Добірка наукової літератури з теми "Antibody avidity"

Fard, Amir Hossein Mohagheghi. Positivity for and avidity of human herpesviruses IgG antibody determined by ELISA. Manchester: University of Manchester, 1996.

Bristow, Michelle A. Measurement of antibody avidity for hepatitis B virus. 1996.

Lyons, Marie. The development of a redioimmunoassay for use in antibody avidity measurements in the diagnosis of human herpesvirus-6 infections. 1995.

Bruderer, U., E. Fürer, S. J. Cryz, and A. B. Lang. "The Role of Human Monoclonal Antibody Specificity and Avidity in the Protection Against Gram-negative Bacteria." In Immunotherapeutic Prospects of Infectious Diseases, 373–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-76120-1_50.

Dakshinamurti, Krishnamurti, and Edward S. Rector. "[12] Monoclonal antibody to biotin." In Avidin-Biotin Technology, 111–19. Elsevier, 1990. http://dx.doi.org/10.1016/0076-6879(90)84266-j.

KOSTULAS, V., T. OLSSON, and H. LINK. "Detection of Oligoclonal IgG in Unconcentrated Cerebrospinal Fluid by Agarose Isoelectric Focusing and Double Antibody Avidin–Biotin-Peroxidase." In Protides of the Biological Fluids, 171–74. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-08-031739-7.50044-6.

Shively, John E., Christoph Wagener, and Brian R. Clark. "[43] Solution-phase RIA and solid-phase EIA using avidin-biotin systems for analysis of monoclonal antibody epitopes and affinity constants." In Immunochemical Techniques Part I: Hybridoma Technology and Monoclonal Antibodies, 459–72. Elsevier, 1986. http://dx.doi.org/10.1016/0076-6879(86)21045-9.

"from CD99 high expressors but membranes from CD99 low expressors required exposure of 5 minutes before the 32 kD band was apparent [50]. Unfortunately, these tests gave no information about the Xga protein because the position of the Xga band was masked by the antibody light chain which became labelled. However, a 32 kD band was seen in the Xga-immunoprecipitate from Xg(a+) but not from Xg(a-) cells [50]. It has not yet been proved that this is the CD99 protein because this band was not stained by immunoblotting Xga-immunoprecipitates with 12E7. The luciferin-enhanced luminescent proceedure to detect the avidin-biotin label is very much more sensitive than immunoblotting. Our results support the theory that Xga and CD99 may be associated in the membrane. Cloning of the XG gene will increase our understanding of this relationship. The important blood group genes have been cloned but two big problems remain, regulation on antigen expression and the function of blood group polymorphisms. Rare phenotypes should still be studied because they will contribute to unravelling the mechanisms responsible for the polymorphisms. The wealth of serological information which continues to increase includes many examples of variable expression of red cell antigens. Some antigens do not show the same variation on other cells suggesting that some modes of regulation may be limited to red cells. Association of blood group antigens with proteins of known function and identification of red cell antigens on cells other than red cells will contibute to understanding the functions of the blood group polymorphisms. REFERENCES 1. P.L. Mollison, C.P. Engelfreit and M. Contreras, Blood Transfusion in Clinical Medicine. Blackwell Scientfic Publications, Oxford (1993). 2. M. Lewis (Chairman) et al, Vox Sang., 61_, 158-160 (1991). 3. G.L. Daniels, J.J. Moulds (chairman) et al, Vox Sang., 65, 77-80 (1993). 4. A.C. Petty, J. Immunol. Meth., 161. 91-95 (1993). 5. J. M. Moulds, in Immunobiology of Transfusion Medicine. G. Garratty ed. Marcel Dekker. Inc., New York, (1994) pp. 273-297. 6. J.M. Moulds, M.W. Nickells, J.J. Moulds, M.C. Brown and J.P. Atkinson, J. Exp. Med., 173, 1159-1163 (1991). 7. N. Rao, D.J. Ferguson, S-F. Lee and M.J. Telen, J. Immun., 146, 3502-3507 (1991). 8. A.C. Petty, (abs) Transfusion Medicine 3 Suppl 1, 84 (1993). 9. J.M. Moulds, J.J. Moulds, M. Brown and J.P. Atkinson, Vox Sang. 62, 230-235 (1992)." In Transfusion Immunology and Medicine, 198. CRC Press, 1995. http://dx.doi.org/10.1201/9781482273441-16.

"designation will be used for the 12E7 antigen. CD99 was first detected by 12E7, a monoclonal antibody made in response to a T-cell line, and was initially thought to be a ‘thymus-leukaemia’ marker antigen [41]. Many similar antibodies were made which reacted with different epitopes of the same molecule [see 42]. Independently, CD99 was identified as E2, a T-cell adhesion molecule, and as a marker antigen for Ewing’s tumours [see 40]. CD99 is expressed on many tissues including red cells. By somatic cell hybridization and biochemical studies, Goodfellow and his colleagues have shown that MIC2, the structural locus encoding the 12E7 antigen, is located on the short arm of the X chromosome and on the short arm of the Y chromosome within the pairing regions [43]. MIC2 has been cloned [44]. XG is X-borne. On red cells, CD99 expression is a quantitative polymorphism [45]. Family studies proved that this polymorphism is also caused by regulator genes on X and Y chromosomes. XG appears to be the regulator on the X [46]. There is variation in CD99 expression on cells other than red cells. In a recent publication, CD99 was found on all haemopoeitic cells but was variably expressed during leucocyte differentiation [40]. Use of different monoclonal antibodies and variability of expression during maturation offered an explanation for the previous apparently contradictory findings by different laboratories. Both Xga and CD99 are sialoglycoproteins [47,48,49]. These glycoproteins differ in Mr and in their sialic acid content [49]. Immunostaining of separated membrane components with 12E7 and similar antibodies had demonstated that the MIC2 gene product was a 30-32 kD protein. 12E7 also bound to an intracellular band of 28 kD which was found in mouse cell lines in addition to human cell lines, platelets, lymphocytes and red cells but it was not encoded by the MIC2 gene [47]. Immunoblotting assays have shown that Xga was associated with two diffuse bands of 22-25 kD and 26.5-29 kD [49]. These findings supported the evidence that Xga and CD99 were products of different structural loci. However, XG appears to regulate CD99 expression on red cells and Latron and colleagues found that purified CD99 protein inhibited binding of 12E7 and of anti-Xga to red cells [48]. We have studied the immunochemical relationship of Xga and CD99 [50]. One approach was immunoprecipitation of membrane components from biotin labelled cells. Bands are detected by chemiluminescence via peroxidase-conjugated avidin. The 32 kD protein of CD99 was visualised by this technique and the quantitative polymorphism was also demonstrated since the 32 kD band is seen on X-ray film after 2 minutes in membranes." In Transfusion Immunology and Medicine, 197. CRC Press, 1995. http://dx.doi.org/10.1201/9781482273441-15.

Friess, Thomas, Stefanie Lechner, Esther Abraham, Ann-Marie Broeske, Sabine Bader, Andreas Roller, Meher Majety, et al. "Abstract 952: Induction of avidity-driven hyperclustering of DR5 by a new FAP-DR5 bispecific antibody (RG7386) leads to strong anti-tumor efficacy." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-952.

Deak, Laura Laura Codarri, Stefan Seeber, Mario Perro, Patrick Weber, Laura Lauener, Standford Chen, Sonja Offner, et al. "Abstract 2270: RG7769 (PD1-TIM3), a novel heterodimeric avidity-driven T cell specific PD-1/TIM-3 bispecific antibody lacking Fc-mediated effector functions for dual checkpoint inhibition to reactivate dysfunctional T cells." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-2270.

Narang, Upvan, George P. Anderson, Keeley D. King, Heidi S. Liss, and Frances S. Ligler. "Enhanced biosensor performance using an avidin-biotin bridge for antibody immobilization." In BiOS '97, Part of Photonics West, edited by Richard B. Thompson. SPIE, 1997. http://dx.doi.org/10.1117/12.273534.

Meyers, K. M., K. J. Wardrop, C. M. Helmick, and F. P. White. "PRESENCE OF VWF IN VASCULAR ENDOTHELIUM BUT NOT PLATELETS FROM CONTROL DOGS AND VIIIR:AG-DEFICIENT DOGS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644501.

Risberg, B., G. K. Hansson, E. Eriksson, and B. Wiman. "IMMUNOHISTOCHEMICAL LOCALIZATION OF PLASMINOGEN ACTIVATOR INHIBITOR (PAI) IN TISSUE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644443.

Mathew, Trupthi, Punarvasu Joshi, Shalini Prasad, Michael Goryll, Andreas Spanias, and Trevor J. Thornton. "Silicon Based Pore Systems for Emerging Biosensor Applications." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-11707.

Tomaslni, B. R., and D. F. Mosher. "PREFERENTIAL RECOGNITION OF VITRONECTIN (S-PR0TEIN) BY A MONOCLONAL ANTIBODY UPON INTERACTION WITH THROMBIN, ANTITHROMBIN AND GLYCOSAMINOGLYCANS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643634.

Hirai, K., K. Yasunaga, and R. Ryo. "STUDIES ON PLATELET ANTIGENS AGAINST SERA FROM PATIENTS WITH ITP." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644583.

Rodríguez, José A., Héctor E. López-Valdes, Gustavo F. Helguera, Sokuntheavy So, Rosendo Luria-Pérez, Tracy R. Daniels, Andrew C. Charles, and Manuel L. Penichet. "Abstract 4456: Molecular events required for the induction of lethal iron deprivation in malignant hematopoietic cells via an antibody-avidin fusion protein specific for human transferrin receptor 1." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4456.

Grøndahl-HANSEN, J., N. Agerlin, L. S. Nielsen, and K. Danø. "SENSITIVE AND SPECIFIC ENZYME-LINKED IMMUNOSORBENT ASSAY FOR UROKINASE-TYPE PLASMINOGEN ACTIVATOR IN HUMAN PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644425.