Rabbit Antiserum

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Robert W. Harrison - One of the best experts on this subject based on the ideXlab platform.

  • Staphylococcal α-toxin: A structure-function study using a monoclonal antibody
    Toxicon, 2003
    Co-Authors: Sidney Harshman, N Sugg, Bahiru Gametchu, Robert W. Harrison
    Abstract:

    Abstract A monoclonal antibody (A-Tox-653.1) selected for its reactivity in a dot immunoblot assay with denatured staphylococcal α-toxin has been isolated and its capacity to block the hemolytic and lethal activities of α-toxin measured. In addition, reactivity with monomer, hexamer, 123 I-monoiodinated and CNBr peptides of α-toxin was studied. In all cases the reactions of the monoclonal antibody were compared to those obtained with anti-α-toxin Rabbit hyperimmune serum. We find that while both the monoclonal antibody and the Rabbit Antiserum react with all forms of α-toxin, only the Rabbit Antiserum blocks hemolytic or lethal activity. Further, the Rabbit Antiserum reacts with CNBr fragments IV, V ad VII, whereas the monoclonal antibody reacts only with the carboxy terminal CNBr peptide VII. We conclude that, in solution, the carboxy terminal segment of α-toxin is relatively free and reaction with the monoclonal antibody neither impedes its binding to the specific receptor on the membrane nor interferes with formation of the hexamer complex.

Wang Xiaomei - One of the best experts on this subject based on the ideXlab platform.

  • fusion expression of vp2 gene of infectious bursal disease virus and the preparation of Rabbit Antiserum against vp2 protein
    Chinese Journal of Animal Infectious Diseases, 2009
    Co-Authors: Wang Xiaomei
    Abstract:

    The VP2 gene of Infectious bursal disease virus(IBDV) strain Gt was amplified by RT-PCR and cloned into expression vector pET30a.The gene in the recombinant vector was identified by PCR amplification,restriction endonucleases digestion and gene sequencing.The VP2 expression in E.coli DE3 was induced by IPTG.Anti-VP2 serum was prepared in Rabbits and tested for reactivity in indirect ELISA,immunofluorecence and Western blot.The Rabbit Antiserum had ELISA titer greater than 1∶25 600.The Antiserum also reacted with the recombinant VP2 protein expressed in sf9 cells and native IBDV particles in DF-1 cells by immunofluorecence,In Western blot,the Antiserum reacted with IBDV prepared from Vero cells.The availability of VP2 protein and Antiserum will be helpful for the further study on molecular biology of IBDV.

Liu Yi - One of the best experts on this subject based on the ideXlab platform.

  • Detection of Wheat yellow mosaic virus by Heterogeneous Animal Double-antibody Sandwich ELISA
    Virologica Sinica, 2020
    Co-Authors: Liu Yi
    Abstract:

    With purified Wheat yellow mosaic virus (WYMV) particles as antigen, cavy was injected to produce specific Antiserum. Its titer was tested as 1/128 by the method of micro-immunoprecipitation. Using cavy Antiserum as capture antibody for trapping the virus and Rabbit Antiserum as detection antibody, the experiment system of heterogeneous animal DAS-ELISA (HADAS-ELISA) was established to detect WYMV. The system has the advantage of better specificity and sensitivity of detection. This method was proved to be successful and prattical in the detection of the virus in field-collected samples , indicating that the experiment system of HADAS-ELTSA is superior to the indirect ELISA with Rabbit Antiserum only.

Sidney Harshman - One of the best experts on this subject based on the ideXlab platform.

  • Staphylococcal α-toxin: A structure-function study using a monoclonal antibody
    Toxicon, 2003
    Co-Authors: Sidney Harshman, N Sugg, Bahiru Gametchu, Robert W. Harrison
    Abstract:

    Abstract A monoclonal antibody (A-Tox-653.1) selected for its reactivity in a dot immunoblot assay with denatured staphylococcal α-toxin has been isolated and its capacity to block the hemolytic and lethal activities of α-toxin measured. In addition, reactivity with monomer, hexamer, 123 I-monoiodinated and CNBr peptides of α-toxin was studied. In all cases the reactions of the monoclonal antibody were compared to those obtained with anti-α-toxin Rabbit hyperimmune serum. We find that while both the monoclonal antibody and the Rabbit Antiserum react with all forms of α-toxin, only the Rabbit Antiserum blocks hemolytic or lethal activity. Further, the Rabbit Antiserum reacts with CNBr fragments IV, V ad VII, whereas the monoclonal antibody reacts only with the carboxy terminal CNBr peptide VII. We conclude that, in solution, the carboxy terminal segment of α-toxin is relatively free and reaction with the monoclonal antibody neither impedes its binding to the specific receptor on the membrane nor interferes with formation of the hexamer complex.

George Miller - One of the best experts on this subject based on the ideXlab platform.

  • Two 21-kilodalton components of the Epstein-Barr virus capsid antigen complex and their relationship to ZEBRA-associated protein p21 (ZAP21).
    Journal of Virology, 1996
    Co-Authors: Tricia R. Serio, A Angeloni, J L Kolman, L Gradoville, D A Katz, W. M. J. Van Grunsven, Jaap M. Middeldorp, George Miller
    Abstract:

    The viral capsid antigen complex of Epstein-Barr virus (EBV), an important serodiagnostic marker of infection with the virus, consists of at least four components, with molecular masses of 150, 110, 40, and 21 kDa. Here we show that the 21-kDa component of the viral capsid antigen consists of products of two EBV genes, BFRF3 and BLRF2. Both products were expressed from late transcripts, were recognized by human antisera, and were present in virions. The BFRF3 product, but not that of BLRF2, fulfilled the definition of ZEBRA-associated protein p21 (ZAP21). In cells in which EBV was lytically replicating, BFRF3 protein was coimmunoprecipitated together with ZEBRA by a Rabbit Antiserum directed against amino acids 197 to 245 of BZLF1. In EBV-negative cells cotransfected with BZLF1 and BFRF3 expression vectors, BFRF3 was also coimmunoprecipitated with this Antiserum. Although this Antiserum could not detect BFRF3 on an immunoblot, it was able to immunoprecipitate BFRF3 in the absence of ZEBRA expression. The Rabbit Antiserum to amino acids 197 to 245 of BZLF1 was found to detect the same epitope at the carboxy end of BFRF3 as was recognized by Rabbit Antiserum to BFRF3 itself. Thus, coimmunoprecipitation of BFRF3 p21 with ZEBRA appeared to be due to cross-reactivity of the immunoprecipitating Antiserum rather than to direct association of ZEBRA and BFRF3 p21.