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goat anti human ace2 ectodomain polyclonal abs  (R&D Systems)


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    R&D Systems goat anti human ace2 ectodomain polyclonal abs
    Co-precipitation of recombinant S450–650 with <t>ACE2</t> in the lysate of Vero E6 cells. Vero E6 cells (1 × 10 6 ) were sequentially treated with goat anti-human ACE2 Abs, or goat IgG (2 μg), and FITC-conjugated rabbit anti-goat IgG. The stained cells were subjected to flow cytometric analysis for determination of ACE2 expression on the cell surface (A). For the co-precipitation experiment (B), Vero E6 cells (2.5 × 10 7 ) were treated with, or without, recombinant S450–650 (15 μg/ml) at 4 °C for 1 h. After washes, the cells were lysed using lysis buffer and the lysate treated with PT31 serum followed by protein-A/G-agarose precipitation. The precipitated materials were run on SDS-PAGE 12% gels and the protein bands transferred to nitrocellulose membranes for WB assays using goat anti-human ACE2 Abs as the first Abs, the detection Abs were HRP-labeled rabbit anti-goat IgG. In a parallel experiment (C), lysate of the S450–650-treated, or untreated, Vero E6 cells were precipitated using goat anti-human ACE2 Abs and protein-A/G-agarose. The precipitates were assayed by WB using PT31 serum (first Ab) and HRP-labeled goat anti-human IgG (detection Ab).
    Goat Anti Human Ace2 Ectodomain Polyclonal Abs, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti human ace2 ectodomain polyclonal abs/product/R&D Systems
    Average 93 stars, based on 49 article reviews
    goat anti human ace2 ectodomain polyclonal abs - by Bioz Stars, 2026-03
    93/100 stars

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    1) Product Images from "A study on antigenicity and receptor-binding ability of fragment 450–650 of the spike protein of SARS coronavirus"

    Article Title: A study on antigenicity and receptor-binding ability of fragment 450–650 of the spike protein of SARS coronavirus

    Journal: Virology

    doi: 10.1016/j.virol.2006.09.022

    Co-precipitation of recombinant S450–650 with ACE2 in the lysate of Vero E6 cells. Vero E6 cells (1 × 10 6 ) were sequentially treated with goat anti-human ACE2 Abs, or goat IgG (2 μg), and FITC-conjugated rabbit anti-goat IgG. The stained cells were subjected to flow cytometric analysis for determination of ACE2 expression on the cell surface (A). For the co-precipitation experiment (B), Vero E6 cells (2.5 × 10 7 ) were treated with, or without, recombinant S450–650 (15 μg/ml) at 4 °C for 1 h. After washes, the cells were lysed using lysis buffer and the lysate treated with PT31 serum followed by protein-A/G-agarose precipitation. The precipitated materials were run on SDS-PAGE 12% gels and the protein bands transferred to nitrocellulose membranes for WB assays using goat anti-human ACE2 Abs as the first Abs, the detection Abs were HRP-labeled rabbit anti-goat IgG. In a parallel experiment (C), lysate of the S450–650-treated, or untreated, Vero E6 cells were precipitated using goat anti-human ACE2 Abs and protein-A/G-agarose. The precipitates were assayed by WB using PT31 serum (first Ab) and HRP-labeled goat anti-human IgG (detection Ab).
    Figure Legend Snippet: Co-precipitation of recombinant S450–650 with ACE2 in the lysate of Vero E6 cells. Vero E6 cells (1 × 10 6 ) were sequentially treated with goat anti-human ACE2 Abs, or goat IgG (2 μg), and FITC-conjugated rabbit anti-goat IgG. The stained cells were subjected to flow cytometric analysis for determination of ACE2 expression on the cell surface (A). For the co-precipitation experiment (B), Vero E6 cells (2.5 × 10 7 ) were treated with, or without, recombinant S450–650 (15 μg/ml) at 4 °C for 1 h. After washes, the cells were lysed using lysis buffer and the lysate treated with PT31 serum followed by protein-A/G-agarose precipitation. The precipitated materials were run on SDS-PAGE 12% gels and the protein bands transferred to nitrocellulose membranes for WB assays using goat anti-human ACE2 Abs as the first Abs, the detection Abs were HRP-labeled rabbit anti-goat IgG. In a parallel experiment (C), lysate of the S450–650-treated, or untreated, Vero E6 cells were precipitated using goat anti-human ACE2 Abs and protein-A/G-agarose. The precipitates were assayed by WB using PT31 serum (first Ab) and HRP-labeled goat anti-human IgG (detection Ab).

    Techniques Used: Recombinant, Staining, Expressing, Lysis, SDS Page, Labeling

    ACE2 interaction with the β5 and β6 strands of S-RBM. (A) Crystal structure of the RBD in complex of human receptor ACE2 as reported by Li and co-workers . Details of the binding interface between S-RBM and the ACE2 molecule and calculation results of the contact area and binding energy are shown in panels B and C, respectively. The S protein-binding areas of the ACE2 molecule (purple) are colored in green and the β5 and β6 strands in gold. The binding energy here is the energy required to disassemble the RBD-ACE2 complex into separate parts. The figure is prepared using PYMOL and contact area and binding energy calculated by SPDBV. PDB file accession number is 2AJF.
    Figure Legend Snippet: ACE2 interaction with the β5 and β6 strands of S-RBM. (A) Crystal structure of the RBD in complex of human receptor ACE2 as reported by Li and co-workers . Details of the binding interface between S-RBM and the ACE2 molecule and calculation results of the contact area and binding energy are shown in panels B and C, respectively. The S protein-binding areas of the ACE2 molecule (purple) are colored in green and the β5 and β6 strands in gold. The binding energy here is the energy required to disassemble the RBD-ACE2 complex into separate parts. The figure is prepared using PYMOL and contact area and binding energy calculated by SPDBV. PDB file accession number is 2AJF.

    Techniques Used: Binding Assay, Protein Binding



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    goat anti human ace2 ectodomain polyclonal abs  (R&D Systems)
    93
    R&D Systems goat anti human ace2 ectodomain polyclonal abs
    Co-precipitation of recombinant S450–650 with <t>ACE2</t> in the lysate of Vero E6 cells. Vero E6 cells (1 × 10 6 ) were sequentially treated with goat anti-human ACE2 Abs, or goat IgG (2 μg), and FITC-conjugated rabbit anti-goat IgG. The stained cells were subjected to flow cytometric analysis for determination of ACE2 expression on the cell surface (A). For the co-precipitation experiment (B), Vero E6 cells (2.5 × 10 7 ) were treated with, or without, recombinant S450–650 (15 μg/ml) at 4 °C for 1 h. After washes, the cells were lysed using lysis buffer and the lysate treated with PT31 serum followed by protein-A/G-agarose precipitation. The precipitated materials were run on SDS-PAGE 12% gels and the protein bands transferred to nitrocellulose membranes for WB assays using goat anti-human ACE2 Abs as the first Abs, the detection Abs were HRP-labeled rabbit anti-goat IgG. In a parallel experiment (C), lysate of the S450–650-treated, or untreated, Vero E6 cells were precipitated using goat anti-human ACE2 Abs and protein-A/G-agarose. The precipitates were assayed by WB using PT31 serum (first Ab) and HRP-labeled goat anti-human IgG (detection Ab).
    Goat Anti Human Ace2 Ectodomain Polyclonal Abs, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti human ace2 ectodomain polyclonal abs/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    goat anti human ace2 ectodomain polyclonal abs - by Bioz Stars, 2026-03
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Co-precipitation of recombinant S450–650 with ACE2 in the lysate of Vero E6 cells. Vero E6 cells (1 × 10 6 ) were sequentially treated with goat anti-human ACE2 Abs, or goat IgG (2 μg), and FITC-conjugated rabbit anti-goat IgG. The stained cells were subjected to flow cytometric analysis for determination of ACE2 expression on the cell surface (A). For the co-precipitation experiment (B), Vero E6 cells (2.5 × 10 7 ) were treated with, or without, recombinant S450–650 (15 μg/ml) at 4 °C for 1 h. After washes, the cells were lysed using lysis buffer and the lysate treated with PT31 serum followed by protein-A/G-agarose precipitation. The precipitated materials were run on SDS-PAGE 12% gels and the protein bands transferred to nitrocellulose membranes for WB assays using goat anti-human ACE2 Abs as the first Abs, the detection Abs were HRP-labeled rabbit anti-goat IgG. In a parallel experiment (C), lysate of the S450–650-treated, or untreated, Vero E6 cells were precipitated using goat anti-human ACE2 Abs and protein-A/G-agarose. The precipitates were assayed by WB using PT31 serum (first Ab) and HRP-labeled goat anti-human IgG (detection Ab).

    Journal: Virology

    Article Title: A study on antigenicity and receptor-binding ability of fragment 450–650 of the spike protein of SARS coronavirus

    doi: 10.1016/j.virol.2006.09.022

    Figure Lengend Snippet: Co-precipitation of recombinant S450–650 with ACE2 in the lysate of Vero E6 cells. Vero E6 cells (1 × 10 6 ) were sequentially treated with goat anti-human ACE2 Abs, or goat IgG (2 μg), and FITC-conjugated rabbit anti-goat IgG. The stained cells were subjected to flow cytometric analysis for determination of ACE2 expression on the cell surface (A). For the co-precipitation experiment (B), Vero E6 cells (2.5 × 10 7 ) were treated with, or without, recombinant S450–650 (15 μg/ml) at 4 °C for 1 h. After washes, the cells were lysed using lysis buffer and the lysate treated with PT31 serum followed by protein-A/G-agarose precipitation. The precipitated materials were run on SDS-PAGE 12% gels and the protein bands transferred to nitrocellulose membranes for WB assays using goat anti-human ACE2 Abs as the first Abs, the detection Abs were HRP-labeled rabbit anti-goat IgG. In a parallel experiment (C), lysate of the S450–650-treated, or untreated, Vero E6 cells were precipitated using goat anti-human ACE2 Abs and protein-A/G-agarose. The precipitates were assayed by WB using PT31 serum (first Ab) and HRP-labeled goat anti-human IgG (detection Ab).

    Article Snippet: Goat anti-human ACE2 ectodomain polyclonal Abs was purchased from R&D systems (Minneapolis, MN, USA).

    Techniques: Recombinant, Staining, Expressing, Lysis, SDS Page, Labeling

    ACE2 interaction with the β5 and β6 strands of S-RBM. (A) Crystal structure of the RBD in complex of human receptor ACE2 as reported by Li and co-workers . Details of the binding interface between S-RBM and the ACE2 molecule and calculation results of the contact area and binding energy are shown in panels B and C, respectively. The S protein-binding areas of the ACE2 molecule (purple) are colored in green and the β5 and β6 strands in gold. The binding energy here is the energy required to disassemble the RBD-ACE2 complex into separate parts. The figure is prepared using PYMOL and contact area and binding energy calculated by SPDBV. PDB file accession number is 2AJF.

    Journal: Virology

    Article Title: A study on antigenicity and receptor-binding ability of fragment 450–650 of the spike protein of SARS coronavirus

    doi: 10.1016/j.virol.2006.09.022

    Figure Lengend Snippet: ACE2 interaction with the β5 and β6 strands of S-RBM. (A) Crystal structure of the RBD in complex of human receptor ACE2 as reported by Li and co-workers . Details of the binding interface between S-RBM and the ACE2 molecule and calculation results of the contact area and binding energy are shown in panels B and C, respectively. The S protein-binding areas of the ACE2 molecule (purple) are colored in green and the β5 and β6 strands in gold. The binding energy here is the energy required to disassemble the RBD-ACE2 complex into separate parts. The figure is prepared using PYMOL and contact area and binding energy calculated by SPDBV. PDB file accession number is 2AJF.

    Article Snippet: Goat anti-human ACE2 ectodomain polyclonal Abs was purchased from R&D systems (Minneapolis, MN, USA).

    Techniques: Binding Assay, Protein Binding