trem2 ectodomain  (Sino Biological)

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

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

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

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

Journal: Cell Genomics

Article Title: Single-cell profiling of bone metastasis ecosystems from multiple cancer types reveals convergent and divergent mechanisms of bone colonization

doi: 10.1016/j.xgen.2025.100888

Figure Lengend Snippet: Bone stromal drives divergent bone colonization and immune evasion mechanisms (A) Analysis of cell-cell communication signal flow. Outgoing signal strength is shown on the x axis and incoming signal strength on the y axis, comparing the Mφ-OC and Treg-Tex archetypes with healthy samples serving as references. (B) Identification of key ligand-receptor pairs that differentially regulate the OC populations. This analysis compares the relative signaling strengths between the Mφ-OC and Treg-Tex archetypes, focusing on osteoclasts as the signal receivers (from A). (C) Schematic illustration of in vitro experimental validation for estimated signaling molecules. CD14 + monocytes isolated from human peripheral blood were enriched for osteoclastogenesis induction, with selected factors added to the culture medium to test their predicted roles in regulating differential osteoclastogenesis. Osteoclastogenesis was then evaluated by both qPCR and TRAP staining. (D) qPCR analysis of osteoclast signature genes to validate differential osteoclastogenesis regulation by estimated signaling molecules. Each signaling factor was tested using graded concentrations: TWEAK (TNFSF12; 0.1, 1, 10 ng/μL), COMP (5, 50, 500 ng/μL), and NRG1 (10, 100, 1000 ng/μL), TNFSF10 (1, 10, 100 ng/μL), SEMA4A (1, 10, 100 ng/μL), EFNA5 (1, 10, 100 ng/μL), BMP8A (1, 10, 100 ng/μL). Each condition has five replicates. Statistical significance was assessed using one-way ANOVA, with significance levels: ∗ p < 0.05; ∗∗ p < 0.01; ∗∗∗ p < 0.001; ∗∗∗∗ p < 0.0001.

Article Snippet: recombinant human TNFSF10 , Sino Biological , Cat#10409-HNAE-100.

Techniques: In Vitro, Biomarker Discovery, Isolation, Staining