4A5, was established. A sandwich antigen capture (Ag-capture) ELISA using the monoclonal antibody and an anti-LASV-rNP rabbit serum as capture and detection antibodies, respectively, was then developed. Authentic LASV nucleoprotein in serum samples collected from hamsters experimentally infected with LASV was detected by the Ag-capture ELISA. The Ag-capture ELISA specifically detected LASV-rNP but not the rNPs of lymphocytic choriomeningitis virus or Junin virus. The sensitivity of the Ag-capture ELISA in detecting LASV antigens was comparable to that of reverse transcription-PCR in detecting LASV RNA. These LASV rNP-based diagnostics were confirmed to be useful in the diagnosis of LF even in institutes without a high containment laboratory, since the antigens can be prepared without manipulation of the infectious viruses.

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Tanaka, Tetsuya, Ichiro Nakamura, Nai-Yuan Lee, Haruto Kumura, and Kei-ichi Shimazaki. "Expression of bovine lactoferrin and lactoferrin N-lobe by recombinant baculovirus and its antimicrobial activity against Prototheca zopfii." Biochemistry and Cell Biology 81, no. 5 (October 1, 2003): 349–54. http://dx.doi.org/10.1139/o03-062.

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Lactoferrin (LF) is a multifunctional, iron-binding glycoprotein found in secretory fluids of mammals. In this study, DNA encoding bovine lactoferrin (bLF) or the N-terminal half of bLF (bLF N-lobe) was inserted into a baculovirus transfer vector, and a recombinant virus expressing bLF or bLF N-lobe was isolated. An 80-kDa bLF-related protein expressed by the recombinant baculovirus was detected by monoclonal antibodies against bLF N-lobe and the C-terminal half of bLF (bLF C-lobe). A 43-kDa bLF N-lobe-related protein expressed by the recombinant baculovirus was detected by anti-bLF N-lobe monoclonal antibody, but not by anti-bLF C-lobe monoclonal antibody. These proteins were also secreted into the supernatant of insect cell cultures. Recombinant bLF (rbLF) and bLF N-lobe (rbLF N-lobe) were affected by tunicamycin treatment, indicating that rbLF and rbLF N-lobe contain an N-linked glycosylation site. Antimicrobial activity of these recombinant proteins against Prototheca zopfii (a yeast-like fungus that causes bovine mastitis) was evaluated by measuring the optical density of the culture microplate. Prototheca zopfii was sensitive to rbLF and rbLF N-lobe, as well as native bLF. There was no difference in antimicrobial activity between rbLF N-lobe and bLF C-lobe.Key words: lactoferrin, lactoferrin N-lobe, baculovirus, antimicrobial activity, Prototheca zopfii.

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Orlandi, R., M. Cattaneo, F. Troglio, M. Campiglio, I. Biunno, and S. Mnard. "Production of a monoclonal antibody directed against the recombinant SEL1L protein." International Journal of Biological Markers 17, no. 2 (2002): 104–11. http://dx.doi.org/10.5301/jbm.2008.4015.

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Iizuka, Masashi, Shingo Ogawa, Atsushi Takeuchi, Shinichi Nakakita, Yuhki Kubo, Yoshitaka Miyawaki, Jun Hirabayashi, and Masahiro Tomita. "Production of a recombinant mouse monoclonal antibody in transgenic silkworm cocoons." FEBS Journal 276, no. 20 (September 9, 2009): 5806–20. http://dx.doi.org/10.1111/j.1742-4658.2009.07262.x.

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Lam, Xanthe M., Janet Y. Yang, and Jeffrey L. Cleland. "Antioxidants for Prevention of Methionine Oxidation in Recombinant Monoclonal Antibody HER2." Journal of Pharmaceutical Sciences 86, no. 11 (November 1997): 1250–55. http://dx.doi.org/10.1021/js970143s.

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Greiner, J., F. Guadagni, P. Noguchi, S. Pestka, D. Colcher, P. Fisher, and J. Schlom. "Recombinant interferon enhances monoclonal antibody-targeting of carcinoma lesions in vivo." Science 235, no. 4791 (February 20, 1987): 895–98. http://dx.doi.org/10.1126/science.3580039.

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Journal articles on the topic 'Recombinant monoclonal antibody'

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