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Littérature scientifique sur le sujet « Recombinant monoclonal antibody »

Auteur : Grafiati

Publié le 14 mars 2023

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Articles de revues sur le sujet "Recombinant monoclonal antibody"

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Siegel, D. L. « Recombinant monoclonal antibody technology ». Transfusion Clinique et Biologique 9, n^o 1 (janvier 2002) : 15–22. http://dx.doi.org/10.1016/s1246-7820(01)00210-5.

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Liu, Hongcheng, Georgeen Gaza-Bulseco et Chris Chumsae. « Glutamine deamidation of a recombinant monoclonal antibody ». Rapid Communications in Mass Spectrometry 22, n^o 24 (30 décembre 2008) : 4081–88. http://dx.doi.org/10.1002/rcm.3831.

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Eltarhoni, Khadiga, Faddy Kamel, Katrina Ihebunezie, Pasha Nisar et Mikhail Soloviev. « Therapeutic Antibodies in Cancer Treatment in the UK ». International Journal of Molecular Sciences 23, n^o 23 (23 novembre 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 et T. Viskovic. « generation of hapten-specific recombinant antibodies : antibody phage display technology : a review ». Veterinární Medicína 50, No. 6 (28 mars 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 et Birte Aggeler. « Recombinant Rabbit Monoclonal Antibodies to Study Apoptosis and Apoptotic Pathways (132.4) ». Journal of Immunology 184, n^o 1_Supplement (1 avril 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., et I. Barker. « Virus Strain Discrimination Using Recombinant Antibodies ». Disease Markers 16, n^o 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, n^o 4 (20 mars 2018) : 513–38. http://dx.doi.org/10.1080/19420862.2018.1438797.

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Schrader, John W., et Gary R. McLean. « Multispecificity of a recombinant anti-ras monoclonal antibody ». Journal of Molecular Recognition 31, n^o 2 (8 novembre 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 et Reinhard Bredehorst. « Bivalent monoclonal IgY antibody formats by conversion of recombinant antibody fragments ». Journal of Biotechnology 124, n^o 2 (juillet 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, n^o 3 (14 février 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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Thèses sur le sujet "Recombinant monoclonal antibody"

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Johansson, Daniel X. « Expression and interaction studies of recombinant human monoclonal antibodies / ». Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-137-1/.

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Sheikholvaezin, Ali. « Recombinant antibodies and tumor targeting ». Doctoral thesis, Umeå : Univ, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-875.

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López, Cerro Maria Teresa. « Strategies to improve Chlamydomonas reinhardtii as a recombinant protein host : from a small growth factor to a complex monoclonal antibody production ». Doctoral thesis, Universitat de Barcelona, 2018. http://hdl.handle.net/10803/586310.

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Chlamydomonas reinhardtii has emerged as a promising alternative host for recombinant protein expression. Despite its advantageous characteristics and low-cost production, its use is hampered by low expression levels of nuclear transgenes. In this thesis we test several strategies designed to reduce or overcome this limitation. As a result, on the base of a secreted fusion protein comprising a small growth factor and a reporter, the use of regulatory and stabilizing regions resulted in expression levels ranging from 1 to 100 µg /L of culture. We report the expression of a fully-assembled monoclonal antibody in Chlamydomonas nucleus, therefore, validating Chlamydomonas as a host for complex protein production. The cassettes and high throughput screenings developed emerge as innovative tools expanding the molecular toolbox available for Chlamydomonas nucleus. In addition, a scalable purification method to recover the target protein from culture medium has been developed and validated indicating a simple downstream processing for secreted recombinant protein production. Finally, we report that Chlamydomonas secreted components induce proliferation of murine fibroblasts and have a synergistic effect with supplied hEGF, unveiling the potential of extracellular components of Chlamydomonas for a variety of applications.
Las proteínas recombinantes ofrecen un gran potencial para diversas aplicaciones impactando procesos industriales, investigación, el mercado cosmético y el mercado terapéutico. Chlamydomonas reinhardtii es un huésped prometedor para expresión de proteínas recombinantes. A pesar de ofrecer características ventajosas y bajos costes de producción, su uso se ve limitado por bajos niveles de expresión de transgenes nucleares. En la presente tesis se testan diversas estrategias con el objetivo de superar esta limitación. Como resultado, en base a la secreción de una proteína de fusión formada por un factor de crecimiento y un reportero, el uso de regiones reguladoras y estabilizadoras ha resultado en niveles de expresión entre 1 y 100 µg /L de cultivo. Además, en la presente tesis se recoge la expresión nuclear de un anticuerpo monoclonal en Chlamydomonas, así como su secreción y acumulación en el medio. Este anticuerpo está correctamente plegado y reconoce su antígeno. Esto representa un punto clave para Chlamydomonas ya que significa su validación como huésped para la expresión de proteínas complejas. Los vectores y cribados desarrollados emergen como recursos innovadores que expanden la batería de herramientas disponible para la modificación genética del núcleo de Chlamydomonas. Además, se ha desarrollado y validado un método de purificación de proteína recombinante des de medio. La simplicidad de este método de purificación indica la potencia de Chlamydomonas como huésped industrial para la expresión de proteínas recombinantes. Finalmente, en la presente tesis se reporta la proliferación de fibroblastos murinos inducida por componentes secretados por Chlamydomonas y su efecto sinérgico cuando se aplican con el factor de crecimiento humano, revelando así el potencial de los componentes extracelulares de Chlamydomonas.

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Fiddes, Jane L. Sutton Biotechnology &amp Biomolecular Sciences Faculty of Science UNSW. « Development of recombinant human monoclonal antibodies suitable for blood grouping using antibody engineering techniques ». Awarded by:University of New South Wales. Biotechnology & ; Biomolecular Sciences, 2007. http://handle.unsw.edu.au/1959.4/40503.

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Transfusion medicine is an important part of modern health care and the provision of reliably phenotyped red blood cells (RBC) is essential for safe and effective blood transfusions. For identification of many RBC antigens, monoclonal antibodies of either murine or human origin are available for use in agglutination assays, in which they perform as well as or better than the human polyclonal antibody preparations which they have replaced. However, the detection of some blood groups is still reliant on the use of human polyclonal antisera, which is a less reliable reagent source with respect to availability, batch to batch variation and bio-safety. The use of recombinant antibody and phage display technology for the discovery of new monoclonal antibodies with specificity for some of these RBC antigens has the potential to deliver an economical, unlimited supply of specific antibody reagents suitable for use in RBC phenotyping. Samples of human B cells from donors producing useful phenotyping antibodies were identified and transformed using Epstein Barr virus into lymphocyte cell lines. Antibody genes were obtained from the cell lines in the form ofRNA which was reverse transcribed, amplified by PCR and cloned into a phagemid vector system to generate several combinatorial antibody libraries. These antibody libraries were displayed on the surface of phage particles and subjected to antigen-driven selection by several rounds of phage display biopanning using soluble and cell based RBC antigens. In addition a large naIve library was biopanned against the same antigens in an attempt to isolate a wide range of antibodies suitable for blood typing. Several high quality combinatorial antibody libraries with respect to size (> 107 clones) and diversity were generated. Biopanning of recombinant libraries resulted in enrichment of phage antibodies specific for RBC antigens, and several clones were isolated which were shown to be specific for Duffy a antigen. The isolated antibodies would be ideal candidates for re-engineering into multivalent antibody molecules capable of direct agglutination of RBC and as such, have the potential to replace human polyclonal sera in the identification of Duffy a RBC antigen phenotyping.

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Cromwell, Mary Ellen Miley. « Self-association, crystallization, and phase separation : understanding intermolecular interactions for a monoclonal antibody / ». Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2008.

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Thesis (Ph.D. in Pharmaceutical Sciences) -- University of Colorado Denver, 2008.
Typescript. Includes bibliographical references (leaves 209-236). Free to UCD affiliates. Online version available via ProQuest Digital Dissertations;

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Bailey, Laura. « Investigating the influence of long-term culture and feed additions on recombinant antibody production in Chinese hamster ovary cells ». Thesis, University of Manchester, 2011. https://www.research.manchester.ac.uk/portal/en/theses/investigating-the-influence-of-longterm-culture-and-feed-additions-on-recombinant-antibody-production-in-chinese-hamster-ovary-cells(1ccfdb8f-c0a6-49c8-a7a7-5e79b84e2862).html.

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Chinese hamster ovary (CHO) cell lines are frequently used as hosts for the production of recombinant therapeutics, such as monoclonal antibodies (MAbs), due to their ability to perform correct post-translational modifications. A major issue for use of CHO cells lines for the production of recombinant proteins is the selection of cell lines that do not retain stable protein expression during long-term culture (LTC). Instability of expression impairs process yields, effective usage of time and money, and regulatory approval. Protein production is complex and is influenced by cell growth, transcription, translation, protein folding and post-translational processing and secretory events, which may interact to determine stability of expression during prolonged culture. This thesis aims to identify features associated with stability/instability of recombinant protein expression and methods to improve protein production, with the addition of chemically defined (CD) feed and chemicals. Two exemplar CHO cell lines, which secrete the same recombinant antibody were characterised in response to LTC, feed and DMSO addition. Both cell lines (3.90 and 51.69) exhibited unstable protein production over LTC, with a loss in final antibody titres and specific productivity (Qp). The instability observed within the exemplar cell lines was not due to decreased recombinant gene copy numbers or mRNA expression but was associated with lower viable cell densities, increased ER stress (GADD153 and spliced XBP-1 [XBP-1(s)]) and enhanced rates of lactate utilisation (observed during the decline phase of batch culture). Improvement of recombinant protein expression in response to feed or DMSO addition was associated with lower expression of ER stress markers (ATF4, XBP-1(s) and GADD153 at mRNA level and GADD153 at protein level) and alterations to the metabolic activity of the cultures (prevention of alanine and lactate re-utilisation, and greater glucose utilisation between the stationary and decline phase of batch culture).Although feed or DMSO addition improved recombinant protein production, these additions did not reverse the appearance or progression of instability for cells after LTC. ER stress expression was not abolished as a consequence of feed or DMSO addition. Expression of stress markers at earlier time points may be the factor that limits antibody production and secretion. The consequences of the presence of feed and DMSO addition on ER stress markers and antibody production serves to highlight approaches that may be utilised for engineering more productive or stable protein production phenotypes in parental cell lines.

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Thirumangalathu, Renuka. « Understanding physical and chemical stability of proteins in solution : relevance to therapeutic protein and monoclonal antibody formulations / ». Connect to abstract via ProQuest. Full text is not available online, 2007.

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Thesis (Ph.D. in Pharmaceutical Sciences) -- University of Colorado Denver, 2007.
Typescript. Includes bibliographical references (leaves 133-143). Online version available via ProQuest Digital Dissertations.

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Maiocchi, Rebecca. « Recovery of rare cells and single cells analysis : different opportunities and challenging applications ». Doctoral thesis, Università di Siena, 2021. http://hdl.handle.net/11365/1128669.

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Single-cell biology is a new discipline which aims to address and solve the problem of cellular heterogeneity. Single-cell omic, which allows the molecular investigation of different cell types in a high throughput manner, is driving the Precision and Personalized Medicine approaches. Single B cell isolation strategies, the starting points of the single-cell omics, have become essential research procedures for efficiently sampling the natural repertoire of immunized animals and humans (Tiller et al, 2008). The goal of the first study is to demonstrate the feasibility of a novel approach to rapidly generate recombinant mAbs recovering rare antigen-specific plasma cells from complex samples derived from immunized mice. TLS Foundation, where this work has been carried out, has recently invested in Precision Medicine activities and, in particular, in the development of an alternative method to hybridoma technology to isolate rare antigen-specific B cells from blood of immunized or infected individuals. In Study 1 we have set-up a FACS sorter free method for a fast identification and isolation of antigen-specific plasma cells producing IgG with unique and desirable features and, moreover, we have obtained high yield TAP-PCR products. This could simplify the actual hybridoma technology procedure for the identification and molecular cloning of antigen-specific antibodies from single-B cells. Single-cell biology is also used to address and solve problems related to tumour heterogeneity. Cancer is one of the research areas that has greatly benefited from single-cell analysis. The complexity of immune responses to cancer has hampered the development of novel therapeutical approaches with the exception of monoclonal antibody based-therapies that target specific immunomodulators. In the last 10 years PD-1 blockade monoclonal therapy has indeed revolutionized cancer treatments but a substantial population of patients is still unresponsive. To rescue unresponsive patients, the mechanism of unresponsiveness and phenotype must be elucidated. The second part of this work (Study 2) deals with the possibility to reveal one of the mechanism responsible for T cells exhaustion in patients that are non-responsive to monoclonal anti-PD1 therapy. We demonstrated that there is a correlation between the overexpression of TFX (Transcriptional Factor X, the real name of the factor has been hidden for confidentiality) and the onset of the characteristic features of exhaustion. Indeed the KO of this gene restores in T cells their functionality through a more active metabolism. Further in-depth study of the modulation of this transcription factor may elucidate the pathways and the genes responsible for the exhaustion phenotype in T cells.

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Caucheteur, Déborah. « Nouveau format de banques d’anticorps recombinants humains pour un criblage fonctionnel à grande échelle ». Thesis, Montpellier, 2018. http://www.theses.fr/2018MONTT012.

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Les anticorps monoclonaux (mAb) sont depuis les années 2000 devenus des médicaments incontournables et de routine en thérapie et notamment en cancérologie. Le domaine continue à croître très rapidement et devant l’abondance des molécules disponibles, il est de plus en plus important d’apporter des molécules innovantes à haute valeur ajoutée pour la thérapie. Deux grandes approches sont utilisées pour sélectionner ces mAbs : l’hybridation lymphocytaire à partir de souris normales ou humanisées ; Les systèmes de display comme le phage-display. Les intérêts majeurs du phage display sont la rapidité de développement des mAbs, la facilité de manipulation chez E. coli, l’accès aux techniques de "protein engineering". Classiquement, les anticorps sont d’abord sélectionnés sur leur capacité de liaison à l’antigène puis ensuite testés pour leur efficacité fonctionnelle dans des modèles cellulaires. Cependant, seulement une partie de l'activité des anticorps est expliquée par leur liaison à l’antigène et l’activité thérapeutique dépend aussi fortement de leur capacité à recruter le système immunitaire (ADCC) et à activer la cascade du complément (CDC).Ce projet de thèse consiste à développer un nouveau format de banque d'anticorps recombinants combinant la puissance de la sélection par phage display à un criblage fonctionnel au format IgG entières produites en cellules eucaryotes. Ce nouveau système est basé sur des régions initiatrices hybrides contenant à la fois des promoteurs et des séquences signal procaryotes et eucaryotes permettant l’expression dans ces deux systèmes cellulaires, et des évènements de recombinaisons sites-spécifiques transférant le fragment Fab du vecteur de display vers le chromosome d’une lignée cellulaire de mammifère spécialement développée pour aboutir à la sécrétion d’un anticorps humain monoclonal par la cellule. L’approche habituelle de reclonage un par un du vecteur E. Coli au format IgG n’est plus nécessaire puisqu’il se fait directement par transfection. Ce nouveau système rend possible le couplage d’une sélection par phage display à un criblage fonctionnel direct sur une large population de clones monoclonaux humains
Since 2000, monoclonal antibodies (mAb) have become essential and routine drugs in therapy and particularly in oncology. The field continues to grow very quickly and given the abundance of molecules available, it is increasingly important to bring innovative molecules with a high added value for therapy.Two main approaches are used to select these mAbs: hybridoma technology using normal or humanized mice; display systems such as phage-display. The major interests of phage display are the speed of mAb development, the facilities offered by E. coli and the easy access to protein engineering techniques. Typically, antibodies are first selected on their ability to bind to the antigen, and then tested for their functional efficiency in cellular models. However, only a part of the activity of antibodies is explained by their binding to the antigen, and the therapeutic activity also depends strongly on their ability to recruit the immune system (ADCC) and activate the complement cascade (CDC).This thesis project consists in the development of a new recombinant antibody library format combining the power of phage display selection with functional screening in a whole IgG format produced in eukaryotic cells. This new system is based on hybrid promoter and signal peptide regions allowing expression both in prokaryotic and eukaryotic cells, and a site-specific recombination event that exchanges the Fab between the display vector and the chromosome of an especially developed mammalian cell line resulting in the secretion of a monoclonal human antibody by the cell. The usual approach of recloning one by one from E.Coli vector to an IgG format is no more needed since it is done directly by transfection. This new system makes possible to couple selection by phage display with a direct functional screening of a large population of human monoclonal clones

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Lien, Ting-Ya, et 連亭雅. « Selection of Monoclonal Antibody Against Recombinant Grb2-SH2 Domain ». Thesis, 2014. http://ndltd.ncl.edu.tw/handle/bzuekd.

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碩士
國立中興大學
生命科學院碩士在職專班
102
Cancer was the leading cause of death in Taiwan. Breast cancer was the most prevalent cancer in female. Clinical breast cancer therapies include surgery, chemical and radial therapy. Several drugs were used for chemical therapy, however, these drug treatments have many side effects, even leading to some other cancers development. The drug with low side effect is needed to avoid these side effects. Antibody, from the immune system?has high specificity to a candidate specific cell or a molecul and becomes a potential drug for targeted therapy. Cancer development comes from abnormal growth mechanism from normal cells. According to previous study, Grb2 protein (Growth factor receptor-bound protein 2) with SH2 domain (Src-homology 2 domain) was connected to cancer cell proliferation. In this study, we tried to acquire a SH2 domin specific antibody to prevent cancer cell abnormal growth. MCF-7 cell was used and its genome was served as template to amplified Grb2 gene SH2 domain fragment to further insert this DNA fragment into expression plasmid. SH2 domain fragment of Grb2 was expressed in E.coli expression system. Expressed protein was gathered as antigen to immune the mouse. After elevated immune response, mice were screened and sacrifice to obtain antibody in sera. The B Cells were fused with NS1 myeloma cells to produce hybridoma. We got 2 limes of SH2 antibody producing hybridoma after the monoclonal selection. The 6H3 antibody was highly specific to SH2 protein and will be use to enginerring for scFv drug development in the future.

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Livres sur le sujet "Recombinant monoclonal antibody"

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Oehlrich, Marcus. Recombinant monoclonal antibody trastuzumab for the treatment of metastatic breast cancer with tumors overexpressing the HER2-neu proto-oncogene : A systematic review. Berlin : dissertation.de, 2003.

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Chapitres de livres sur le sujet "Recombinant monoclonal antibody"

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Davies, Sarah L., et David C. James. « Engineering Mammalian Cells for Recombinant Monoclonal Antibody Production ». Dans Cell Engineering, 153–73. Dordrecht : Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-2245-5_8.

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Ubah, Obinna, et Soumya Palliyil. « Monoclonal Antibodies and Antibody Like Fragments Derived from Immunised Phage Display Libraries ». Dans Recombinant Antibodies for Infectious Diseases, 99–117. Cham : Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-72077-7_6.

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Kolb, Andreas F., Monika Lechermaier, Angehen Heister, Atiye Toksoy et Stuart G. Siddell. « Isolation and Recombinant Expression of an MHV-JHM Neutralising Monoclonal Antibody ». Dans Advances in Experimental Medicine and Biology, 657–64. Boston, MA : Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_85.

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Dorn-Beineke, Alexandra, Stefanie Nittka et Michael Neumaier. « Technology and Production of Murine Monoclonal and Recombinant Antibodies and Antibody Fragments ». Dans Animal Cell Biotechnology, 93–121. Totowa, NJ : Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-399-8_3.

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Boggiano, T., A. Fernandez, C. Hermida, J. Villán, E. Ojito, Y. Hidalgo, M. Arias et J. Gomez. « Study for the Production of a Recombinant Monoclonal Antibody in Stirred Tank ». Dans Animal Cell Technology, 435–40. Dordrecht : Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5404-8_69.

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Prachasuphap, Apichai, Chaivat Kittigul, Patcharee Sunthoranandh, Panadda Dhepakson, Nongluk Buddhirakkul et Kruavon Balachandra. « Construction of recombinant monoclonal antibody against hepatitis b surface antigen by phage display ». Dans Animal Cell Technology : Basic & ; Applied Aspects, 227–32. Dordrecht : Springer Netherlands, 2006. http://dx.doi.org/10.1007/1-4020-4457-7_31.

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Kelley, Brian, Robert Kiss et Michael Laird. « A Different Perspective : How Much Innovation Is Really Needed for Monoclonal Antibody Production Using Mammalian Cell Technology ? » Dans New Bioprocessing Strategies : Development and Manufacturing of Recombinant Antibodies and Proteins, 443–62. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/10_2018_59.

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Inoue, Y., S. Kawamoto, S. Shirahata, K. Teruya, H. Tachibana, L. B. López, K. Seki et al. « Production of Recombinant Human Monoclonal Antibody Using Hyper Producing BHK-21 Cells in Protein-Free Medium ». Dans Animal Cell Technology : Basic & ; Applied Aspects, 179–83. Dordrecht : Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5746-9_28.

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Makimoto, Yutaka, Eiji Takahashi et Hiroshi Takasugi. « Relationship Between Cell Cycle Phases and Monoclonal Antibody Production in Microcarrier Perfusion Culture of Recombinant CHO Cells ». Dans Animal Cell Technology : Basic & ; Applied Aspects, 103–7. Dordrecht : Springer Netherlands, 2002. http://dx.doi.org/10.1007/978-94-017-0728-2_19.

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Kawatsu, K., Y. Ushio, K. Tsukiguma, Y. Ishikawa et H. Yokote. « An Engineering Method to High Yielding Production of Recombinant Anti-HIV Monoclonal Antibody Using Generic Multi Feed Fermentation ». Dans Animal Cell Technology : Basic & ; Applied Aspects, 191–95. Dordrecht : Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0726-8_33.

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Actes de conférences sur le sujet "Recombinant monoclonal antibody"

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Muzychenko, B. A., et Ya I. Melnikova. « IMMUNOCHEMICAL CHARACTERISTICS OF FRAGMENTS OF ANTIBODIES TO FERRITIN ». Dans SAKHAROV READINGS 2022 : ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2022. http://dx.doi.org/10.46646/sakh-2022-2-128-131.

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In this study, the antigen-binding properties of several scFv fragments of the HSF 102 monoclonal antibody were analyzed, which can be used to optimize protocols for creating recombinant monoclonal antibodies and their fragments with different linker peptide lengths.

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Quertermous, T., J. M. Schnee, M. S. Runge, G. R. Matsueda, N. W. Hudson, J. G. Seidman et E. Haber. « EXPRESSION OF A RECOMBINANT ANTIBODY-TARGETED THROMBOLYTIC MOLECULE ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644616.

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We have recently shown that targeting tissue-type plasminogen activator (t-PA) by covalent linkage to a fibrin-specific monoclonal antibody (59D8) produces a more potent thrombolytic agent which also induces less fibrinogenolysis. A recombinant molecule encoding a t-PA-59D8 fusion protein was constructed to provide a ready source of this agent for further study, and to allow tailoring of the active moities for maximal activity. DNA sequence coding for the 59D8 heavy chain (HC) antigen combining site was cloned from a lambdaphage library by selection with a joining region probe. Gene segments coding for this cloned HC rearrangement, the amino portion of the mouse gamma 2b HC constant region, and the catalytic B chain of t-PA were joined in the pSV2-gpt expression vector. The desired coding sequence was confirmed by nucleotide sequence analysis. The construct was transfected by electroporation into 59D8 hybridoma HC loss variants. Transfectants were screened for antifibrin antibody activity. Positive clones were shown to produce mRNA which hybridized to the human t-PA gene in Northern blot analysis. Supernatants from 5 of these clones were subjected to affinity chromatography on a synthetic fibrin-like peptide-Sepharose column followed by a benzamidine-Sepharose column. Western blots of SDS polyacrylamide gels run under reducing conditions revealed binding to a 60 kd band by a monoclonal antihuman t-PA antibody, consistent with a 59D8 HC-t-PA fusion protein. Also, binding to a 25 kd band by goat anti-mouse Fab indicated the presence of 59D8 light chain. Affinity purified protein was shown to have amidolytic activity of similar potency to t-PA in a chromogenic substrate assay utilizing S-2288. Bifunctionality of the purified protein was demonstrated first by an assay which requires the protein to bind to immobilized fibrin and simultaneously exhibit activity in the S2288 assay, and second by simultaneous fibrin and iodinated anti-t-PA binding.

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Subiantistha, T., S. Pambudi, A. F. Rahmani, S. A. Puteri et R. Lestari. « Cloning of recombinant fab from monoclonal antibody anti-dengue NS1 induced by recombinant CHO-K1 cells into pGEM-T vector ». Dans PROCEEDINGS OF THE 4TH INTERNATIONAL SYMPOSIUM ON CURRENT PROGRESS IN MATHEMATICS AND SCIENCES (ISCPMS2018). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5132532.

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Haber, Edgar, Marchall T. Runge, Christoph Bode, Betsy Branscomb et Janet Schnee. « ANTIBODY TARGETED FIBRINOLYSIS ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643723.

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Chemical conjugates of fibrin-specificantibodies and plasminogen activators. Urokinase or tPA were linked covalently toamonoclonal antibody specific for the amino terminus of the beta chain of human fibrin (59D8) by means of the unidirectionalcross-linking reagent SPDP. The fibrinolytic potency of the conjugates at equal amidolytic activities was compared to the native plasminogen activators in an assay measuring lysis of 1251-fibrin monomer covalently linked to Sepharose CL-4B. Urokinase was least potent, tPA exhibited a 10fold increase in fibrinolysis whereas both the urokinase and tPA antibody conjugates and a urokinase-Fab conjugate were 250fold more potent than urokinase and 25 fold more potent than tPA. Enhanced fibrinolysis was fully inhibited by b peptide indicating its dependence on antigen binding. In a plasma assay conjugates of tPA orUK to antibody produced a 3.2- to 4.5-fold enhancement in clot lysis in human plasma over that of the respective unconjugated plasminogen activator. However, the UK-59D8 conjugate was only as potent as tPAalone. Antibody-conjugated tPA or UK consumed less fibrinogen, alpha 2-antiplasminand plasminogen than did the unconjugatedactivators, at equipotent thrombolytic concentrations. In a quantitative rabbit thrombolysis model, the activity of the purified conjugate was compared with that oftPA alone and that of a conjugate betweentPA and a digoxin-specific monoclonal antibody. After correction for spontaneous lysis, tPA-59D8 was shown to be 2.8 to,9.6times more potent than tPA alone. Unconjugated tPA and tPA-digoxin were equipotent.At equivalent thrombolytic concentrations, tPA-59D8 degraded less fibrinogen and consumed less alpha 2-antiplasmin than did tPA alone. These results suggest that tPA can be efficiently directed to the site of a thrombus by conjugation to an antifibrin monoclonal antibody, resulting in both more potent and more selective thrombolysis.A recombinant fusion protein comprising a fibrin-specific antibody site and theB chain of tPA. The rearranged 59D8 heavychain gene was cloned and combined in theexpression vector pSV2gpt withsequence coding for a portion of the Gamma 2b constant region and the catalytic beta chain of t-PA. This construct was transfected into heavy chain loss variant cells derived from the 59D8 hybridoma. Recombinant protein was purified by affinitychromatography and analyzed with Western blots. These revealed a 65-kD heavy chain-t-PA fusion protein that is secreted in association with the 59D8 light chain in the form of a 170-kD disulfide linked dimer. A chromogenic substrate assay showed the fusion protein to have 70 percent of the peptidolytic activity of native t-PA and to activate plasminogen as efficiently as t-PA. In a competitive binding assay, reconstituted antibody was shown to have a binding profile similar to that of native 59D8. Thus by recombinant techniques we have produced a novel hybrid protein capable of high affinity fibrin binding andplasminogen activation.Chemical conjugates between a fibrin-specific and a tPA-specific antibody. A heteroantibody duplex (duplex) with specificities for both tPA and fibrin was synthesized by conjugating iminothiolane-modified anti-tPA monoclonal antibody (TCL8) toantifibrin antibody 59D8. Addition of both duplex and tPA to a plasma clot assay gave more lysis (200 units produced 23.1 lysis; 400 units, 29.5 lysis) than did tPAalone (200 units, 1.8% lysis; 400 units,19% lysis). Despite increased potency associated with duplex addition, fibrinogen and alpha-2-antiplasmin levels at equal tPA concentrations did not differ. Thus, itis possible to concentrate tPA (added separately) to the site of a thrombus in plasma using a heteroantibody duplex with specificities for both tPA and fibrin.Biosynthetically produced heteroduplexantibodies that are both fibin and tPA-specific. The bispecific antibodies were prepared in two ways. First, polyethylene glycol-mediated fusions were performed with two different hybridoma cell lines: anti-fribrin b chain producer, 59D8 and anti-tPA producer, TCL8. TCL8 cells were selected for HPRT-minus variants and then fused with TK-deficient 59D8 cells. One cell line, F36.23, possessed both anti-human fibrin and anti-human t-PA immunoreactivities. A second method yielded another bispecific antibody, F32.1. This cell line was selected after fusing TCL8 (HPRT-minus) cells with spleen cells from a mouseimmunized with a fibrin-like peptide corresponding to the amino terminus of fibrinalpha-chains. Affinity-purified F32.1 andF36.23 retained anti-fibrin and anti-t-PAactivity and enhanced fibrinolytic potency of tPA by a factor of 10.

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Pancham, N., M. Dumas, J. Brown, T. C. Michaud et W. J. Knowles. « SYNTHETIC PEPTIDE ANTIBODIES RECOGNIZE PLASMA AND RECOMBINANT FVIII ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644027.

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Monoclonal antibodies were raised against synthetic peptides corresponding to the N-termini of the 90kd and 80kd subunits of human FVIII. Preliminary screening was performed directly against the peptides (linked to albumin) coated onto polystyrene wells. IgG was purified by Protein A-Sepharose and affinity purified using the immunogen peptides linked to Sepharose. Immunoreactivity with both plasma and recombinant FVIII was compared by Western blotting, two-site ELISA employing a neutralizing rabbit anti-FVIII IgG as capture antibody, and inhibition in a fluid phase FVIII activity assay. None of the antibodies neutralized clotting or amidolytic activities associated with either FVIII protein. All of the antibodies immunoblotted intacl or thrombin digested FVIII polypeptides according to their anticipated epitope recognition sites; this was useful in determining identity between the two types of FVIII protein. Furthermore, when either FVIII protein was bound to polyclonal IgG coated onto polystyrene microtiter wells, the 80kd antipeptide antibody was capable of detecting both antigens with equal affinity. These results, coupled with results using the 90k antipeptide suggest that epitope accessibility for these antipeptide antibodies is the same for plasma and recombinant FVIII under the conditions tested.

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Ny, T., L. Hansson et B. Åstedt. « ISOLATION OF cDNA FOR TYPE-2 PLASMINOGEN ACTIVATOR INHIBITOR ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642855.

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The placental type plasminogen activator inhibitor (PAI-2) has been purified from extracts of human placenta and from a histiocytic lymphoma cell line. It is mainly an uPA inhibitor but it also inhibits the two-chain form of tPA.In order to determine the factors regulating PAI-2 gene expression and thereby clarify the physiological role of PAI-2 we have undertaken the molecular cloning of PAI-2 cDNA. A λgt11 expression library prepared from placental mRNA, was screened, immunologically using a monoclonal antibody probe developed against PAI-2 purified from human placenta. When 1.7×105 recombinant phages were screened six positive clones were obtained. Hybridization experiments and comparison of restriction enzyme cleavege pattern revealed that the DNA inserts of the six clones were, related. To identify the clones as coding for PAI-2, a lysogen made from one of them was induced, and the proteins were separated by SDS-PAGE. In immuno-blotting wxperiments the recombinant fusion protein and purified PAI-2 were recognized by the monoclonal antibody and a monospecific polyclonal antibody against PAI-2, revealing an immunological similarity. The nucleotide sequence of the largest cDNA was determined. It was found to code for a protein with extensive sequence homology with members of the serine protease inhibitor family (serpins) Alignment of the active center region with other serpins indicates that PAI-2 is an arg-serpin, as expected for an inhibitor of plasminogen activators.

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Puteri, S. A., S. Pambudi, A. F. Rahmani, T. Subiantistha et R. Lestari. « Cloning of recombinant fab from monoclonal antibody anti-dengue NS1 induced by Saccharomyces cerevisiae in Escherichia coli TOP10 ». Dans PROCEEDINGS OF THE 4TH INTERNATIONAL SYMPOSIUM ON CURRENT PROGRESS IN MATHEMATICS AND SCIENCES (ISCPMS2018). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5132530.

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Pedersen, Mikkel W., Helle J. Jacobsen, Thomas T. Poulsen, Per J. Meijer et Michael Kragh. « Abstract 4562 : Superior targeting of the human epidermal growth factor receptor 2 (HER-2) with recombinant monoclonal antibody mixtures ». Dans Proceedings : AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011 ; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4562.

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Uzan, G., A. Lajmanovich, M. H. Prandini, Ph Frachet, A. Duperray et G. Marguerie. « MOLECULAR CLONING OF PLATELET GPIIb FROM HEL CELLS AND HUMAN MEGAKARYOCYTES ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643960.

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Platelet GP IIb-IIIa is an heterodimer which functions as a receptor for fibrinogen, fibronectin and Von Willebrand factor and is implicated in platelet adhesive reactions. To study the structure function relationship of this glycoprotein, a recombinant DNA approach was initiated. cDNA expression libraries were constructed in » gtll vector, from erythro-leukemia cells (HEL) and megakaryocytes mRNA. The human megakaryocytes were isolated from patients with chronic myeloid leukemia. The HEL library was initially screened with polyclonal antibodies anti GPIIb IIIa. One clone, λIIbI, containing a 1.65 kbp insert reacted with a panel of different polyclonal antibodies anti GPIIb IIIa and a monoclonal antibody anti GPIIb. To further characterize this clone the synthesis of the fusion protein was induced by IPTG. The bacterial protein was then blotted onto nitro cellulose and incubated with antisera anti GPIIb-IIIa. Antibodies that specifically bound with the fusion protein were eluted and tested on platelet membrane extracts. The selected antibodies produced a positive signal at the GPIIb position similar to the signal produced by the monoclonal antibody anti GPIIb on the same membrane extract. Finally on western blotting, a protein of Mr= 170kD reacted with the monoclonal antibody anti GPIIb. λIIbI insert was used to screen the megakaryocyte library and 3 clones, λIIb2,λIIb3 and λIIb4 were isolated. The size of HEL cells and megakaryocytes GPIIb mRNA was estimated by northern blotting. Only one species of 3.9 kb was identified in both cells. The four different clones accounted for 50% of the coding sequence of this mRNA.Sequencing of these cDNAs indicated that the plasmatic domain of GPIIb contains a cystein rich region. The sequence of these clones will allow the study of the adhesines genetic diversity in different cellular systems.

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Piérard, L., P. Jacobs, D. Gheysen, M. Hoylaerts, A. Cravador, A. Herzog, D. Collen et A. Bollen. « MUTANT AND CHIMAERIC RECOMBINANT PLASMINOGEN ACTIVATORS ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643942.

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In order to produce plasminogen activators (PA) more specific and more active than their natural counterparts, we designed recombinant genes encoding mutant forms of urokinase (u-PA) and chimaeric molecules combining fragments of tissue type plasminogen activator (t-PA) and of u-PA. The following constructs have been realized : 1°) u-PA where amino acids Arg156 and Lys158 have been replaced by Thr. The purpose of this approach was to obtain a prourokinase molecule displaying similar properties as the natural single chain urokinase (scu-PA) but resistant to the cleavage by plasmin ; 2°) u-PA where the second cleavage site, Lys135-Lys136, was also eliminated either by replacing amino acid 132 to amino acid 147 by a shorter link (Ser-Thr) as found in t-PA, or by replacing the two lysines by glutamine residues. The resulting molecules correspond thus to completely uncleavable scu-PA forms ; 3°) an hybrid composed of the finger domain of t-PA and of the B-chain of u-PA ; 4°) an hybrid made of the A-chain of t-PA and of the B-chain of u-PA ; 5°) an hybrid where the kringle 2 of t-PA has been inserted between the kringle domain and the B-chain of u-PA. The last three constructs have been made to confer the fibrin binding specificity of t-PA to the B-chain of u-PA.All recombinant DNAs were introduced, via an expression vector, into R1610 and CosI cells. Secretion of the recombinant products was monitored by ELISA and activities were assayed in an immobilized system involving a monoclonal antibody (AAU2) raised against 33K u-PA, plasminogen and the specific chromogenic substrate S2251. In this assay, all recombinant products, except the plasmin resistant (156-158) scu-PA, showed apparent specific activities comparable to the activity of natural two-chain u-PA. Potential interest of these new plasminogen activators in therapy will be discussed and further characterization of the new molecules will-be presented.

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Rapports d'organisations sur le sujet "Recombinant monoclonal antibody"

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Chan, Eva. Expression and Purification of Recombinant Protein to Generate a Monoclonal Antibody to the PX domain of Tks5 ? Isoform in Cancer Cells. Portland State University Library, janvier 2016. http://dx.doi.org/10.15760/honors.323.

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McElwain, Terry, Eugene Pipano, Guy Palmer, Varda Shkap, Stephen Hines et Douglas Jasmer. Protection of Cattle Against Babesiosis : Immunization with Recombinant DNA Derived Apical Complex Antigens of Babesia bovis. United States Department of Agriculture, juin 1995. http://dx.doi.org/10.32747/1995.7612835.bard.

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Bovine babesiosis caused by Babesia bovis continues to be a significant deterrent to global livestock production. Current control methods have both biological and technical drawbacks that have stimulated research on improved methods of vaccination. This BARD project has focused on characterization of candidate Babesia bovis vaccine antigens located in the apical complex, a unique group of subcellular organelles - including rhoptries, micronemes, and spherical bodies - involved in the invation of erythrocytes. Spherical bodies and rhoptries were partially purified and their contents characterized using monoclonal antibodies. Existing and newly developed monoclonal antibodies bound to antigens in the spherical body, rhoptry, merozoite membrane, and infected erythrocyte membrane. In an initial immunization study using biologically cloned strains, it was demonstrated that strain-common epitopes are important for inducing immune protection against heterologous challenge. Rhoptry-associated antigen 1 (RAP-1) had been demonstrated previously to induce partial immune protection, fulfilled criteria of broad interstrain B and T cell epitope conservation, and thus was further characterized. The RAP-1 gene family consists of at least two gene copies, is homologous to the RAP-1 gene family in B. bigemina, and contains significant sequence similarity to other erythroparasitic protozoan candidate vaccine antigens, including the apical membrane antigen of Plasmodium falciparum. A new RAP-1 monoclonal antibody was developed that inhibits merozoite growth in vitro, demonstrating the presence of a RAP-1 neutralization sensitive domain. Based on these observations, cattle were immunized with Mo7 (Mexico) strain recombinant RAP-1 representing one of the two gene copies. All cattle responded with variable levels of serum antibodies inhibitory to heterologous Israel strain merozoite growth in vitro, and RAP-1 specific T lymphocytes that proliferated when stimulated with either homologous or heterologous native parasite antigen. Minimal protection from clinical disease was present after virulent Israel (heterologous) strain B. bovis challenge. In total, the results support the continued development of RAP-1 as a vaccine antigen, but indicate that additional information about the native structure and function of both RAP-1 gene copies, including the relationship of conserved and polymorphic sequences to B and T cell lepitopes relevant for protection, is necessary for optimization of RAP-1 as a vaccine component.

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