Relevant bibliographies by topics / Monoclonal antibody probes Diagnostic use

Academic literature on the topic 'Monoclonal antibody probes Diagnostic use'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Monoclonal antibody probes Diagnostic use"

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McQuaid, S., and G. M. Allan. "Detection protocols for biotinylated probes: optimization using multistep techniques." Journal of Histochemistry & Cytochemistry 40, no. 4 (April 1992): 569–74. http://dx.doi.org/10.1177/40.4.1552190.

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Recent studies using biotinylated in situ hybridization (ISH) have utilized a wide range of detection protocols for the biotinylated hybrids, leading to conflicting reports in the literature regarding sensitivity. In this study we compared 11 different detection protocols for biotinylated ISH using a measles virus-specific RNA probe on formalin-fixed, paraffin-embedded central nervous system tissue infected with measles virus. Maximum sensitivity was achieved with five-step detection protocols incorporating the use of a monoclonal antibody to biotin. Single-step detection protocols were found to be insensitive, as shown by their failure to detect viral nucleic acid in infected white-matter cells. Only by increasing the number of steps in the detection protocols were these infected cells demonstrable. Unless pre-hybridization, hybridization, and detection protocols are optimized, the results obtained in pathogenicity studies using ISH could be misinterpreted, leading to false conclusions about nucleic acid distribution. This also applies to the ever-increasing use of ISH for diagnostic purposes.
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Rosenberg, J. S., M. J. Melnicoff, and P. Wilding. "Fc receptors for IgG on human neutrophils: analysis of structure and function by using monoclonal antibody probes." Clinical Chemistry 31, no. 9 (September 1, 1985): 1444–48. http://dx.doi.org/10.1093/clinchem/31.9.1444.

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Abstract Structural and functional characteristics of Fc receptors for IgG (Fc gamma) on human neutrophils were examined with two monoclonal antibody probes specific for the Fc gamma receptors, Leu 11b and 3G8. To determine the distribution, density, and membrane mobility of the Fc gamma receptor, we used immunogold staining techniques, flow cytometry analysis, and fluorescence microscopy. Both 3G8 and Leu 11b inhibited several cell functions, thereby depicting the regulatory role of the Fc gamma receptor in mediating neutrophil activities. Among the functions studied were release of lysosomal enzymes, release of superoxide anion (O2-), and Fc-dependent rosette formation and phagocytosis. The densities of Fc gamma determinants recognized by Leu 11b and 3G8 on cells from a patient with chronic myelogenous leukemia were less than the density of epitopes on neutrophils from a normal individual. Taken together, the detailed analysis of physical and functional aspects of the Fc gamma receptor on neutrophils described in this study serve as a model for further assessment of the use of Fc gamma phenotyping of cells as a diagnostic tool.
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Parker, Edward, Christina MacLaughlin, Samantha Wala, Gilbert Walker, and Chen Wang. "Targeting CLL Cells Using Rituximab-Conjugated Surface Enhanced Raman Scattering (SERS) Gold Nanoparticles." Blood 116, no. 21 (November 19, 2010): 2691. http://dx.doi.org/10.1182/blood.v116.21.2691.2691.

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Abstract Abstract 2691 Measuring the expression of cell surface markers is crucial to the effective diagnosis of lymphoproliferative disorders such as chronic lymphocytic leukemia (CLL). However, conventional fluorescent probes are constrained by the degradative effect of photobleaching and the broad emission spectra of dyes, which restricts the multiplexing capacity of marker detection. Recent developments in nanoparticle-based technology may confer significant advantages over these traditional tools. In particular, surface enhanced Raman scattering (SERS) nanoparticles (NPs) can now be targeted to cells via conjugation to monoclonal antibodies. These particles are composed of colloidal gold cores surrounded by an organic dye with a distinct Raman-scattering signature. In addition to providing stable long-term signals, Raman probes typically exhibit spectral bands more than 30 times narrower than those of fluorescence techniques, thereby greatly increasing the multiplexing potential of phenotypic analysis. In this study, we developed SERS NPs conjugated to the monoclonal antibody rituximab in order to target the surface marker CD20. Rituximab has been established as an effective therapeutic antibody in the treatment of several B-cell disorders, though its precise mechanism of action is unclear. The preparation of SERS probes was achieved by coating 60 nm gold particles with the Raman-active reporter malachite green isothiocyanate (MGITC) followed by a stabilizing layer of polyethylene glycol (PEG). These particles were then covalently linked to rituximab using ethyl dimethylaminopryl carbiimide (EDC) and sulfo-NHS chemistry. Following the incubation of CLL cells with rituximab conjugates, samples were examined using darkfield microscopy, and Raman scatter analyzed using a Raman spectroscope. The resulting spectra were concordant with the successful retention of SERS probes, as indicated by an increase in the intensity of MGITC Raman peaks as the staining concentration of conjugates increased. However, the significant background signal obtained using unconjugated control NPs highlights the necessity to incorporate more rigorous steps to remove unbound particles in future studies. Darkfield imaging strongly confirmed the successful binding of SERS probes to CLL cells, which notably failed to retain control NPs. Conjugate targeting was also disrupted by blocking CD20 binding sites with unconjugated rituximab prior to SERS probe staining, thereby confirming that NP targeting was not the product of non-specific binding. Together, these results strongly indicate the successful incorporation of a therapeutic antibody into the NP-based targeting of CD20. In conjunction with SERS probes directed at other markers, this novel diagnostic approach could have a profound impact on the multiplexing capacity of cell surface marker detection during the diagnosis of lymphoproliferative disorders. In addition, the long-term stability of these probes might facilitate the use of NP conjugates as tracers to examine the effects of rituximab binding, thereby providing valuable insight into the mechanisms of antibody-based immunotherapy. Disclosures: No relevant conflicts of interest to declare.
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Ruppel, Andreas, Ute Breternitz, and Reinhard Burger. "Diagnostic Mr 31 000 Schistosoma mansoni proteins: requirement of infection, but not immunization, and use of the “miniblot” technique for the production of monoclonal antibodies." Journal of Helminthology 61, no. 2 (June 1987): 95–101. http://dx.doi.org/10.1017/s0022149x00009810.

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ABSTRACTAntibodies directed against diagnostic Mr 31 000 polypeptide(s) of adult Schistosoma mansoni were already formed in mice during prepatency. In contrast, repeated immunization of mice with homogenates of adult schistosomes failed to elicit antibodies detectable in immunoblots in the Mr 31 000 region. Therefore, spleen cells of infected mice were used to produce hybridoma lines. The “miniblot technique” was developed in order to detect in hybridoma supernatants antibodies against schistosome Mr 31 000 components. Electrophoretically separated total S. mansoni proteins were transferred onto nitrocellulose, and the position of the Mr 31 000 components was determined with polyclonal antisera and immunoblotting. Pieces of about 3 square mm of nitrocellulose bearing the diagnostic proteins were incubated with about 100 μ1 of hybridoma supernatant in microtitre plates and subsequently probed with peroxidase-conjugated antibody to mouse IgG. This screening technique identified hybridomas secreting antibody to the relevant S. mansoni antigens. It is applicable to other defined parasit antigens, which are, however, not available in biochemically purified form. The monoclonal antibodies produced against the proteins with diagnostic potential reacted with antigens localized in the schistosome gut.
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Bains, William. "Simplified format for DNA probe-based tests." Clinical Chemistry 37, no. 2 (February 1, 1991): 248–53. http://dx.doi.org/10.1093/clinchem/37.2.248.

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Abstract The approach I describe to using DNA probes in diagnostic tests is simpler than most existing formats. DNA in a sample is labeled by chemical reaction with bisulfite and methylamine to generate a sulfonated derivative. The DNA need not be purified to do this. The labeled sample is then incubated with an unlabeled, purified probe DNA, which is immobilized to a solid support. The amount of label remaining on the solid support after washing is detected by a monoclonal antibody that recognizes modified cytosines. The intensity of the signal depends on the amount of target DNA in the sample. Detection limits depend on the amount of immobilized DNA and on the degree of physical entrapment of the labeled DNA in sample material, but can be as low as 5 pg. This format is well suited to automation for use with existing robotic enzyme immunoassay procedures.
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Sapozhnikova, Ksenia A., Vsevolod A. Misyurin, Dmitry Y. Ryazantsev, Egor A. Kokin, Yulia P. Finashutina, Anastasiya V. Alexeeva, Igor A. Ivanov, et al. "Sensitive Immunofluorescent Detection of the PRAME Antigen Using a Practical Antibody Conjugation Approach." International Journal of Molecular Sciences 22, no. 23 (November 27, 2021): 12845. http://dx.doi.org/10.3390/ijms222312845.

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Bioconjugation of antibodies with various payloads has diverse applications across various fields, including drug delivery and targeted imaging techniques. Fluorescent immunoconjugates provide a promising tool for cancer diagnostics due to their high brightness, specificity, stability and target affinity. Fluorescent antibodies are widely used in flow cytometry for fast and sensitive identification and collection of cells expressing the target surface antigen. Nonetheless, current approaches to fluorescent labeling of antibodies most often use random modification, along with a few rather sophisticated site-specific techniques. The aim of our work was to develop a procedure for fluorescent labeling of immunoglobulin G via periodate oxidation of antibody glycans, followed by oxime ligation with fluorescent oxyamines. Here, we report a novel technique based on an in situ oxime ligation of ethoxyethylidene-protected aminooxy compounds with oxidized antibody glycans. The approach is suitable for easy modification of any immunoglobulin G, while ensuring that antigen-binding domains remain intact, thus revealing various possibilities for fluorescent probe design. The technique was used to label an antibody to PRAME, a cancer-testis protein overexpressed in a number of cancers. A 6H8 monoclonal antibody to the PRAME protein was directly modified with protected-oxyamine derivatives of fluorescein-type dyes (FAM, Alexa488, BDP-FL); the stoichiometry of the resulting conjugates was characterized spectroscopically. The immunofluorescent conjugates obtained were applied to the analysis of bone marrow samples from patients with oncohematological diseases and demonstrated high efficiency in flow cytometry quantification. The approach can be applied for the development of various immunofluorescent probes for detection of diagnostic and prognostic markers, which can be useful in anticancer therapy.
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Zhu, Lei, Hannu Koistinen, Ulf Landegren, and Ulf-Håkan Stenman. "Proximity Ligation Measurement of the Complex between Prostate Specific Antigen and α1-Protease Inhibitor." Clinical Chemistry 55, no. 9 (September 1, 2009): 1665–71. http://dx.doi.org/10.1373/clinchem.2009.127779.

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Abstract Background: Prostate specific antigen (PSA)–α1-protease inhibitor complex (PSA-API) is a minor form of PSA in serum. It may be useful for prostate cancer (PCa) diagnosis, but its specific detection is hampered by nonspecific background. To avoid this, we developed an immunoassay for PSA-API based on proximity ligation. Methods: We used a monoclonal antibody (mAb) to total PSA (tPSA) to capture PSA, while using another anti-tPSA mAb together with an anti-API mAb as probes. We measured PSA-API by quantification of amplified DNA strands conjugated to the probes. We measured serum PSA-API in 84 controls and 55 men with PCa who had PSA concentrations of 4.0–10 μg/L. Results: The detection limit of the assay was 6.6 ng/L. The proportion of PSA-API to tPSA (%PSA-API) tended to be lower in men with PCa (2.8%) than without cancer (3.3%) but was not statistically significant (P = 0.363). When used alone, %PSA-API [area under the curve (AUC) 0.546] did not improve detection of PCa, whereas %fPSA (AUC 0.710) and the sum of %fPSA and %PSA-API (AUC 0.723) did. At 90% diagnostic sensitivity, the diagnostic specificity for cancer was not significantly better for %fPSA + %PSA-API than for %fPSA alone (36% vs 30%). Conclusions: Proximity ligation eliminated nonspecific background, enabling accurate measurement of PSA-API in serum specimens with moderately increased tPSA. The combined use of %PSA-API and %fPSA provided a modest improvement for PCa detection, but based on the current study cohort, it is uncertain whether the improvement has clinical utility. .
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Lamy, A., E. Labourier, O. Prigneau, F. Di Fiore, R. Sesboüá, and J. Sabourin. "A method to assess KRAS/BRAF genotype in patients with metastatic colorectal cancer (mCRC) elligible for anti-EGFR therapies." Journal of Clinical Oncology 29, no. 4_suppl (February 1, 2011): 383. http://dx.doi.org/10.1200/jco.2011.29.4_suppl.383.

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383 Background: KRAS/BRAF mutation screening is a new diagnostic tool since activating mutations, especially for KRAS, are strong negative predictive factors for anti-EGFR monoclonal antibody therapies. Therefore, standardized, reliable, and rapid mutation detection methods are needed. The goal of the present study is to evaluate the concordance between a clinically validated laboratory-developed KRAS/BRAF SNaPshot test and a novel research use assay, the Signature KRAS/BRAF Mutations kit (Asuragen Inc.), in representative clinical specimens. Methods: Genomic DNA from FFPE mCRC specimens previously tested with the SNaPshot assay were analyzed using the Signature KRAS/BRAF mutations assay. The Signature assay consists of multiplex PCR followed by multiplex hybridization to fluorescent beads coupled to capture probes and detection on the Luminex analyzer. The qualitative assay detects 12 mutations in KRAS codons 12/13 and BRAF V600E based on the median fluorescence intensity (MFI) generated by each bead above (positive) or below (negative) a fixed cut off. Results: To date, KRAS/BRAF mutational status was successfully assessed with the signature assay in 248 samples. After initial testing, signature and SNaPshot assays were in qualitative agreement for 232 samples (93.5%): 166 positive for KRAS, 46 positive for BRAF, and 20 double negative. 16 samples (6%) presented discrepant results: (i) 11 false negative samples with fluorescence signals for the expected mutations above the average assay background signal but below the 450 MFI positive cut off preselected for this study (330-431 MFI), (ii) 3 samples positive for both KRAS and BRAF and (iii) 2 false positive samples. 7 discrepant samples have been retested to date resulting in an overall agreement of 99.6% (239/240). However, different KRAS mutations were identified by the SNaPshot and signature assays in 3 positive samples. Conclusions: The signature KRAS/BRAF mutations assay is an attractive method, easy to use, less time consuming than the SNaPshot assay, and potentially adaptable to routine clinical testing. Further analysis will establish and validate cut offs to be used in routine diagnostic procedures. No significant financial relationships to disclose.
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Dunn, Bruce E. "Nucleic acid and monoclonal antibody probes, applications in diagnostic microbiology." Human Pathology 22, no. 4 (April 1991): 403–4. http://dx.doi.org/10.1016/0046-8177(91)90095-7.

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Parratt, D. "Nucleic Acid and Monoclonal Antibody Probes. Applications in Diagnostic Microbiology." Journal of Clinical Pathology 42, no. 12 (December 1, 1989): 1313. http://dx.doi.org/10.1136/jcp.42.12.1313-c.

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Dissertations / Theses on the topic "Monoclonal antibody probes Diagnostic use"

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Wong, Yin-ki Sylvia, and 黃賢琪. "Detection of platelet antibodies by monoclonal antibody immobilizationof platelet antigens (MAIPA) assay." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2005. http://hub.hku.hk/bib/B45010523.

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Mohr, Alexandra. "Use of a monoclonal antibody to detect gray mold (Botrytis cinerea) in strawberry." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33812.

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Gray mold, caused by Botrytis cinerea is the major cause of postharvest loss in strawberries. Detection of flower and fruit infections enables producers to make intelligent management decisions. A plate-trapped ELISA protocol using a Botrytis-specific monoclonal antibody (BC-12.CA4) was developed for the detection of Botrytis cinerea in strawberry flower receptacles and red fruits. Horseradish peroxidase, was chosen as enzyme conjugate because it gave lower background absorbance in disease-free samples. B. cinerea reference antigen (RAg) was isolated from strawberry. BC-12.CA4 was very sensitive to the RAg, detecting up to 6 mug/ml of RAg when mixed with strawberry extracts. The MAb did not show any reaction to Rhizopus sp., Mucor sp. and Penicillium sp. associated with strawberry. B. cinerea could be detected in receptacles two days after inoculation. Treatment of inoculated receptacles with paraquat speeded-up detection. Inoculated red fruit infection could be detected after three days of incubation. Disease in commercially-produced receptacles and red fruits were assessed visually and by ELISA. The ELISA detected B. cinerea in 95% of commercial flower samples, whereas the traditional visual method detected only 50 to 70%. No dramatic differences between methods were found for red fruits.
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Books on the topic "Monoclonal antibody probes Diagnostic use"

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R, Walker Matthew, and Rapley Ralph, eds. Molecular and antibody probes in diagnosis. Chichester: Wiley, 1993.

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Gmür, Rudolf. Value of new serological probes for the study of putative periodontal pathogens: A survey after five years of application. Chicago: Quintessence Pub. Co., 1995.

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C, Gallo Robert, Della Porta Giuseppe, Albertini Alberto, and BIOTECH RIA 86 Meeting (1986 : Florence, Italy), eds. Monoclonals and DNA probes in diagnostic and preventive medicine. New York: Raven Press, 1987.

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Magerstadt, Michael. Antibody conjugates and malignant disease. Boca Raton: CRC Press, 1991.

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J, Ruiter Dirk, Fleuren Gert Jan, and Warnaar Sven O, eds. Application of monoclonal antibodies in tumor pathology. Dordrecht: Nijhoff, 1987.

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International Congress on Rapid Methods and Automation in Microbiology and Immunology (7th 1993 London, England). Rapid methods and automation in microbiology and immunology: RAMI-93. Andover, Hampshire: Intercept, 1994.

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1946-, Swaminathan Bala, and Prakash Gyan 1956-, eds. Nucleic acid and monoclonal antibody probes: Applications in diagnostic microbiology. New York: M. Dekker, 1989.

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¹¹¹Indium-labeled antimyosin monoclonal antibody. Glenview, Ill: Physicians & Scientists Pub. Co., 1992.

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1952-, Wick Mark R., and Siegal Gene Philip, eds. Monoclonal antibodies in diagnostic immunohistochemistry. New York: Dekker, 1988.

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Swaminathan, Bala. Nucleic Acid and Monoclonal Antibody Probes: Applications in Diagnostic Microbiology (Infectious Disease and Therapy). Marcel Dekker, 1989.

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Book chapters on the topic "Monoclonal antibody probes Diagnostic use"

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Söylemez, Fatma, and Çağatay Han Türkseven. "Aptamers and Possible Effects on Neurodegeneration." In Neuroprotection - New Approaches and Prospects. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.89621.

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Aptamers are a new class of recognizing agents which are defined as short biomolecules like oligonucleotides and peptides that are used in diagnostics and therapeutics. They can bind to specific targets with extremely high affinity based on their structural conformations. It is believed that in the near future, aptamers could replace monoclonal antibody. The biggest advantage of using aptamers is that the process is in vitro in nature and does not require the use of animals and they also have unique properties, such as thermal stability, low cost, and unlimited applications. Aptamers have been studied as a biomaterial in numerous investigations concerning their use as a diagnostic and therapeutic tool and biosensing probe. DNA aptamers were also used for the diagnosis and treatment of neurodegeneration and neurodegenerative diseases. For example, functional nucleic acid aptamers have been developed to detect Aβ fragments in Alzheimer’s brain hippocampus tissue samples. Aptamers are promising materials for diverse areas, not just as alternatives to antibodies but as the core components of medical equipment. Although they are in the preliminary stages of development, results are quite encouraging, and it seems that aptamer research has a very bright future in neuroscience.
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Zveiter de Moraes, Jane, Barbara Hamaguchi, Camila Braggion, Enzo Speciale, Fernanda Cesar, Gabriela Soares, Juliana Osaki, Rodrigo Aguiar, and Tauane Pereira. "Alternative Methods to Animal Use for Monoclonal Antibody Generation and Production." In Monoclonal Antibodies [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.95485.

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Monoclonal antibody (mAb) has broad applicability in research, diagnosis, and treatment. After the introduction of hybridoma technology in 1975, the mAb market has increased dramatically, moving a large industry of more than US$ 140 billions in 2020. In 1954, the concept of the 3R’s was proposed and much changed the animal use scenario, including the recent ban on inducing ascites in mice for the production of mAb. In light of this, the generation and production of antibodies had to be reassessed. In this chapter, we present an overview of the main alternative technologies to the use of animals in the generation and production of mAb. Antibody display libraries and in silico modeling are very promising technologies that may provide mAb genetic constructs that, in the sequence, may be expressed on mammalian, bacterial, yeast or plant systems. Although the total replacement of the use of animals in the entire process is not currently feasible, it is possible to find ways to reduce and refine the use of animals in obtaining and producing mAb.
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Zveiter de Moraes, Jane, Barbara Hamaguchi, Camila Braggion, Enzo Speciale, Fernanda Cesar, Gabriela Soares, Juliana Osaki, Rodrigo Aguiar, and Tauane Pereira. "Alternative Methods to Animal Use for Monoclonal Antibody Generation and Production." In Monoclonal Antibodies [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.95485.

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Monoclonal antibody (mAb) has broad applicability in research, diagnosis, and treatment. After the introduction of hybridoma technology in 1975, the mAb market has increased dramatically, moving a large industry of more than US$ 140 billions in 2020. In 1954, the concept of the 3R’s was proposed and much changed the animal use scenario, including the recent ban on inducing ascites in mice for the production of mAb. In light of this, the generation and production of antibodies had to be reassessed. In this chapter, we present an overview of the main alternative technologies to the use of animals in the generation and production of mAb. Antibody display libraries and in silico modeling are very promising technologies that may provide mAb genetic constructs that, in the sequence, may be expressed on mammalian, bacterial, yeast or plant systems. Although the total replacement of the use of animals in the entire process is not currently feasible, it is possible to find ways to reduce and refine the use of animals in obtaining and producing mAb.
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Boumaiza, Mohamed, Samia Rourou, Paolo Arosio, and Mohamed Nejib Marzouki. "The Use of Ferritin as a Carrier of Peptides and Its Application for Hepcidin." In BioMechanics and Functional Tissue Engineering [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.94408.

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Hepcidin a 25-amino-acid and highly disulfide bonded hormone, is the central regulator of iron homeostasis. In this chapter we propose ferritin as a peptide carrier to promote the association of the hybrid hepcidin/ferritin nanoparticle with a particular cell or tissue for therapeutic or diagnostic use. Indeed, human ferritin H-chain fused directly (on its 5’end) with camel mature hepcidin was cloned into the pASK-43 plus vector and expressed using BL21 (DE3) pLys E. coli strain. The transformed E.coli produced efficiently hepcidin-ferritin construct (hepcH), consisting of 213 amino acids with a molecular weight of 24 KDa. The recovered product is a ferritin exposing hepcidin on outer surface. The hepcH monomer was characterized by immunoblotting using a monoclonal antibody specific for human ferritin and a polyclonal antibody specific for hepcidin-25. The results were also confirmed by MALDI-TOF mass spectrometry. The recombinant native human ferritin and the commercial human hepcidin-25 were used as controls in this experiment. The assembly of hepcH, as an heteropolymer molecule, was performed in presence of denatured human ferritin-H and -L chains. After cysteine oxidation of the recombinant nanoparticles, cellular binding assays were performed on mammalian cells such as mouse monocyte–macrophage cell line J774, HepG2 and COS7.
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Conference papers on the topic "Monoclonal antibody probes Diagnostic use"

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Fulcher, C. A., R. A. Houghten, S. de Graaf Mahoney, J. R. Roberts, and T. S. Zimmerman. "SYNTHETIC PEPTIDE PROBES OF FACTOR VIII IMMUNOLOGY AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644768.

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In order to develop specific immunologic reagents for mapping functionally important sites on FVIII, we have prepared rabbit polyclonal antibodies against synthetic peptides of FVIII derived from regions along the entire FVIII amino acid sequence. To date, a total of 70 peptides have been synthesized and characterized by amino acid and HPLC analysis. The peptides were coupled to keyhole limpet hemocyanin with glutaraldehyde as a linkage reagent and used to immunize rabbits. Antisera were tested by ELISA assay on polystyrene microtiter plates coated with either the peptide immunogen, or purified FVIII. The antisera were also tested for their ability to inhibit FVIII clotting activity and to react with separated FVIII polypeptides on immunoblots.Of the 70 peptides, all reacted with the peptide immunogen, 45 reacted with purified FVIII and 33 reacted with FVIII on immunoblots. Because we had obtained evidence that cleavage of the amino terminal region of the 80 kDa polypeptide may play a role in FVIII activation by thrombin, a series of partially overlapping peptides, 15 residues in length, were synthesized in this area. After affinity purifying these antibodies on columns of FVIII immobilized on agarose, adjusting the antibodies to equal antigen binding titers by dot immunoblotting and testing for inhibition of FVIII activity, only one antibody could strongly inhibit FVIII clotting activity. This inhibition could be blocked by the peptide itself at nanomolar concentrations and no significant inhibition could be shown by antibodies to partially overlapping peptides individually, or in combination. These data suggest that a site important to FVIII function can be localized to a 15 amino acid residue region of the 80 kDa polypeptide of FVIII. In addition, a second inhibitoryantibody was identified which was produced against a peptide in the carboxy terminal region of the 54 kDa thrombin fragment of FVIII and this area is currently being studied in a similar manner. In addition, two monoclonal anti-FVIII synthetic peptide antibodies have been produced which react with purified FVIII on immunoblots. One of these antibodies also functions as an immunoadsorbent when linked to agarose and FVII can be purified in this manner, using the synthetic peptide as eluant. It is evident that antibodies to synthetic peptides of FVIII can be useful probes of FVIII structure, function and interactions as well as being of use in FVIII purification.
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