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apoe protein  (MedChemExpress)


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    Structured Review

    MedChemExpress apoe protein
    Apoe Protein, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/apoe protein/product/MedChemExpress
    Average 94 stars, based on 2 article reviews
    apoe protein - by Bioz Stars, 2026-06
    94/100 stars

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    (a) SDS-PAGE analysis showing successful cross-linking of the heterodimeric <t>TREM2</t> ECD /Trx-ApoE3 complex. (b) Representative high-quality MS/MS spectra of inter-protein cross-linked peptides. (c) Bar representation showing intra-protein XLs, inter-protein XLs, and inter-protein self-links. Figure was created using xiNET . ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299).
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    (A–C) FESEM images and (D–F) corresponding analysis images and (i–iii) histograms of <t>APO,</t> <t>BLG,</t> and LYS hydrogels, respectively. Macroscopic images of self-standing hydrogels are also included (A–C inset).
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    Image Search Results


    (a) SDS-PAGE analysis showing successful cross-linking of the heterodimeric TREM2 ECD /Trx-ApoE3 complex. (b) Representative high-quality MS/MS spectra of inter-protein cross-linked peptides. (c) Bar representation showing intra-protein XLs, inter-protein XLs, and inter-protein self-links. Figure was created using xiNET . ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299).

    Journal: bioRxiv

    Article Title: XL-MS and De Novo Protein Design Identified a Common Motif for TREM2 Binding

    doi: 10.64898/2026.04.23.720433

    Figure Lengend Snippet: (a) SDS-PAGE analysis showing successful cross-linking of the heterodimeric TREM2 ECD /Trx-ApoE3 complex. (b) Representative high-quality MS/MS spectra of inter-protein cross-linked peptides. (c) Bar representation showing intra-protein XLs, inter-protein XLs, and inter-protein self-links. Figure was created using xiNET . ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299).

    Article Snippet: 20 μM Trx-ApoE3 (Sino Biological 10817-H30E) and 20 μM TREM2 ectodomain were incubated for 1 h at 4°C.

    Techniques: SDS Page, Tandem Mass Spectroscopy

    (a) Mapping intra-ApoE3 cross-links onto the NMR structure (pdb 2L7B). Red line: incompatible XLs with Cβ-Cβ solvent accessible surface distance (SASD) > 35 Å. Blue line: compatible XLs. (b) Filtering the structure ensemble of ApoE3 (Protein Ensemble Database PED07094) by intra-ApoE3 XLs yielded Model 49 with the highest structural compatibility. (c) The best-scoring model of TREM2/ApoE3 complex generated using Haddock. (d) Zoom-in view of the binding interface. ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299). TREM2 ECD : CDR1(residue 40-42), CDR2(residue 69-72), and CDR3 (residue 88-91).

    Journal: bioRxiv

    Article Title: XL-MS and De Novo Protein Design Identified a Common Motif for TREM2 Binding

    doi: 10.64898/2026.04.23.720433

    Figure Lengend Snippet: (a) Mapping intra-ApoE3 cross-links onto the NMR structure (pdb 2L7B). Red line: incompatible XLs with Cβ-Cβ solvent accessible surface distance (SASD) > 35 Å. Blue line: compatible XLs. (b) Filtering the structure ensemble of ApoE3 (Protein Ensemble Database PED07094) by intra-ApoE3 XLs yielded Model 49 with the highest structural compatibility. (c) The best-scoring model of TREM2/ApoE3 complex generated using Haddock. (d) Zoom-in view of the binding interface. ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299). TREM2 ECD : CDR1(residue 40-42), CDR2(residue 69-72), and CDR3 (residue 88-91).

    Article Snippet: 20 μM Trx-ApoE3 (Sino Biological 10817-H30E) and 20 μM TREM2 ectodomain were incubated for 1 h at 4°C.

    Techniques: Solvent, Generated, Binding Assay, Residue

    (a-m) Design models of mini-proteins in complex with TREM2 ECD (left) and binding affinity determined by microscale thermophoresis (right). Numbers in brackets represent the 68.3% confidence interval calculated by “error-surface projection” .

    Journal: bioRxiv

    Article Title: XL-MS and De Novo Protein Design Identified a Common Motif for TREM2 Binding

    doi: 10.64898/2026.04.23.720433

    Figure Lengend Snippet: (a-m) Design models of mini-proteins in complex with TREM2 ECD (left) and binding affinity determined by microscale thermophoresis (right). Numbers in brackets represent the 68.3% confidence interval calculated by “error-surface projection” .

    Article Snippet: 20 μM Trx-ApoE3 (Sino Biological 10817-H30E) and 20 μM TREM2 ectodomain were incubated for 1 h at 4°C.

    Techniques: Binding Assay, Microscale Thermophoresis

    (a) SDS-PAGE analysis showing successful cross-linking of the heterodimeric TREM2 ECD /Trx-ApoE3 complex. (b) Representative high-quality MS/MS spectra of inter-protein cross-linked peptides. (c) Bar representation showing intra-protein XLs, inter-protein XLs, and inter-protein self-links. Figure was created using xiNET . ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299).

    Journal: bioRxiv

    Article Title: XL-MS and De Novo Protein Design Identified a Common Motif for TREM2 Binding

    doi: 10.64898/2026.04.23.720433

    Figure Lengend Snippet: (a) SDS-PAGE analysis showing successful cross-linking of the heterodimeric TREM2 ECD /Trx-ApoE3 complex. (b) Representative high-quality MS/MS spectra of inter-protein cross-linked peptides. (c) Bar representation showing intra-protein XLs, inter-protein XLs, and inter-protein self-links. Figure was created using xiNET . ApoE3: light blue (N-terminal region, residues 1-167), light yellow (hinge region, residues 168-205), and pink (C-terminal region, residues 206-299).

    Article Snippet: 20 μM Trx-ApoE3 (Sino Biological 10817-H30E) and 20 μM TREM2 ectodomain were incubated for 1 h at 4°C.

    Techniques: SDS Page, Tandem Mass Spectroscopy

    (A–C) FESEM images and (D–F) corresponding analysis images and (i–iii) histograms of APO, BLG, and LYS hydrogels, respectively. Macroscopic images of self-standing hydrogels are also included (A–C inset).

    Journal: ACS Applied Materials & Interfaces

    Article Title: Integrating Deep Learning and Real-Time Imaging to Visualize In Situ Self-Assembly of Self-Healing Interpenetrating Polymer Networks Formed by Protein and Polysaccharide Fibers

    doi: 10.1021/acsami.5c11459

    Figure Lengend Snippet: (A–C) FESEM images and (D–F) corresponding analysis images and (i–iii) histograms of APO, BLG, and LYS hydrogels, respectively. Macroscopic images of self-standing hydrogels are also included (A–C inset).

    Article Snippet: Horse spleen from APO protein, BLG from bovine milk protein, and LYZ from hen egg white protein were purchased from MERCK LIFE SCIENCE SLU.

    Techniques:

    (A–C) Hydrogel disc exterior HRSEM images and (D–F) hydrogel disc interior HRSEM images of APO-, BLG-, and LYS-PHY IPN hydrogels, respectively. The red arrows highlight the brighter protein fibers. Macroscopic images of hydrogel discs are also included (insets). (G–L) Corresponding analysis images.

    Journal: ACS Applied Materials & Interfaces

    Article Title: Integrating Deep Learning and Real-Time Imaging to Visualize In Situ Self-Assembly of Self-Healing Interpenetrating Polymer Networks Formed by Protein and Polysaccharide Fibers

    doi: 10.1021/acsami.5c11459

    Figure Lengend Snippet: (A–C) Hydrogel disc exterior HRSEM images and (D–F) hydrogel disc interior HRSEM images of APO-, BLG-, and LYS-PHY IPN hydrogels, respectively. The red arrows highlight the brighter protein fibers. Macroscopic images of hydrogel discs are also included (insets). (G–L) Corresponding analysis images.

    Article Snippet: Horse spleen from APO protein, BLG from bovine milk protein, and LYZ from hen egg white protein were purchased from MERCK LIFE SCIENCE SLU.

    Techniques:

    (A–C) Hydrogel disc exterior SEM images and (D–F) hydrogel disc interior SEM images of APO-, BLG-, and LYS-PHY IPN hydrogels, respectively. (G,–L) CNN analysis images. Blue color: PHY and magenta color: AF; (i–vi) the corresponding histograms are also shown.

    Journal: ACS Applied Materials & Interfaces

    Article Title: Integrating Deep Learning and Real-Time Imaging to Visualize In Situ Self-Assembly of Self-Healing Interpenetrating Polymer Networks Formed by Protein and Polysaccharide Fibers

    doi: 10.1021/acsami.5c11459

    Figure Lengend Snippet: (A–C) Hydrogel disc exterior SEM images and (D–F) hydrogel disc interior SEM images of APO-, BLG-, and LYS-PHY IPN hydrogels, respectively. (G,–L) CNN analysis images. Blue color: PHY and magenta color: AF; (i–vi) the corresponding histograms are also shown.

    Article Snippet: Horse spleen from APO protein, BLG from bovine milk protein, and LYZ from hen egg white protein were purchased from MERCK LIFE SCIENCE SLU.

    Techniques:

    3D CLSM images of (A) ATTO488-APO, (B) ATTO488-BLG, (C) ATTO488-LYS, (D) pure PHY, (E) ATTO488-APO-PHY, (F) ATTO488-BLG-PHY, (G) ATTO488-LYS-PHY, and (H) ATTO488-PHY hydrogels. (i–iv) Hydrogel discs under white light and (v–viii) under UV light irradiation.

    Journal: ACS Applied Materials & Interfaces

    Article Title: Integrating Deep Learning and Real-Time Imaging to Visualize In Situ Self-Assembly of Self-Healing Interpenetrating Polymer Networks Formed by Protein and Polysaccharide Fibers

    doi: 10.1021/acsami.5c11459

    Figure Lengend Snippet: 3D CLSM images of (A) ATTO488-APO, (B) ATTO488-BLG, (C) ATTO488-LYS, (D) pure PHY, (E) ATTO488-APO-PHY, (F) ATTO488-BLG-PHY, (G) ATTO488-LYS-PHY, and (H) ATTO488-PHY hydrogels. (i–iv) Hydrogel discs under white light and (v–viii) under UV light irradiation.

    Article Snippet: Horse spleen from APO protein, BLG from bovine milk protein, and LYZ from hen egg white protein were purchased from MERCK LIFE SCIENCE SLU.

    Techniques: Irradiation