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Kosmas, C., H. Kalofonos, and A. A. Epenetos. "Monoclonal Antibodies." Drugs 38, no. 5 (November 1989): 645–57. http://dx.doi.org/10.2165/00003495-198938050-00001.
Nowak, Thomas P. "Monoclonal Antibodies." American Journal of Clinical Oncology 10, no. 4 (August 1987): 278–80. http://dx.doi.org/10.1097/00000421-198708000-00002.
Ghobrial, Rafik M., Ronald W. Busuttil, and Jerzy W. Kupiec-Weglinski. "Monoclonal antibodies." Current Opinion in Organ Transplantation 2, no. 1 (October 1997): 82–88. http://dx.doi.org/10.1097/00075200-199710000-00015.
Rosen, Steven T., Elyse A. Lambiase, Yixing Ma, James A. Radosevich, and Alan L. Epstein. "Monoclonal antibodies." Postgraduate Medicine 77, no. 4 (March 1985): 129–34. http://dx.doi.org/10.1080/00325481.1985.11698922.
Plumpton, Christopher. "Monoclonal antibodies against phytochrome." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358677.
Benjamin, Richard John. "Tolerance induction with monoclonal antibodies." Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253988.
Qin, Shi-Xin. "Transplantation tolerance with monoclonal antibodies." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305697.
Heron, Andrew David. "The stability of monoclonal antibodies." Thesis, University of Glasgow, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252169.
Isaacs, John Dudley. "Improving serotherapy with monoclonal antibodies." Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386115.
Master of Science Department of Physics Jeremy D. Schmit Antibodies are large Y-shaped proteins which are used by immune system to identify and neutralize pathogens. Monoclonal antibody therapy is used to treat different patient conditions. There are problems associated with the manufacturability and deliverability of mAb solutions due to the viscous nature of the protein. The viscosity of antibody solutions increases with the increase in concentration and decreases with applied shear. We want to know why these behaviours are seen and to address this problem we have developed a theory describing the rapid viscosity increase with increasing concentration. We use the polymer theory to explain this behaviour. Here antibodies are treated as polymers. The length of the polymer depend on the aggregation. The reptation time increases approximately as the cubic power of size of aggregate (N³ ). We see the shear thinning behaviour is dependent on the Ab-Ab binding energy and find the relationship between the size of the aggregate
and the binding energy. We find aggregate size and morphology using several models for Ab-Ab interaction sites. We use the head to head binding (fAb-fAb binding) model to describe aggregation state in our viscosity theory. The size of the aggregate and hence the reptation time is captured by the binding energy. When the binding energy increases the zero shear viscosity increases and the reptation time decreases. Likewise when the binding energy decreases the zero shear viscosity decreases and the reptation time increases. We have yet to find the correct exponents for the shear thinning behaviour of different mAbs which would be our future work.
Alexandrovich, Susan K. "Characterization of monoclonal antibodies against digoxin /." Online version of thesis, 1987. http://hdl.handle.net/1850/10681.
The available antibodies against CFTR are not sensitive enough to detect CFTR at endogenous or near endogenous levels making detection at native levels difficult. We raised two monoclonal antibodies, 22E8 and 23C5, against the R domain of human CFTR with the goal of identifying an antibody sensitive enough to detect CFTR in native airway cells. These antibodies were characterized for their ability to detect over-expressed as well as endogenous levels of CFTR in immunoblotting, immunoprecipitation and immunofluorescence. Their ability to detect CFTR was also compared with commercial antibodies M3A7 and 24-1. We show that 23C5 and 22E8 are more sensitive than the commercial antibodies and are able to detect CFTR in over-expressed and endogenous cells by immunoblotting. However, only 23C5 is able to immunoprecipitate CFTR and neither is able to detect CFTR in native airway cells by immunoblotting or are suitable for immunofluorescence. These antibodies will enable studies of CFTR biogenesis in endogenous cells. A l'heure actuelle les anticorps dirigés contre la protéine CFTR ne sont pas suffisamment sensibles pour détecter cette protéine de facon endogène rendant ainsi l'étude de cette protéine difficile dans les tissus. Notre laboratoire a fabriqué deux anticorps monoclonaux , nommés 22E8 et 23C5, dirigés contre le domaine R de la protéine CFTR. L'abilité de ces anticorps à détecter l'expression de CFTR que ce soit de façon endogène ou lorsque la protéine est surexprimée a été testée à l'aide des techniques d'immunoblotting, d'immunoprécipitation et d'immunofluorescence. Afin de verifier leur sensibilité et leur capacité à détecter la protéine CFTR, ces anticorps ont été comparés aux anticorps M3A7 et 24-1 qui sont disponibles dans le commerce et connus pour détecter de facon optimale la protéine CFTR. Les resultats obtenus dans les lignées cellulaires à l'aide de la technique d'immunoblotting ont permis de montrer que les anticorps 23C5 et 22E8 sont plus sensibles que les anticorps commerciaux, de plus ils sont capables de détecter à la fois les protéines endogènes et sur-exprimées. Bien que l'anticorps 23C5 soit capable d'immunoprécipiter la protéine CFTR, aucun des deux anticorps n'a permis la detection de la protéine CFTR par immunoblotting dans les cellules de culture primaire. De plus, ces anticorps n'ont pas permis la detection de la protéine CFTR par immunofluorescence. Ainsi l'utilisation de ces anticorps nous donnera l'opportunité d'étudier la protéine CFTR dans les cellules l'exprimant de facon endogène afin de mieux comprendre sa regulation et son traffic.
Borrebaeck, Carl A. K., and James W. Larrick, eds. Therapeutic Monoclonal Antibodies. London: Palgrave Macmillan UK, 1990. http://dx.doi.org/10.1007/978-1-349-11894-6.
Peters, J. H., and D. Baron. "Introduction." In Monoclonal Antibodies, 1–17. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_1.
Peters, J. H., M. Schulze, M. Grol, S. Schiefer, H. Baumgarten, J. Endl, H. Xu, et al. "Demonstration of Monoclonal Antibodies." In Monoclonal Antibodies, 316–461. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_10.
Baron, D. "Safety Precautions at Work." In Monoclonal Antibodies, 463–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_11.
Peters, Johann Hinrich, and Horst Baumgarten. "Appendix." In Monoclonal Antibodies, 466–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_12.
Wiggenhauser, A., J. H. Peters, and H. Baumgarten. "Preconditions for Hybridoma Technology." In Monoclonal Antibodies, 18–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_2.
Baumgarten, H., M. Schulze, J. H. Peters, and T. Hebell. "Immunization." In Monoclonal Antibodies, 39–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_3.
Wiggenhauser, A., J. H. Peters, H. Baumgarten, and A. Borgya. "Taking Blood and Isolating Cells." In Monoclonal Antibodies, 71–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_4.
Peters, J. H., E. Debus, H. Baumgarten, R. Würzner, M. Schulze, and Helga Gerlach. "Cell Culture." In Monoclonal Antibodies, 88–136. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_5.
Baron, D., J. H. Peters, R. K. H. Gieseler, S. Lenzner, H. Baumgarten, R. Würzner, B. Goller, and Th Werfel. "Production of Hybridomas." In Monoclonal Antibodies, 137–222. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_6.
Baumgarten, H., R. Franze, J. H. Peters, A. Borgya, D. Baron, E. Debus, and M. Kubbies. "Mass Production of Monoclonal Antibodies." In Monoclonal Antibodies, 223–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_7.
Тези доповідей конференцій з теми "Antibodies, Monoclonal":
1
Kiefel, V., S. Santoso, and C. Mueller-Eckhardt. "ANALYSIS OF PLATELET REACTIVE ANTIBODIES USING MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643929.
The characterization of platelet reactive alloantibodies and autoantibodies is mandatory for the diagnosis of posttransfusion purpura, neonatal alloimmune thrombocytopenia, autoimmune thrombocytopenia and for the selection of platelet donors prior to platelet transfusions in immunized polytransfused patients. The platelet immunofluorescence test is suitable for the detection of platelet reactive antibodies. In many cases, however, mixtures containing different platelet reactive antibodies have to be dissected.In order to analyze these sera, we have developed a novel enzyme immunoassay based upon monoclonal antibody specific immobilization of platelet antigens (MAIPA). In brief, platelets are incubated simultaneously with the (human) serum to be investigated and a monoclonal (mouse) antibody directed against an epitope on the same platelet membrane glycoprotein (GP). Platelets are then washed and solubilized in TRIS buffered saline containing NP40. The lysed platelets are then pipetted into the wells of microtiter plates, coated with goat anti mouse IgG where mouse anti GP-complexes are immobilized. Human platelet reactive antibodies on the same GP are detected using enzyme labelled goat anti human IgG, IgM, or IgA, respectively. Using mab Gi5, mab FMC25, mab w6.32 directed against epitopes on the glycoprotein complex IIb/IIIa, glycoprotein Ib and HLA class I molecule, respectively, and a panel of typed platelet donors, even sera containing different platelet reactive antibodies are readily analyzed. Results of experiments with platelet specific alloantibodies (anti P1A1, anti P1A2 and anti Bak(a)), autoantibodies (against the GP Ilb/IIIa complex and GP Ib) and a drug dependent antibody show that this assay allows to discriminate all these different platelet reactive antibodies.
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Yang, Wu, Li-ming Wang, Zhao Wei, and Yuan Junlin. "Preliminary Production of Anti- Glufosinate Monoclonal Antibodies." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.18.
Young, Colin R., Alice Lee, and Larry H. Stanker. "Detection of Campylobacter species using monoclonal antibodies." In Photonics East (ISAM, VVDC, IEMB), edited by Yud-Ren Chen. SPIE, 1999. http://dx.doi.org/10.1117/12.335779.
Ray, Jason C., Penelope Allen, Ann Bacsi, Julian Bosco, Luke Chen, Michael Eller, Lyndell Lim, et al. "076 Inflammatory complications of CGRP monoclonal antibodies." In ANZAN Annual Scientific Meeting 2021 Abstracts. BMJ Publishing Group Ltd, 2021. http://dx.doi.org/10.1136/bmjno-2021-anzan.76.
Metzelaar, M. J., H. K. Nieuwenhuis, and J. J. Sixma. "DETECTION OF ACTIVATED PLATELETS WITH MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643829.
Blood tests reflecting in-vivo activation of platelets are potentially useful in evaluating patients with thrombotic diseases. Recently monoclonal antibodies have been described that react preferentially with activated platelets. We prepared an IgG2b antibody, designated RUU-AP 2.28, that reacted with a 53.000 MW protein that is located in a special subclass of platelet granules in unstimulated platelets and that is exposed on the surface of activated platelets. Increased numbers of platelets that expressed the 2.28 antigen on their surface were observed in patients undergoing cardiopulmonary bypass and in patients with acute deep venous thrombosis. The percentage of RUU-AP 2.28 positive platelets in the circulation was 3,9 ± 2.7 (SD)% in the controls, (n = 20), 24.6 ± 13.5% in patients after cardiopulmonary surgery (n = 10) and 8.5% in patients with acute deep venous thrombosis (n = 2).In order to detect also earlier stages of platelet activation, such as secretion-independent phenomena, we produced new monoclonal antibodies by fusing spleen cells from Balb/c mice, immunized with thrombin stimulated, paraformaldehyde fixed platelets, with Ag 8653 myeloma cells. As a screening assay we used an ELISA with freshly fixed platelets or fixed thrombin-activated platelets. We detected six monoclonal antibodies (RUU-AP 1-6) specific for thrombin-activated platelets. The results of the ELISA were confirmed by flow cytofluorometry.None of the antibodies inhibited platelet aggregation induced by ADP, collagen or ristocetin. Ascites of IgGl antibody RUU-AP 3 reacted with normal thrombin-activated platelets but did not react with thrombin-activated platelets from a patient with Glanzmann’s disease. In addition antibody RUU-AP 3 reacted with normal platelets stimulated with 1 pM of ADP. These data suggest that antibody RUU-AP 3 detects a secretion-independent conformational change in the platelet membrane glycoprotein IIb-IIIa complex.
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Brown, Michael C., Ross Chambers, Dale V. Onisk, Tony R. Joaquim, Lewis J. Stafford, Klaus Lindpaintner, Daniel Keter, and James W. Stave. "Abstract 4325: Monoclonal antibodies to transmembrane proteins." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4325.
Hessing, Martin, Joost C. M. Meijers, Jan A. van Mourik, and Bonno N. Bouma. "MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S AND C4b-BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644291.
Protein S (PS) circulates in plasma both free and in reversible association with the complement component C4b-binding protein (C4bp). Only free PS is functional as a cofactor for activated protein C (APC). Cleavage of PS by thrombin at a site near the r-carboxyglutamic acid domain is associated with a loss of cofactor activity. This may be a control mechanism for the anticoagulant activity of APC. These observations led us to investigate the role of C4bp and thrombin in the regulation of PS. Complex formation between purified PS and C4bp was studied in plasma and in a system with purified components. 125I-labeled PS was first incubated with either C4bp or citrated plasma and then subjected to polyacrylamide gelelectrophoresis in the absence of SDS. The formation of the C4bp-PS complex in plasma and in the purified system was demonstrated by autoradiography. Crossed immuno-electrophoresis using an antiserum against PS was performed in the presence of 8 mM EDTA. Human citrated plasma showed two precipitin peaks. Free PS migrated rapidly in the first dimension, whereas the C4bp-PS complex was just anodal to the application slot. The addition of C4bp to either plasma or purified PS resulted in the disappearance of the free PS peak and an increase of the slower migrating peak. The effect of purified C4bp on the PS-cofactor function of APC was studied in citrated plasma. The prolongation of the APTT induced by the addition of APC could be inhibited by the addition of increasing amounts of C4bp. Monoclonal antibodies to PS and C4bp were prepared and characterized. The monoclonal antibodies to either PS or C4bp did not block the complex formation between and PS, as was demonstrated by dot blotting of C4bp with 125I-PS and agarose gelelectrophoresis followed by Western blotting. Three out of 7 monoclonal antibodies to PS did not detect PS after thrombin cleavage on an immunoblot after non-reduced SDS polyacrylamide gelelectrophoresis. These 3 antibodies gave a significant shortening of the prolonged APTT induced by the addition of APC to normal plasma, indicating that these monoclonals inhibited the cofactor function of PS. The other 4 monoclonals to PS that did detect PS after thrombin cleavage on an immunoblot, gave only a minor inhibition of the PS cofactor function.
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Clemetson, K. J., R. Weber, and J. L. McGregor. "TOPOLOGY OF PLATELET GPIb INVESTIGATED BY LOCATION OF MONOCLONAL ANTIBODY EPITOPES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643625.
A large number of monoclonal antibodies to platelet membrane glycoprotein lb (GPIb) have been described but for most of these the position of the epitope is not known. Since many of these influence platelet function, a better understanding of struc-ture-function relationships requires this knowledge. The position of the epitopes for the monoclonal antibodies API (Dr. T.J. Kunicki), AN51 and SZ-2 (Dr. C-G. Ruan), WM23 (Dr. M.C. Berndt) and PI were determined by analysis of proteolytic cleavage fragments of glycocalicin via affinity chromatography on the monoclonal antibodies coupled to Sepharose, elution with diethyl ami ne solution, separation on SDS-gel electrophoresis and detection by silver-staining. First, intact glycocalicin was examined and was found to bind to all monoclonals with the exception of PI. All monoclonals bound intact GPIb. WM23 bound a 70 kDa glycopeptide from the highly-glycosylated 90 kDa tryptic fragment of glycocalicin. API, AN51 and SZ-2 all bound to 45 kDa and 40 kDa, poorly glycosylated tryptic fragments. The 40 kDa fragment is derived from the 45 kDa fragment and has been shown to be the N-terminal region of GPIb. All these monoclonals have been shown to inhibit von Willebrand factor induced platelet agglutination. Platelets were treated with either elastase or calcium activated protease and monoclonal binding checked by immunofluorescence. The immunofluorescence with API, AN51 and SZ-2 was minimal compared to control platelets whereas that of PI remained as strong as the controls. This indicates that the epitope for PI lies on GPIb in a region other than glycocalicin and its absence from glycocalicin is not simply due to conformational changes in that fragment. Since PI inhibits platelet activation by thrombin and ADP it must act via conformational effects and not by blocking the thrombin receptor which lies on the 45 kDa region of glycocalicin. These results support a more complex role for GPIb in platelet activation.
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Chumak, N. S., and Y. I. Melnikova. "OBTAINING AND IMMUNOCHEMICAL TESTING OF APOFERRITIN." In 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-2022-1-289-293.
The process of direct binding of monoclonal antibodies to apoferritin immobilized on polystyrene, as well as the method of competitive interaction of monoclonal antibodies with apoferritin in solution, have been experimentally studied. It was found that the immobilization of apoferritin on a polystyrene surface leads to a change in the epitope structure of this protein and to the elimination of reactive epitopes of binding of monoclonal antibodies. The soluble form of apoferritin effectively binds to monoclonal antibodies in a competitive assay, which confirms the conformational nature of the clusters of determinants on the surface of apoferritin.
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Berkner, J. A., G. Mitra, and J. W. Bloom. "MONOCLONAL ANTIBODY BINDING TO FACTOR VIII:C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644063.
The interactions of monoclonal antibodies with highly purified Factor VIII:c have been studied utilizing the ELISA technique. ELISA plates were coated with Factor VIII:c, protein A purified monoclonal IgG was then added and bound antibody detected with peroxidase labeled antimouse IgG. A Scatchard-Sips plot approach to data analysis was used to calculate binding constants. The binding constants for four antibodies designated BD10, AD7, C7F7 and 39MH8 were as follows: BD10, KO = 7.1 x 108 M-1, n = 1.1 (moles antibody/moles ligand); AD7, KO = 3.1 x 108 M-1, n = 2.7; C7F7, KO = 3.6 x 1011M-1, n = 0.03; 39MH8, K = 6.0 x 1011 M-1, n = 0.03. The binding constants for C7F7 to the purified carboxy-terminal (residues 1649-2332) 80 kD functional region of the Factor VIII:c molecule were also determined: KO = 1.0 x 1011 M-1, n = 0.55. On the basis of these results the following conclusions can be drawn: 1) the antibodies can be divided into two groups: high affinity (suitable for use in immunopurification), C7F7 and 39MH8; low affinity: BD10 and AD7; 2) the antibodies in the low affinity group have valance values two orders of magnitude higher than the high affinity antibodies, C7F7 and 39MH8. The difference might be explained by the high affinity antibody epitopes on the immobilized Factor VIII:c being less exposed to the solution; 3) C7F7 binding to the 80 kD polypeptide, compared to the whole Factor VIII:c molecule, gave virtually identical Kc values, but dramatically different valance values. This suggests that the C7F7 epitope is more accessible on the 80 kD polypeptide.
Звіти організацій з теми "Antibodies, Monoclonal":
1
Snyder, Christopher M., and Lawrence J. Wysocki. Dissecting Immunogenicity of Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada407659.
Snyder, Christopher M., and Lawrence J. Wysocki. Dissecting Immunogenicity of Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada417364.
Jaszczak, R. J. SPECT assay of radiolabeled monoclonal antibodies. Office of Scientific and Technical Information (OSTI), February 1992. http://dx.doi.org/10.2172/7197646.
Jaszczak, R. J. SPECT assay of radiolabeled monoclonal antibodies. Office of Scientific and Technical Information (OSTI), February 1992. http://dx.doi.org/10.2172/7288347.
Chia, John K. Polymyxin B(PMB)-Specific Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada231817.
Ivy, John M. Production of Anti-Ferret IgA Antibodies; and production of monoclonal antibodies. Fort Belvoir, VA: Defense Technical Information Center, April 1994. http://dx.doi.org/10.21236/ada279534.
Sato, J. D. Receptor Monoclonal Antibodies that Inhibit Tumor Angiogenesis. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada398146.
Sato, J. D. Receptor Monoclonal Antibodies that Inhibit Tumor Angiogenesis. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada383129.
Glassy, Mark C. Neutralizing Monoclonal Antibodies against Biological Toxins. Phase 1. Fort Belvoir, VA: Defense Technical Information Center, August 1993. http://dx.doi.org/10.21236/adb176298.
Jaszczak, Ronald, J. Final Progress Report: SPECT Assay of Radiolabeled Monoclonal Antibodies. Office of Scientific and Technical Information (OSTI), September 2004. http://dx.doi.org/10.2172/886018.
