The Experts below are selected from a list of 27 Experts worldwide ranked by ideXlab platform

P.e. Fraser - One of the best experts on this subject based on the ideXlab platform.

  • Assembly of the presenilin γ‐/ε‐secretase complex
    Journal of Neurochemistry, 2011
    Co-Authors: P.h. St George-hyslop, P.e. Fraser
    Abstract:

    The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2). Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 Antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.

  • Assembly of the presenilin γ-/ε-secretase complex.
    Journal of neurochemistry, 2011
    Co-Authors: P.h. St George-hyslop, P.e. Fraser
    Abstract:

    The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2). Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 Antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.

P.h. St George-hyslop - One of the best experts on this subject based on the ideXlab platform.

  • Assembly of the presenilin γ‐/ε‐secretase complex
    Journal of Neurochemistry, 2011
    Co-Authors: P.h. St George-hyslop, P.e. Fraser
    Abstract:

    The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2). Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 Antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.

  • Assembly of the presenilin γ-/ε-secretase complex.
    Journal of neurochemistry, 2011
    Co-Authors: P.h. St George-hyslop, P.e. Fraser
    Abstract:

    The presenilin complex is composed of four core proteins (presenilin 1 or presenilin 2, APH1, nicastrin, and PEN2). Several endogenous proteins have been reported to selectively modulate the function of the presenilin complexes; these include transmembrane trafficking protein, 21-KD (TMP21), CD147 Antigen (basigin), the γ-secretase-activating protein (gSAP), and the orphan G-protein-coupled receptor 3. Because the structure and assembly of these complexes underlies their activity, this review will discuss current work on the assembly of the complex and on presenilin-interacting proteins that regulate secretase activity.

Zhi-nan Chen - One of the best experts on this subject based on the ideXlab platform.

  • purification of a polyclonal antibody against CD147 for elisa using Antigen immunoaffinity chromatography
    Molecular Medicine Reports, 2017
    Co-Authors: Shasha Li, Yang Zhang, Bin Wang, Ye Wang, Zhi-nan Chen
    Abstract:

    The immunoglobulin superfamily member CD147 is a widely expressed glycoprotein that occurs in both a membrane‑spanning and soluble form. Sandwich ELISA is a powerful tool for analyzing soluble Antigens. The aim of the present study was to obtain a highly specific polyclonal antibody against human CD147 that can be used for sandwich ELISA analysis. Expression of recombinant CD147 by a eukaryotic expression system was used to immunize rabbits to obtain antiserum. A highly specific polyclonal antibody that was able to detect soluble CD147 in sandwich ELISA was obtained by Antigen‑immunoaffinity chromatography purification. The purity of rabbit anti‑CD147 polyclonal antibodies was ~99%, and ELISA analysis was able to determine the titer of the rabbit anti‑CD147 polyclonal antibodies at 1:512,000. The lowest concentration of the standard CD147 Antigen that the sandwich ELISA was able to detect was 31.25 pg/ml. The sandwich ELISA system was composed of anti‑hepatoma HAb18 monoclonal antibodies and purified rabbit anti‑CD147 polyclonal antibodies. The present study demonstrated that Antigen‑immunoaffinity chromatography may be a good technique for the purification of polyclonal antibodies, which may be used to detect Antigen in sandwich ELISAs.

  • Purification of a polyclonal antibody against CD147 for ELISA using Antigen‑immunoaffinity chromatography
    Molecular Medicine Reports, 2017
    Co-Authors: Shasha Li, Yang Zhang, Bin Wang, Ye Wang, Zhi-nan Chen
    Abstract:

    The immunoglobulin superfamily member CD147 is a widely expressed glycoprotein that occurs in both a membrane‑spanning and soluble form. Sandwich ELISA is a powerful tool for analyzing soluble Antigens. The aim of the present study was to obtain a highly specific polyclonal antibody against human CD147 that can be used for sandwich ELISA analysis. Expression of recombinant CD147 by a eukaryotic expression system was used to immunize rabbits to obtain antiserum. A highly specific polyclonal antibody that was able to detect soluble CD147 in sandwich ELISA was obtained by Antigen‑immunoaffinity chromatography purification. The purity of rabbit anti‑CD147 polyclonal antibodies was ~99%, and ELISA analysis was able to determine the titer of the rabbit anti‑CD147 polyclonal antibodies at 1:512,000. The lowest concentration of the standard CD147 Antigen that the sandwich ELISA was able to detect was 31.25 pg/ml. The sandwich ELISA system was composed of anti‑hepatoma HAb18 monoclonal antibodies and purified rabbit anti‑CD147 polyclonal antibodies. The present study demonstrated that Antigen‑immunoaffinity chromatography may be a good technique for the purification of polyclonal antibodies, which may be used to detect Antigen in sandwich ELISAs.

Shasha Li - One of the best experts on this subject based on the ideXlab platform.

  • purification of a polyclonal antibody against CD147 for elisa using Antigen immunoaffinity chromatography
    Molecular Medicine Reports, 2017
    Co-Authors: Shasha Li, Yang Zhang, Bin Wang, Ye Wang, Zhi-nan Chen
    Abstract:

    The immunoglobulin superfamily member CD147 is a widely expressed glycoprotein that occurs in both a membrane‑spanning and soluble form. Sandwich ELISA is a powerful tool for analyzing soluble Antigens. The aim of the present study was to obtain a highly specific polyclonal antibody against human CD147 that can be used for sandwich ELISA analysis. Expression of recombinant CD147 by a eukaryotic expression system was used to immunize rabbits to obtain antiserum. A highly specific polyclonal antibody that was able to detect soluble CD147 in sandwich ELISA was obtained by Antigen‑immunoaffinity chromatography purification. The purity of rabbit anti‑CD147 polyclonal antibodies was ~99%, and ELISA analysis was able to determine the titer of the rabbit anti‑CD147 polyclonal antibodies at 1:512,000. The lowest concentration of the standard CD147 Antigen that the sandwich ELISA was able to detect was 31.25 pg/ml. The sandwich ELISA system was composed of anti‑hepatoma HAb18 monoclonal antibodies and purified rabbit anti‑CD147 polyclonal antibodies. The present study demonstrated that Antigen‑immunoaffinity chromatography may be a good technique for the purification of polyclonal antibodies, which may be used to detect Antigen in sandwich ELISAs.

  • Purification of a polyclonal antibody against CD147 for ELISA using Antigen‑immunoaffinity chromatography
    Molecular Medicine Reports, 2017
    Co-Authors: Shasha Li, Yang Zhang, Bin Wang, Ye Wang, Zhi-nan Chen
    Abstract:

    The immunoglobulin superfamily member CD147 is a widely expressed glycoprotein that occurs in both a membrane‑spanning and soluble form. Sandwich ELISA is a powerful tool for analyzing soluble Antigens. The aim of the present study was to obtain a highly specific polyclonal antibody against human CD147 that can be used for sandwich ELISA analysis. Expression of recombinant CD147 by a eukaryotic expression system was used to immunize rabbits to obtain antiserum. A highly specific polyclonal antibody that was able to detect soluble CD147 in sandwich ELISA was obtained by Antigen‑immunoaffinity chromatography purification. The purity of rabbit anti‑CD147 polyclonal antibodies was ~99%, and ELISA analysis was able to determine the titer of the rabbit anti‑CD147 polyclonal antibodies at 1:512,000. The lowest concentration of the standard CD147 Antigen that the sandwich ELISA was able to detect was 31.25 pg/ml. The sandwich ELISA system was composed of anti‑hepatoma HAb18 monoclonal antibodies and purified rabbit anti‑CD147 polyclonal antibodies. The present study demonstrated that Antigen‑immunoaffinity chromatography may be a good technique for the purification of polyclonal antibodies, which may be used to detect Antigen in sandwich ELISAs.

Yang Zhang - One of the best experts on this subject based on the ideXlab platform.

  • purification of a polyclonal antibody against CD147 for elisa using Antigen immunoaffinity chromatography
    Molecular Medicine Reports, 2017
    Co-Authors: Shasha Li, Yang Zhang, Bin Wang, Ye Wang, Zhi-nan Chen
    Abstract:

    The immunoglobulin superfamily member CD147 is a widely expressed glycoprotein that occurs in both a membrane‑spanning and soluble form. Sandwich ELISA is a powerful tool for analyzing soluble Antigens. The aim of the present study was to obtain a highly specific polyclonal antibody against human CD147 that can be used for sandwich ELISA analysis. Expression of recombinant CD147 by a eukaryotic expression system was used to immunize rabbits to obtain antiserum. A highly specific polyclonal antibody that was able to detect soluble CD147 in sandwich ELISA was obtained by Antigen‑immunoaffinity chromatography purification. The purity of rabbit anti‑CD147 polyclonal antibodies was ~99%, and ELISA analysis was able to determine the titer of the rabbit anti‑CD147 polyclonal antibodies at 1:512,000. The lowest concentration of the standard CD147 Antigen that the sandwich ELISA was able to detect was 31.25 pg/ml. The sandwich ELISA system was composed of anti‑hepatoma HAb18 monoclonal antibodies and purified rabbit anti‑CD147 polyclonal antibodies. The present study demonstrated that Antigen‑immunoaffinity chromatography may be a good technique for the purification of polyclonal antibodies, which may be used to detect Antigen in sandwich ELISAs.

  • Purification of a polyclonal antibody against CD147 for ELISA using Antigen‑immunoaffinity chromatography
    Molecular Medicine Reports, 2017
    Co-Authors: Shasha Li, Yang Zhang, Bin Wang, Ye Wang, Zhi-nan Chen
    Abstract:

    The immunoglobulin superfamily member CD147 is a widely expressed glycoprotein that occurs in both a membrane‑spanning and soluble form. Sandwich ELISA is a powerful tool for analyzing soluble Antigens. The aim of the present study was to obtain a highly specific polyclonal antibody against human CD147 that can be used for sandwich ELISA analysis. Expression of recombinant CD147 by a eukaryotic expression system was used to immunize rabbits to obtain antiserum. A highly specific polyclonal antibody that was able to detect soluble CD147 in sandwich ELISA was obtained by Antigen‑immunoaffinity chromatography purification. The purity of rabbit anti‑CD147 polyclonal antibodies was ~99%, and ELISA analysis was able to determine the titer of the rabbit anti‑CD147 polyclonal antibodies at 1:512,000. The lowest concentration of the standard CD147 Antigen that the sandwich ELISA was able to detect was 31.25 pg/ml. The sandwich ELISA system was composed of anti‑hepatoma HAb18 monoclonal antibodies and purified rabbit anti‑CD147 polyclonal antibodies. The present study demonstrated that Antigen‑immunoaffinity chromatography may be a good technique for the purification of polyclonal antibodies, which may be used to detect Antigen in sandwich ELISAs.