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cell culture expressing epha2 crd  (MedChemExpress)


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    MedChemExpress cell culture expressing epha2 crd
    FIGURE 4 Analysis of S1-mediated crystal lattice packing interactions in <t>FabS1CE-C1:-EPHA2-CRD</t> and FabS1C-C1 structures. (a) Crystal lattice packing arrangement (upper panel) with symmetry mates, and asymmetric unit (lower panel) of (i) FabS1CE-C1: EPHA2-CRD (P3221 space group, trigonal crystal system), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group, monoclinic crystal system), and (iii) FabS1C-C1 (P21 space group). ASU Fab heavy- and light-chains are colored light blue or gray, respectively. Symmetry mate Fab heavy- and light-chains are colored dark blue and green, respectively. EPHA2-CRD is colored magenta. The heavy- and light-chain variable (VH and VL) and constant domains (CH and CL) of the Fab are labeled in (i). (b) S1 substitutions (Q165S and K167Y) and residues in the nearby loop region (N170, A171, L172. S174) cooperate to form crystal lattice packing sites in the following structures: (i) FabS1CE-C1: EPHA2-CRD (P3221 space group), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group), and (iii and iv) FabS1C-C1. NB: In the S1-crystal lattice packing site of FabS1CE-C1:EPHA2-CRD (P21 space group) (ii), the K72 side chain of the packing Fab VH domain remains partially unresolved from the electron density indicating a dynamic interaction.
    Cell Culture Expressing Epha2 Crd, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cell culture expressing epha2 crd/product/MedChemExpress
    Average 91 stars, based on 3 article reviews
    cell culture expressing epha2 crd - by Bioz Stars, 2026-04
    91/100 stars

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    1) Product Images from "Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes."

    Article Title: Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes.

    Journal: Protein science : a publication of the Protein Society

    doi: 10.1002/pro.4824

    FIGURE 4 Analysis of S1-mediated crystal lattice packing interactions in FabS1CE-C1:-EPHA2-CRD and FabS1C-C1 structures. (a) Crystal lattice packing arrangement (upper panel) with symmetry mates, and asymmetric unit (lower panel) of (i) FabS1CE-C1: EPHA2-CRD (P3221 space group, trigonal crystal system), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group, monoclinic crystal system), and (iii) FabS1C-C1 (P21 space group). ASU Fab heavy- and light-chains are colored light blue or gray, respectively. Symmetry mate Fab heavy- and light-chains are colored dark blue and green, respectively. EPHA2-CRD is colored magenta. The heavy- and light-chain variable (VH and VL) and constant domains (CH and CL) of the Fab are labeled in (i). (b) S1 substitutions (Q165S and K167Y) and residues in the nearby loop region (N170, A171, L172. S174) cooperate to form crystal lattice packing sites in the following structures: (i) FabS1CE-C1: EPHA2-CRD (P3221 space group), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group), and (iii and iv) FabS1C-C1. NB: In the S1-crystal lattice packing site of FabS1CE-C1:EPHA2-CRD (P21 space group) (ii), the K72 side chain of the packing Fab VH domain remains partially unresolved from the electron density indicating a dynamic interaction.
    Figure Legend Snippet: FIGURE 4 Analysis of S1-mediated crystal lattice packing interactions in FabS1CE-C1:-EPHA2-CRD and FabS1C-C1 structures. (a) Crystal lattice packing arrangement (upper panel) with symmetry mates, and asymmetric unit (lower panel) of (i) FabS1CE-C1: EPHA2-CRD (P3221 space group, trigonal crystal system), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group, monoclinic crystal system), and (iii) FabS1C-C1 (P21 space group). ASU Fab heavy- and light-chains are colored light blue or gray, respectively. Symmetry mate Fab heavy- and light-chains are colored dark blue and green, respectively. EPHA2-CRD is colored magenta. The heavy- and light-chain variable (VH and VL) and constant domains (CH and CL) of the Fab are labeled in (i). (b) S1 substitutions (Q165S and K167Y) and residues in the nearby loop region (N170, A171, L172. S174) cooperate to form crystal lattice packing sites in the following structures: (i) FabS1CE-C1: EPHA2-CRD (P3221 space group), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group), and (iii and iv) FabS1C-C1. NB: In the S1-crystal lattice packing site of FabS1CE-C1:EPHA2-CRD (P21 space group) (ii), the K72 side chain of the packing Fab VH domain remains partially unresolved from the electron density indicating a dynamic interaction.

    Techniques Used: Labeling



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    cell culture expressing epha2 crd  (MedChemExpress)
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    MedChemExpress cell culture expressing epha2 crd
    FIGURE 4 Analysis of S1-mediated crystal lattice packing interactions in <t>FabS1CE-C1:-EPHA2-CRD</t> and FabS1C-C1 structures. (a) Crystal lattice packing arrangement (upper panel) with symmetry mates, and asymmetric unit (lower panel) of (i) FabS1CE-C1: EPHA2-CRD (P3221 space group, trigonal crystal system), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group, monoclinic crystal system), and (iii) FabS1C-C1 (P21 space group). ASU Fab heavy- and light-chains are colored light blue or gray, respectively. Symmetry mate Fab heavy- and light-chains are colored dark blue and green, respectively. EPHA2-CRD is colored magenta. The heavy- and light-chain variable (VH and VL) and constant domains (CH and CL) of the Fab are labeled in (i). (b) S1 substitutions (Q165S and K167Y) and residues in the nearby loop region (N170, A171, L172. S174) cooperate to form crystal lattice packing sites in the following structures: (i) FabS1CE-C1: EPHA2-CRD (P3221 space group), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group), and (iii and iv) FabS1C-C1. NB: In the S1-crystal lattice packing site of FabS1CE-C1:EPHA2-CRD (P21 space group) (ii), the K72 side chain of the packing Fab VH domain remains partially unresolved from the electron density indicating a dynamic interaction.
    Cell Culture Expressing Epha2 Crd, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cell culture expressing epha2 crd/product/MedChemExpress
    Average 91 stars, based on 1 article reviews
    cell culture expressing epha2 crd - by Bioz Stars, 2026-04
    91/100 stars
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    FIGURE 4 Analysis of S1-mediated crystal lattice packing interactions in FabS1CE-C1:-EPHA2-CRD and FabS1C-C1 structures. (a) Crystal lattice packing arrangement (upper panel) with symmetry mates, and asymmetric unit (lower panel) of (i) FabS1CE-C1: EPHA2-CRD (P3221 space group, trigonal crystal system), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group, monoclinic crystal system), and (iii) FabS1C-C1 (P21 space group). ASU Fab heavy- and light-chains are colored light blue or gray, respectively. Symmetry mate Fab heavy- and light-chains are colored dark blue and green, respectively. EPHA2-CRD is colored magenta. The heavy- and light-chain variable (VH and VL) and constant domains (CH and CL) of the Fab are labeled in (i). (b) S1 substitutions (Q165S and K167Y) and residues in the nearby loop region (N170, A171, L172. S174) cooperate to form crystal lattice packing sites in the following structures: (i) FabS1CE-C1: EPHA2-CRD (P3221 space group), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group), and (iii and iv) FabS1C-C1. NB: In the S1-crystal lattice packing site of FabS1CE-C1:EPHA2-CRD (P21 space group) (ii), the K72 side chain of the packing Fab VH domain remains partially unresolved from the electron density indicating a dynamic interaction.

    Journal: Protein science : a publication of the Protein Society

    Article Title: Engineered antigen-binding fragments for enhanced crystallization of antibody:antigen complexes.

    doi: 10.1002/pro.4824

    Figure Lengend Snippet: FIGURE 4 Analysis of S1-mediated crystal lattice packing interactions in FabS1CE-C1:-EPHA2-CRD and FabS1C-C1 structures. (a) Crystal lattice packing arrangement (upper panel) with symmetry mates, and asymmetric unit (lower panel) of (i) FabS1CE-C1: EPHA2-CRD (P3221 space group, trigonal crystal system), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group, monoclinic crystal system), and (iii) FabS1C-C1 (P21 space group). ASU Fab heavy- and light-chains are colored light blue or gray, respectively. Symmetry mate Fab heavy- and light-chains are colored dark blue and green, respectively. EPHA2-CRD is colored magenta. The heavy- and light-chain variable (VH and VL) and constant domains (CH and CL) of the Fab are labeled in (i). (b) S1 substitutions (Q165S and K167Y) and residues in the nearby loop region (N170, A171, L172. S174) cooperate to form crystal lattice packing sites in the following structures: (i) FabS1CE-C1: EPHA2-CRD (P3221 space group), (ii) FabS1CE-C1:EPHA2-CRD (P21 space group), and (iii and iv) FabS1C-C1. NB: In the S1-crystal lattice packing site of FabS1CE-C1:EPHA2-CRD (P21 space group) (ii), the K72 side chain of the packing Fab VH domain remains partially unresolved from the electron density indicating a dynamic interaction.

    Article Snippet: Cell culture expressing EPHA2-CRD or antigen-B was supplemented with 5 mM Kifunensine (MedChemExpress) to inhibit mannosidase I activity.

    Techniques: Labeling