immunotransfert – English Translation – Keybot Dictionary

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immunotransfert
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immunoblotting
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immunotransfert
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immunoblotting
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Le Western Blot (ou immunotransfert semi-sec) est une technique de transfert sur nitrocellulose de protéines séparées par électrophorèse. Il permet de détecter et d’identifier des protéines spécifiques dans un échantillon biologique ou encore de tester des anticorps dirigés contre ces protéines.
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Western blot (immunoblot also semi-dried) is a technique for the transfer on nitrocellulose of separated proteins by electrophoresis. It allows to detect and to identify specific proteins in a biological sample or to test antibodies led against these proteins.
  hc-sc.gc.ca  
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Des concentrations d'allergènes jusqu'à 1-12.5 µg/g ont pu être détectées dans les échantillons d'aliments durant les divers tests. Nous avons obtenu aussi une bonne concordance avec d'autres types d'immunodosages, tels que l'immunoélectrophorèse en fusée, le dosage immuno-enzymatique et l'immunotransfert.
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We have evaluated the potential of a surface plasmon resonance (SPR)-based sensor system for food allergen analysis and developed direct and sandwich immunoassays for the detection of milk, egg, hazelnut, peanut, shellfish and sesame seeds in food samples. Affinity-purified polyclonal antibodies against the proteins were immobilized on the biosensor chip. Food samples were injected and the proteins that bound to the antibodies on the surface were detected by a shift in the resonance angle. By adding a second antibody in a sandwich assay, matrix effects could be eliminated and the sensitivity and selectivity enhanced. Detection of allergen levels down to 1-12.5 µg/g in food samples were demonstrated for the various assays. Good agreement was also obtained with other types of immunoassays like rocket immunoelectrophoresis, enzyme immunoassay and immunoblotting.
  www.hc-sc.gc.ca  
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Des concentrations d'allergènes jusqu'à 1-12.5 µg/g ont pu être détectées dans les échantillons d'aliments durant les divers tests. Nous avons obtenu aussi une bonne concordance avec d'autres types d'immunodosages, tels que l'immunoélectrophorèse en fusée, le dosage immuno-enzymatique et l'immunotransfert.
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We have evaluated the potential of a surface plasmon resonance (SPR)-based sensor system for food allergen analysis and developed direct and sandwich immunoassays for the detection of milk, egg, hazelnut, peanut, shellfish and sesame seeds in food samples. Affinity-purified polyclonal antibodies against the proteins were immobilized on the biosensor chip. Food samples were injected and the proteins that bound to the antibodies on the surface were detected by a shift in the resonance angle. By adding a second antibody in a sandwich assay, matrix effects could be eliminated and the sensitivity and selectivity enhanced. Detection of allergen levels down to 1-12.5 µg/g in food samples were demonstrated for the various assays. Good agreement was also obtained with other types of immunoassays like rocket immunoelectrophoresis, enzyme immunoassay and immunoblotting.
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Pour différencier Phellinus pini, Inonotus tomentosus at Inonotus circinatus, un anticorps polyclonal a été produit contre la portion N-terminale d'une protéine de 25 kDa spécifique de P. pini. La spécificité de cet anticorps a été évaluée a des fins de diagnostic à l'aide de l'immunotransfert Western et des techniques ELISA indirecte et par inhibition.
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In order to differentiate among Phellinus pini, Inonotus tomentosus and Inonotus circinatus a polyclonal antibody was raised to a N-terminal part of 25-kDa P. pini-specific protein. The specificity of the polyclonal antibody produced against a synthetic N-terminal peptide of this protein was investigated for diagnostic purposes using Western immunoblot, indirect enzyme-linked immunosorbent assay (ELISA), and inhibition ELISA techniques. The N-terminal synthetic peptide, used as the immunogen, was found to be more than 80% pure by reverse-phase high-performance liquid chromatography. Following immunization, antisera were collected at three different time intervals. The antibody molecules were purified from the crude antisera using immunoaffinity gel chromatography. Following one-dimensional sodium dodecylsulfate-polyacrylamide gel electrophoresis, Western immunoblot analysis showed that the P. pini I polyclonal-antibody detected the immunogen, the 25-kDa protein, in all but one of the P. pini isolates examined, but in none of the isolates of the nontarget species I. tomentosus and I. circinatus. Nevertheless, cross-reactivity was a problem because the P. pini I polyclonal-antibody also recognized bands at other molecular weights in nearly all of the isolates of the other species tested. With the indirect ELISA the P. pini isolates tended to have higher affinity for the polyclonal antibody than the nontarget species, but some cross-reactivity did occur. Inhibition ELISAs, performed over a range of soluble antigen concentrations (1.56-400 ng/100 ml), failed to show a clear distinction between P. pini and the two Inonotus spp. The low level of cross-reactivity observed for I. tomentosus isolate 52 (9%) was also apparent in the indirect ELISA analysis. All three assays indicated that P. pini isolate 41 was the most antigenic. Despite cross-reactivity, the antibody is useful in Western immunoblot for the diagnosis of most P. pini isolates.
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L’ostéopontine bovine (OPNb), une protéine de 60 kDa, et l’isoforme tronquée de 40 kDa ont été caractérisées par spectrométrie de masse et par immunotransfert avec 6 anticorps ciblant différents domaines de la protéine.
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The aim of this study was to characterize the osteopontin (OPN) secreted in bovine milk and to determine whether the different forms are the product of spliced variants. Spliced variants of the human gene and secreted osteopontin isoforms have been reported in human tumor tissue. In bovine milk, we identified 2 major forms: one corresponding to the full-length coding transcript and a truncated version of this form. No alternative spliced transcripts were detected in the lactating mammary gland tissue, in milk somatic cells, or in peripheral blood immune cells. The 60-kDa bovine osteopontin (bOPN) and a truncated 40-kDa protein isoform were confirmed by mass spectrometry and further characterized by immunoblotting using a panel of 6 antibodies targeting different domains of the protein. Of the 3 human anti-OPN antibodies targeting the N-terminal segment of the protein, only one detected all forms on sodium dodecyl sulfate-PAGE; one human anti-OPN antibody failed to detect bOPN, whereas the other detected only the 60-kDa protein, albeit barely in its phosphorylated form. Detection was generally more sensitive when the 60-kDa protein was dephosphorylated. Two polyclonal antibodies raised against bOPN were tested: one targeting the milk-purified bOPN (bOPN-121) and one targeting a bovine epitope (synthetic peptide) corresponding to a carboxy-terminal domain of the protein (bOPN-117). The bOPN-121 antibody detected all forms irrespective of the phosphorylation status of bOPN. The bOPN-117 and the mouse anti-human OPN (hOPN-4) antibodies, which recognized different domains of the carboxy-terminal segment of the protein, also preferentially detected the dephosphorylated 60-kDa protein. Whereas phosphorylation had a major effect on detection for several antibodies, deglycosylation slightly decreased immunodetection for the tested antibodies. In particular, phosphorylation is the major posttranslational modification that influenced the weak detection capacity of several antibodies. This fact needs to be taken into account for immunodetection of milk content. In conclusion, the OPN forms secreted in bovine milk are not the product of alternative splicing. The 40-kDa protein appears to be a truncated hypophosphorylated variant of the fulllength 60-kDa form, which is highly phosphorylated. Together, the proteomic and immunoblotting analyses used to characterize bovine milk OPN revealed the complex nature of the bovine milk OPN forms.