Littérature scientifique sur le sujet « Immunodiagnostic assay »
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Articles de revues sur le sujet "Immunodiagnostic assay"
SAKO, YASUHITO, SONOYO ITOH, MUNEHIRO OKAMOTO, KAZUHIRO NAKAYA et AKIRA ITO. « Simple and reliable preparation of immunodiagnostic antigens forTaenia soliumcysticercosis ». Parasitology 140, no 13 (21 juin 2013) : 1589–94. http://dx.doi.org/10.1017/s0031182013000978.
Texte intégralSilva, Miriam, Anna Santos, Leticia Rocha, Bruna Caetano, Thais Mitsunari, Luanda Santos, Juliana Polatto et al. « Development and Validation of Shiga Toxin-Producing Escherichia coli Immunodiagnostic Assay ». Microorganisms 7, no 9 (21 août 2019) : 276. http://dx.doi.org/10.3390/microorganisms7090276.
Texte intégralOgbonna, G., E. Hryhorenko, J. Parsells, S. Phonethepswath, Y. Huang, B. Smith et L. Sprague. « Performance evaluation of the VITROS® immunodiagnostic products B·R·A·H·M·S PCT assay on the VITROS 3600 immunodiagnostic system ». Clinica Chimica Acta 493 (juin 2019) : S549—S550. http://dx.doi.org/10.1016/j.cca.2019.03.1154.
Texte intégralCaceres, Diego H., et Mark D. Lindsley. « Comparison of Immunodiagnostic Assays for the Rapid Diagnosis of Coccidioidomycosis in Dogs ». Journal of Fungi 8, no 7 (13 juillet 2022) : 728. http://dx.doi.org/10.3390/jof8070728.
Texte intégralProcopiou, Michel, Hazel Finney, Scott A. Akker, Shern L. Chew, William M. Drake, Jacky Burrin et Ashley B. Grossman. « Evaluation of an enzyme immunoassay for plasma-free metanephrines in the diagnosis of catecholamine-secreting tumors ». European Journal of Endocrinology 161, no 3 (septembre 2009) : 509. http://dx.doi.org/10.1530/eje-09-0172e.
Texte intégralSako, Yasuhito, Minoru Nakao, Takashi Ikejima, Xian Zhi Piao, Kazuhiro Nakaya et Akira Ito. « Molecular Characterization and Diagnostic Value ofTaenia solium Low-Molecular-Weight Antigen Genes ». Journal of Clinical Microbiology 38, no 12 (2000) : 4439–44. http://dx.doi.org/10.1128/jcm.38.12.4439-4444.2000.
Texte intégralOgbonna, G., S. Alvey, E. Hryhorenko, J. Parsells, S. Phonethepswath et B. Smith. « M142 Analytical and clinical performance of the vitros® immunodiagnostic products B·R·A·H·M·S PCT assay on the vitros immunodiagnostic systems ». Clinica Chimica Acta 530 (mai 2022) : S268. http://dx.doi.org/10.1016/j.cca.2022.04.024.
Texte intégralCandolfi, E., R. Ramirez, M. P. Hadju, C. Shubert et J. S. Remington. « The Vitek immunodiagnostic assay for detection of immunoglobulin M toxoplasma antibodies. » Clinical and diagnostic laboratory immunology 1, no 4 (1994) : 401–5. http://dx.doi.org/10.1128/cdli.1.4.401-405.1994.
Texte intégralPrasad, B. V. Siva, Vishal Khatri, P. Suresh Yadav, M. Subhosh Chandra, D. Vijaya Lakshmi et Kalyan Goswami. « Immunodiagnostic potential ofWuchereria bancroftiL1 antigen–based filarial immunoglobulin G4 detection assay ». Transactions of The Royal Society of Tropical Medicine and Hygiene 113, no 1 (15 octobre 2018) : 36–43. http://dx.doi.org/10.1093/trstmh/try110.
Texte intégralYamasaki, Hiroshi, Takeshi Nakamura, Pewpan M. Intapan, Wanchai Maleewong, Yasuyuki Morishima, Hiromu Sugiyama, Hiroyuki Matsuoka, Kaoru Kobayashi, Katsuyoshi Takayama et Yukuharu Kobayashi. « Development of a Rapid Diagnostic Kit That Uses an Immunochromatographic Device To Detect Antibodies in Human Sparganosis ». Clinical and Vaccine Immunology 21, no 9 (2 juillet 2014) : 1360–63. http://dx.doi.org/10.1128/cvi.00149-14.
Texte intégralThèses sur le sujet "Immunodiagnostic assay"
MAZZOLENI, ELISA. « Exploration of new techniques for purification and chemo-selective conjugation of bioreagents for immunodiagnostic applications ». Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/68468.
Texte intégralAntigen and antibody are the two key reagents for an immunodiagnostic assay. Investigation of new techniques and improvement of processes such as purification and site-specific labeling of antigen and antibody molecules can promote the development of new more powerful bioreagents able of improving the performance of immunodiagnostic assays. The first part of this thesis aimed to explore innovative biotechnology techniques in antigen production for the improvement of immunoassays that allow the detection of antibodies directed against the Epstein-Barr virus. EBV virus is the causative agent of infectious mononucleosis and it is considered to be associated with a still increasing number of tumors; for this reason it is important to develop diagnostic assays for EBV detection with high specificity and sensitivity. The viral capsid protein VCA p18 is one of the most important antigens for the diagnosis of EBV. The current Diasorin LIAISON EBV VCA IgM and IgG assays rely on a single antigen, consisting in a synthetic peptide corresponding to the immunodominant C-terminal portion of the p18 protein, which is immobilized on solid phase (indirect format). The several methods explored in this thesis have allowed to obtain different variants of the p18 antigen with the aim to improve the performance of DiaSorin LIAISON EBV VCA IgM and IgG assays at different levels: 1_production of p18 antigen; 2_immobilization of p18 antigen on solid phase; 3_immunoassay format. 1_ The length of the immunodominant C-terminal portion of the p18 protein (57aa) appears to be considerable for the synthetic route but, at the same time, too small to be effectively produced in a recombinant fashion. To overcome this problem, we explored the Elastin Like Polypeptides (ELP)-Intein system, a method based on the use of a self-cleavable protein (the intein) and a temperature responsive tag (ELP). This technique has proved to be an excellent system for the preparation of the p18 peptide. 2_The development of different variants of p18 antigen has enabled to explore different techniques for the immobilization of the same antigen on solid phase: direct covalent coating, through streptavidin-biotin complex and through an innovative procedure based on the use of leucine zipper (or “velcro”) peptides. The immobilization of the p18 peptide on solid phase through these different methods occurred successfully and the immunochemical activity of the antigen, immobilized with these innovative techniques, is comparable or better than that of the synthetic peptide used in the current immunoassays. 3_Despite the DiaSorin LIAISON EBV VCA IgM immonoassay has a good analytical performance, in order to obtain an increase of specificity, a new assay format was explored. Unfortunately, the results indicate that this different type of format reaches a lower level of specificity than that of current assay. The second part of this thesis aimed to explore an innovative method for the site-specific labeling of antibodies. One the most promising approach is based on the generation of free thiol groups by selective partial reduction of the interchain disulfide bridges present at the level of the “hinge region” and their reaction to labels carrying sulfhydryl-reactive chemical groups. This technology was used for the biotinylation of two different antibodies currently used in immunoassays for the HIV p24 viral protein and for FGF23 antigen detection. The results suggest that the site-specific biotinylation compared to the random traditional biotinylation promotes a great improvement of antibodies immunochemical activity with a consequent optimization of immunodiagnostic assays performance.
MENTO, ALFREDO. « Unconventional purification and labelling strategies of bioreagents for immunodiagnostic assays ». Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/309986.
Texte intégralAntigens and antibodies are key reagents for the development of accurate, reproducible and sensible immunodiagnostic assays, which are widely used for the detection of infectious diseases (HIV,HBV, HCV, etc.) and the determination of biological markers (vitamins, hormones, etc.). These bioreagents need to be produced at a high purity degree, in stable formulations and with sufficient reproducibility over time (lot to lot consistency). An aspect often overlooked in the production of these reagents is their cost, which must be low enough to not have a significant impact on the final price of the immunochemical assays. The purification and labeling steps of these bioreagents mainly affect the overall cost of them since costly reagents and instrumentations and complex and time-consuming protocols are used.For all these reasons it is important to seek new purification strategies that allow the development of simpler processes, with less use of reagents and shorter protocol times, and at the end minor costs. Therefore, it is necessary to develop innovative purifications and site-specific labelling protocols. In the first part of this project we exploited the ELP-intein system. This method is based on the combination of two technological tools, the Elastin-like-polypeptides (ELPs) (a physico-chemical tool) and the MxeGyrA intein activity (a biochemical tool), belonging to the cis intein family. We focused on the purification and labelling of the C33 antigen from Hepatitis C Virus (HCV). The C33 antigen, which is currently used in the Diasorin LIAISON® XL Murex HCV assay for the detection of human antibodies against the Hepatitis C Virus, was purified using a not conventional purification method without chromatographic steps. Moreover, we realized a site-specific biotinylation of C33 antigen at its C-terminus during the purification exploiting the MxeGyrA intein biological activity. Two different protocols were developed; both of them brought to the obtainment of a biotinylated C33 antigen with high purity and a comparable immunoreactivity with the one currently used in the Diasorin LIAISON® XL Murex HCV assay. In light of these good results, in the second part of the project, we investigated the possibility to apply the Protein Trans Splicing (PTS) technology to perform site-specific labelling of bioreagents. PTS technology exploits the split intein activity. In particular, in our experiments we used the Cfa split-intein which derives from a mutagenesis process of the natural Npu split-intein that significantly improved its kinetic of PTS, thermal stability and tolerance at the chaotropic agents. This new technique allowed us to set up a site-specific labelling protocol for the production of biotinylated bioreagents. Two model protein were used: the same C33 antigen and a recombinant human IgG. Also the use of PTS technique permitted to obtain for both of two proteins a high purity and a comparable performance in the immunoassays. In summary, the ELP-intein system allowed to purify the C33 antigen without chromatographic steps and then to site-specific label the same protein at the C-terminus. Moreover, through the use of the Cfa split-intein system we obtained the site-specific biotinylation of the C33 antigen and the recombinant IgG. A very relevant aspects is that all these proteins are functional in the LIAISON platform. In the future, these protocols could be used for the purification and-or the site-specific labelling of new bioreagents useful for the development of immunodiagnostic assays.
Xu, Mengyun. « Optimised label-free biomarker assays with electrochemical impedance spectroscopy ». Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:e527a06b-25e5-48fe-8be5-3c0c10210b74.
Texte intégralLeidl, Leonhard [Verfasser]. « Relationship of immunodiagnostic assays for tuberculosis and numbers of circulating CD4+ T-cells in HIV-infection / Leonhard Leidl ». Lübeck : Zentrale Hochschulbibliothek Lübeck, 2011. http://d-nb.info/1015754740/34.
Texte intégralCorral, Marcelo Andreetta. « Imunodiagnóstico da estrongiloidíase humana frente a diferentes frações antigênicas de Strongyloides venezuelensis ». Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/5/5134/tde-27082014-111103/.
Texte intégralStrongyloidiasis is a parasitic infection caused by a nematode Strongyloides stercoralis. The definitive diagnosis is made by the larvae visualization in stool samples. However parasitological techniques have low sensitivity. Serological techniques became as suitable diagnostic alternative. Research indicates for the soluble heterologous antigen utilization, mainly Strongyloides venezuelensis. Identification and characterization of membrane antigen may constitute an alternative source of antigen and then assist the development of serological techniques. The aim of this study was evaluate ELISA and WB techniques behind different antigenic fractions of S. venezuelensis´ infective larvae. A total of 92 serum and stool samples was analyzed, 20 from individuals with strongyloidisis (group 1), 32 with other parasitic diseases (group 2) and 40 from individuals with negative coproparasitology (group 3) using Lutz, agar plate culture and Rugai methods. For the antigen preparation infective larvae of S. venezuelensis from experimental infected rats were employed. Six antigenic fractions were prepareted: saline soluble and from membrane fractions (0.01M PBS pH 7.2, and 1% SDS, SS and MS; 25mM Tris-HCl pH 7.5, 1% CHAPS, MT and ST, respectively) and alkaline soluble and membrane fractions (0.15 M NaOH and 1% SDS, SA and MA, respectively). For ELISA technique, plates were sensitized with 10 ug/mL of antigen, serum samples were diluted 1:200 in 0.05% Tween in PBS 3% milk (PBSTM) and conjugate (anti-human IgG peroxidase) in PBSTM. Positive samples were considered when ELISA index was greater than 1. To WB technique, serum samples were diluted 1:100 in Tris-HCl 5% milk (TM) and conjugate (anti-human IgG peroxidase) in the TM. After serological techniques diagnostics parameters were determined by ROC curve how sensitivity (SE), specificity (ES), Likelihood ratio (LR) and determination of diagnostic accuracy (AC) and Kappa (k) index. ELISA technique highlighted the membrane fractions with better performance compared to parameters diagnoses studied (95% SE, 94.4% ES, 94.8% AC, 17.1 LR, 0.848 k). The WB revealed immunodominant antigenic components ranging from 260-10kDa, but there are the fractions of 40-35kDa more frequent in all antigenic fractions. WB technique showed ST fraction better performance in relation to the diagnostic parameters (100% SE, 93.1% ES, 94.5% AC, 14.4 LR, 0.854 k). Membrane fractions in the immunodiagnosis of human strongyloidiasis become an accessible and effective source of antigens in relation to the purified fractions, requiring no additional expense to obtain it
Gottardi, Maiara. « Imunodiagnóstico da infecção por Strongyloides stercoralis em pacientes candidatos a transplante ». Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/5/5134/tde-09012015-162127/.
Texte intégralStrongyloidiasis is an intestinal infection caused by the nematode Strongyloides stercoralis. Most cases progress to a benign chronic condition; however hyperinfection and dissemination may occur, especially in immunocompromised patients. Conventional parasitological methods have low sensitivity and, thus, serological tests may be a good alternative for the diagnosis of this helminthiasis. The aim of this study was to evaluate RIFI, ELISA and WB techniques for the diagnosis of strongyloidiasis in patients candidates for transplants. In order to validate the tests samples of sera from immunocompetent patients (positive for S. stercoralis, positive for other parasitosis, and negatives) were used. Feces and sera samples of patients candidates for transplants were used as follows: 50 for renal transplant, 50 for liver transplant, 50 for bone marrow transplant. Fecal samples of all patients were analyzed by spontaneous sedimentation, Rugai and Agar plate culture techniques. Filarioid larvae of S. venezuelensis were used as source of antigen for serological tests. For RIFI, sera were diluted 1:40 in PBS-TM buffer and human anti-IgG conjugate labeled with fluorescein was diluted 1:500 in PBS with 4% Blue Evans, reading being performed in immunofluorescence microscope using 20X and 40X objectives. For ELISA technique polystyrene plates sensitized with 10?g of antigen (saline and alkaline soluble fractions), individual sera diluted at 1:200 in PBS 0.05% Tween 3% of milk (PBS-TM) and conjugate (human anti-IgG peroxidase) in PBS-TM were used. Samples were considered positive when ELISA index was higher than 1. For WB technique, sera were diluted in Tris-HCl 5% of milk (TM) and conjugate (human anti-IgG peroxidase) in PBS-TM. From 150 patients candidates for transplants analyzed 9.3% (n=14) were positive by parasitological techniques, agar plate culture detected 6.6% (n=10). In RIFI seropositivity for S. stercoralis infection detection was 16.6% (n=25) being 22% renal transplant, 18% hepatic and 10% for bone marrow. By ELISA technique seropositivity was 11.3% (n=17), being 14% in patients candidates for renal transplant, 14% hepatic and 3% bone marrow, using alkaline antigen and 24.6% (n=37), being 18% in patients candidates for renal transplant, 50% hepatic and 6% bone marrow, using saline antigen. By WB technique seropositivity was 20.6% (n=31), being 18% in patients candidates for renal transplant, 32% hepatic and 12% bone marrow, using alkaline antigen, and 18.6% (n=28) being 10% in patients candidates for renal transplant, 14% hepatic and 32% bone marrow, using saline antigen. Application of immunodiagnostic techniques could be indicated in screening of patients in transplant waiting list, however limitations of serological reactions in immunodepressed patients should be considered
Boshoff, Christoffel Hendrik. « Maedi-Visna virus : the development of serum and whole blood immunodiagnostic assays ». Thesis, 1997. http://hdl.handle.net/10413/6083.
Texte intégralThesis (Ph.D.)-University of Natal, Durban, 1997.
YANG, HONG-TONG, et 楊宏通. « Immunodiagnosis of trichomoniasis vaginalis:comparison between indirect fluorescent antibody test (IFAt) and enzyme-linked immunosorbent assay (ELISA) ». Thesis, 1989. http://ndltd.ncl.edu.tw/handle/10639050401194443631.
Texte intégralLivres sur le sujet "Immunodiagnostic assay"
W, Burgess Graham, et James Cook University of North Queensland. Graduate School of Tropical Veterinary Sciences., dir. ELISA technology in diagnosis and research. Townsville, Australia : Graduate School of Tropical Veterinary Science, James Cook University of North Queensland, 1988.
Trouver le texte intégralMarius, Teodorescu, et Froelich Christopher J, dir. Advanced immunoassays in rheumatology. Boca Raton : CRC Press, 1994.
Trouver le texte intégralN, Khan Masood, et Findlay John W. A, dir. Ligand-binding assays : Development, validation, and implementation in the drug development arena. Hoboken, N.J : Wiley, 2010.
Trouver le texte intégralW, Pruzanski, et Keystone E. C, dir. Paraproteins in disease : Investigation of plasma cell dyscrasia. Edinburgh : Churchill Livingstone, 1985.
Trouver le texte intégralQuantitative Immunoassay : A Practical Guide for Assay Establishment, Troubleshooting, and Clinical Application. AACC Press, 2000.
Trouver le texte intégralElisa as diagnostic tool : Prospects and implications. New Delhi : Wiley Eastern, 1992.
Trouver le texte intégralKhan, Masood N., et John W. Findlay. Ligand-Binding Assays : Development, Validation, and Implementation in the Drug Development Arena. Wiley & Sons, Incorporated, John, 2009.
Trouver le texte intégralKhan, Masood N., et John W. Findlay. Ligand-Binding Assays : Development, Validation, and Implementation in the Drug Development Arena. Wiley & Sons, Incorporated, John, 2009.
Trouver le texte intégralFindlay, John W. A., et Masood N. Khan. Ligand-Binding Assays : Development, Validation, and Implementation in the Drug Development Arena. Wiley & Sons, Incorporated, John, 2009.
Trouver le texte intégralChapitres de livres sur le sujet "Immunodiagnostic assay"
Pappas, Michael G. « Immunodiagnostic Assays ». Dans The Biotech Business Handbook, 247–72. Totowa, NJ : Humana Press, 1994. http://dx.doi.org/10.1007/978-1-4612-0293-6_17.
Texte intégralKinders, R., J. Slota, J. Patrick, C. Plate, I. Kafer, W. Caminiti, H. Rittenhouse et G. Manderino. « An Assay for Cryptic Tumor Antigens in Sera of Women with Breast Cancer ». Dans Breast Cancer Immunodiagnosis and Immunotherapy, 55–67. Boston, MA : Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-1296-4_6.
Texte intégralLudwig, George V., Cynthia A. Rossi et Robert L. Bull. « Concepts for the Development of Immunodiagnostic Assays for Detection and Diagnosis of Biothreat Agents ». Dans Biological Weapons Defense, 551–79. Totowa, NJ : Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-764-5:551.
Texte intégralTakemoto, Y., M. Tsuji et Y. Iwanaga. « Immunodiagnosis for Anisakiasis with Detection of IgE Antibody to Human Anisakiasis by Enzyme-Linked Immunosorbent Assay ». Dans Intestinal Anisakiasis in Japan, 187–90. Tokyo : Springer Japan, 1990. http://dx.doi.org/10.1007/978-4-431-68299-8_23.
Texte intégral« Example 3 Troponin measurement by immunoassay – Problem of low assay sensitivity and interference from heterophilic antibodies ». Dans Immunodiagnostics and Patient Safety. Berlin, New York : DE GRUYTER, 2011. http://dx.doi.org/10.1515/9783110249484.129.
Texte intégralRicardo, Lujan, et Cupp Eddie W. « Human Onchocerciasis : New Immunodiagnostic Assays and Control Measures ». Dans Biotechnology for Biological Control of Pests and Vectors, 179–92. CRC Press, 2018. http://dx.doi.org/10.1201/9781351070300-17.
Texte intégralSadeghalvad, Mona, et Nima Rezaei. « Introduction on Monoclonal Antibodies ». Dans Monoclonal Antibodies. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98378.
Texte intégralH. Ravindranath, Mepur, et Fatiha E.L. Hilali. « Monospecific and Polyreactive Monoclonal Antibodies against Human Leukocyte Antigen-E : Diagnostic and Therapeutic Relevance ». Dans Monoclonal Antibodies. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.95235.
Texte intégralActes de conférences sur le sujet "Immunodiagnostic assay"
Essone, Paulin N., Tom H. Ottenhoff, Novel N. Chegou et Gerhard Walzl. « Tuberculosis Immunodiagnostic Tests : A Potential Shift From Iterferon-Gamma (IFN-³) Release Assays To Tumor Necrosis Factor-Alpha (TNF-±) Release Assays With Newly Identified Mycobacterium Tuberculosis Antigens ». Dans American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6508.
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