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Corresponding Antibodies (corresponding + antibody)
Selected AbstractsMultianalyte immunoassay based on surface-enhanced Raman spectroscopyJOURNAL OF RAMAN SPECTROSCOPY, Issue 7 2007Yan Cui Abstract In this paper, two immunoassay methods based on SERS are developed for multiplex analysis, both of which stemmed from the concept of forming a sandwich structure ,capture antibody substrate/antigen/Raman-reporter-labeled immuno-nanoparticles'. They are two-molecule labeled one-nanoparticle and one-molecule labeled two-nanoparticle methods. In both the methods, two different antibodies covalently bound to a solid substrate can specifically capture two different antigens from a sample. The captured antigens in turn bind selectively to their corresponding antibodies immobilized on Raman-reporter-labeled nanoparticles. Multianalyte immunoassay is successfully demonstrated by the detection of characteristic Raman bands of the probe molecules only when the antigen and antibody are matched. Copyright © 2007 John Wiley & Sons, Ltd. [source] Ubiquitous cancer genes: Multipurpose molecules for protein micro-arraysPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 1 2006Brigitte Altenberg Abstract Multipurpose genes in the human genome which are over-expressed in a large variety of different cancers have been identified. Forty-two of the 19,016,human genes annotated to date (0.2%) are ubiquitously over-expressed in half or more of the 36,investigated human cancers. Of these genes, 15,are involved in protein biosynthesis and folding, six of them in glycolysis. A group of 13,solid tumours over-express almost all (39,42 of 42) ubiquitous cancer genes, suggesting a common mechanism underlying these cancers. Others, such as endocrine cancers, have only a few over-expressed ubiquitous cancer genes. The proteins for which these genes code or the corresponding antibodies are candidates for small protein microarrays aiming at maximum information with only a limited number of proteins. Since the over-expression pattern varies from cancer to cancer, distinction between different cancer classes is possible using one single set of protein or antibody molecules. [source] Human ABO Blood Group Is Important in Survival and Function of Porcine Working HeartsAMERICAN JOURNAL OF TRANSPLANTATION, Issue 3 2003Rizwan A. Manji Pig organs express ,Gal antigen and thus are hyperacutely rejected if perfused by human blood. Human B/A antigens are similar to pig ,Gal antigen, suggesting that the corresponding antibodies may cross-react. Our purpose was to determine if there is a human ABO blood-group difference in porcine,human xenotransplantation. Plasma from six A, five B, seven AB, and six O individuals pooled by blood group were tested in an ex-vivo porcine working heart model. Blood-group A plasma-perfused hearts survived 20 ± 14 min (n = 5), B 241 ± 9 min (n = 3), AB 151 ± 37 min (n = 5), and O 9 ± 1 min (n = 8). A and O were different (p < 0.001) from B and AB. Function was significantly better in group B. Edema accumulation and creatine kinase change was highest in A and O. All groups had comparable levels of anti-,Gal antibody, as well as comparable perfusion and operative conditions. Multivariate linear regression analysis showed the anti-B antibody levels to be predictive of survival (p < 0.001). At higher plasma concentrations, hearts perfused with B plasma survived longer (p =,0.01) than AB (218 ± 45 min, n = 4 vs. 6 ± 0 min, n = 3). These results suggest a human ABO blood-group difference in porcine-to-human xenotransplantation, which may be mediated by the anti-A and anti-B antibodies. [source] The utilization of rare blood donorsISBT SCIENCE SERIES: THE INTERNATIONAL JOURNAL OF INTRACELLULAR TRANSPORT, Issue 2 2007S. J. Nance When transfusion is needed for a patient with a rare blood type and the corresponding antibody, it can be challenging and lead to delays in transfusion. Sometimes, the blood cannot be found. Globally, the community of rare donor facilities is extremely collaborative and is quickly engaged in locating and delivering blood to the patients in need of rare blood types. Identifying the rare donor is a resource-intensive activity in every country especially in times of shrinking human and reagent resources. This paper will discuss the process flow for obtaining blood for patient's requiring rare types and the critical steps for each facility in the supply chain. The local facility plays a vital role in the knowledge of patient need and interaction with the patient's physician. The national facility that coordinates obtaining rare blood internationally also plays a vital role. The International Blood Group Reference Laboratory in Bristol as one of its roles, maintains the International Rare Donor Panel and also plays a vital role. These three roles hold the responsibility for collaboration to identify and obtain blood for patients in need. While there are differences in each country's definition of rare blood types, all are in agreement to assist when a country needs blood products. The International Society Blood Transfusion working party for rare donors plays a critical, collaborative role in developing processes between countries to further rare blood transfers between countries and providing expertise when needed. Outcome data are difficult to obtain, therefore success and ultimate improvement is a challenge. This challenge is one that the needs to be met to improve patient outcomes in cases where rare blood is needed throughout the world. [source] C-terminal region-dependent change of antibody-binding to the Eighth Reelin repeat reflects the signaling activity of ReelinJOURNAL OF NEUROSCIENCE RESEARCH, Issue 14 2009Takao Kohno Abstract Reelin is a secreted glycoprotein that plays pivotal roles in the development and function of the brain, but how it activates downstream intracellular signaling is not fully understood. We have recently reported that the highly conserved C-terminal region (CTR) of Reelin is required for its full signaling activity, although the underlying mechanism remains unknown. During biochemical study of Reelin, we serendipitously found that one commercially available anti-Reelin antibody G20 can bind to CTR-lacking mutant Reelin proteins, but not wild-type Reelin, on Western blotting. The G20 epitope resides in the last 19 residues of Reelin-repeat 8 (RR8), and neither posttranslational modification nor proteolysis can explain this effect. Furthermore, when an unrelated sequence, such as FLAG-tag, is inserted between RR8 and CTR, the reactivity of the corresponding antibody greatly decreases. These results suggest that RR8 and CTR form a tight structure that makes the surrounding sequence inaccessible to an antibody. Taking advantage of this phenomenon, we show the existence of CTR-lacking Reelin isoform in vivo for the first time and estimate its contribution to the total amount of secreted Reelin. Importantly, the extent to which Reelin mutants react with G20 is inversely correlated with their signaling activity, indicating that the CTR-induced structural change of RR8 is a prerequisite for downstream signaling activation, presumably via binding to a certain neuronal membrane molecule(s). © 2009 Wiley-Liss, Inc. [source] Studies on fluorescence resonance energy transfer between dyes and water-soluble quantum dotsLUMINESCENCE: THE JOURNAL OF BIOLOGICAL AND CHEMICAL LUMINESCENCE, Issue 4-5 2005Qidan Chen Abstract In this work, donor,acceptor complexes were formed based on antibody,antigen interactions. Immunoglobulin antigen (mouse-IgG) was effectively conjugated to mercaptopropyl acid-modified CdTe quantum dot synthesized in aqueous solution via electrostatic interaction, while organic dyes,tetramethylrhodamine isothiocyanate (TRITC) were attached to the corresponding antibody (anti-mouse IgG). The mutual affinity of the antigen and antibody brought the CdTe quantum dot and TRITC sufficiently close together to allow the resonance dipole,dipole coupling required for fluorescence resonance energy transfer to occur. The formation of immunocomplexes resulted in fluorescence resonance energy transfer from the CdTe quantum dot donors to the TRITC acceptors. Copyright © 2005 John Wiley & Sons, Ltd. 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