Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: Produced anti-TREM2-anti-TfR constructs

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Produced, Construct

Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: Binding of IgG-scFv₂, IgG-scFab, and scFv-VHH to (a) murine TREM2 protein, (b) human TREM2 protein and (c) murine transferrin receptor (TfR) protein, measured by absorbance in ELISA

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: (a) Schematic illustration of the anti-TREM2 antibody formats that were carried forward. (b) Brain concentration of 125 I-labeled bispecific anti-TREM2 antibodies, expressed as percentage of injected dose per gram of brain tissue 2 h post injection. WT n = 13. One-way ANOVA followed by Tukey’s multiple comparisons test (* p < 0.05, ** p < 0.01), mean ± SD

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Concentration Assay, Labeling, Injection

Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: (a) Blood-time concentration (%ID/g of blood) curves up to 72 h post injections (p.i.). Brain concentration of 125 I-labeled bispecific anti-TREM2 antibodies 48 h p.i. (b) expressed as percentage of injected dose per gram of brain tissue (%ID/g of brain) and as (c) brain-to-blood concentration ratio (App NL−G−F n = 10, WT n = 12). Brain concentration of 125 I-labeled bispecific anti-TREM2 antibodies 72 h p.i. (d) expressed as %ID/g of brain and as (e) brain-to-blood concentration ratio (App NL−G−F n = 12, WT n = 13). ( f ) Brain concentration of [ 125 I]IgG-scFv 2 72 h p.i. in App NL−G−F mice untreated ( n = 3) or pre-treated ( n = 3) with a 50-fold higher dose of IgG-scFv 2 four days prior. ( g ) Representative ex vivo autoradiography showing binding of [ 125 I]IgG-scFv 2 72 h p.i. in saggital brain sections prepared from untreated and pre-treated litter mates. Student’s t-test (* p < 0.05, ** p < 0.01, *** p < 0.001), mean ± SD

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Concentration Assay, Labeling, Injection, Ex Vivo, Autoradiography, Binding Assay

Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: Radiolabeling of IgG-scFv 2 with 124 I did not significantly alter the (a) binding to murine TREM2 protein or (b) murine TfR. (c) Experimental workflow for PET-imaging of [ 124 I]IgG-scFv 2 72 h post injection (p.i.). Blood samples were collected from the tail vein at 30 min, 1 h, 2 h, 4 h, 6 h, 24 h, 48 h p.i. Terminal blood samples were collected from the heart prior to transcardial perfusion 72 h p.i. Radioactivity in the collected organs was measured using a γ-counter. (d-f ) PET-imaging showed significantly higher in vivo brain concentration of [ 124 I]IgG-scFv 2 in App NL−G−F mice in comparison to WT mice, (g) which was confirmed by ex vivo measurements. (h) Blood-time concentration (%ID/g of blood) and (i) organ biodistribution 72 h p.i. (App NL−G−F n = 4, WT n = 4). Student’s t-test, Two-way ANOVA followed by Šídák’s multiple comparisons test (* p < 0.05, ** p < 0.01), mean ± SD

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Radioactivity, Binding Assay, Imaging, Injection, In Vivo, Concentration Assay, Comparison, Ex Vivo

Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: (a) TREM2 levels in TBST-extracted brain homogenate were significantly higher in the App NL−G−F mice in comparison to WT mice (App NL−G−F n = 39, WT n = 42). Significant correlations between TREM2 concentrations in brain homogenate and brain concentration (%ID/g) of injected antibody were detected at 72 h p.i. of (b) [ 125 I]IgG-scFv 2 (App NL−G−F n = 6, WT n = 6) and (c) [ 124 I]IgG-scFv 2 (App NL−G−F n = 4, WT n = 4). Mann Whitney test, Pearson correlation test (r), Simple linear regression (R 2 ) (** p < 0.01, **** p < 0.0001), mean ± SD

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Comparison, Concentration Assay, Injection, MANN-WHITNEY

Journal: European Journal of Nuclear Medicine and Molecular Imaging

Article Title: PET imaging of TREM2 in amyloid-beta induced neuroinflammation

doi: 10.1007/s00259-025-07358-0

Figure Lengend Snippet: (a) Aβ38, Aβ40, and Aβ42 concentrations were measured in formic acid-extracted brain homogenate from App NL−G−F mice ( n = 39). Significant correlations between TREM2 concentration and concentration of (b) Aβ38 and (c) Aβ40 were detected in the brain homogenate. (d) Levels of TREM2 and Aβ42 did not correlate. Kruskal-Wallis test followed by Dunn’s multiple comparisons test. Pearson correlation test (r), Simple linear regression (R 2 ) (* p < 0.05, ** p < 0.01, **** p < 0.0001), mean ± SD

Article Snippet: The plate was coated with the following proteins diluted in phosphate buffered saline (PBS): murine TfR protein (0.5 μg/mL, in-house produced), murine TREM2 protein (5 μg/mL, SinoBiological, 158–50149-M02H-100) and human TREM2 protein (0.5 μg/mL, SinoBiological, 158–11084-H08H-100).

Techniques: Concentration Assay

Journal: Neuroreport

Article Title: Regulation of TREM2 expression by an NF-?B-sensitive miRNA-34a

doi: 10.1097/WNR.0b013e32835fb6b0

Figure Lengend Snippet: hsa-miRNA-34a-TREM2-mRNA-3′-UTR complementarity map. The free energy of association (EA) between hsa-miRNA-34a and the TREM2 mRNA-3′-UTR is ~16 kcal/mol; the miRNA-34a seed sequence 3′-UGUGACGG-5′ is highlighted in yellow; the complementary TREM2-3′-UTR recognition sequence 5′-ACACTGCT-3′ is highlighted in red; an ‘|’ indicates a full hydrogen bond between miRNA-34a and the TREM2-mRNA-3′-UTR and a ‘:’ indicates a partial hydrogen bond; the hsa-miRNA-34a recognition feature is located about midway in the 299 basepair TREM2-3′-UTR; several other brain miRNAs located within the TREM2-3′-UTR and may also affect TREM2 mRNA stability and regulate its expression (data not shown); notably, the TREM2 gene has no strong NF-κB binding site within at least 11 kb of its transcription start site; ribonucleotide sequences and alignment derived using miRBASE algorithms (European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton UK; http://www.ebi.ac.uk/enright-srv/microcosm/cgi-bin/targets/v5/detail_view.pl?transcript_id=ENST00000373113); [3–6,8,20].

Article Snippet: Western analysis of TREM2 and β-actin in brain tissues and microglial cells Western immunoblotting was performed for quantification of TREM2 and β-actin protein using human-specific primary antibodies directed against the control protein marker β-actin (3598–100; Sigma-Aldrich Chemical Company) or human or murine TREM2 (B3; sc-373828, H160; sc-49764 or M227; sc-48765; Santa Cruz Biotechnologies, Santa Cruz, California, USA) [ 9 , 11 ].

Techniques: Sequencing, Expressing, Binding Assay, Derivative Assay

Journal: Neuroreport

Article Title: Regulation of TREM2 expression by an NF-?B-sensitive miRNA-34a

doi: 10.1097/WNR.0b013e32835fb6b0

Figure Lengend Snippet: Western analysis in control and AD hippocampal CA1. Quantitation of levels of the 25.4 kDa TREM2 protein compared with the 42.2 kDa β-actin (ACTB; 374 amino acids) in the same sample; the highest abundance of TREM2 was found in the hippocampal CA1 at levels about 5 × more abundant compared with the neocortex; the two controls and two AD samples are obtained from short PMI tissues having a PMI of 2 h or less (further described in the text and legend to Fig. 1); results using TREM2 antibody [sc-373828 shown; the pools of control (N = 9)] and AD (N = 12) were derived from pooled whole brain extracts of short PMI tissues having a mean PMI of ~2 h; age range 66–74 for control and AD samples; TREM2 protein levels in AD samples and pools ranged between 0.32 and 0.58 of controls; *P<0.05; **P<0.01 (analysis of variance) [8–16]. AD, Alzheimer’s disease; PMI, postmortem interval.

Article Snippet: Western analysis of TREM2 and β-actin in brain tissues and microglial cells Western immunoblotting was performed for quantification of TREM2 and β-actin protein using human-specific primary antibodies directed against the control protein marker β-actin (3598–100; Sigma-Aldrich Chemical Company) or human or murine TREM2 (B3; sc-373828, H160; sc-49764 or M227; sc-48765; Santa Cruz Biotechnologies, Santa Cruz, California, USA) [ 9 , 11 ].

Techniques: Western Blot, Control, Quantitation Assay, Derivative Assay

Journal: Neuroreport

Article Title: Regulation of TREM2 expression by an NF-?B-sensitive miRNA-34a

doi: 10.1097/WNR.0b013e32835fb6b0

Figure Lengend Snippet: Functional validation of hsa miRNA-34a-TREM2–3′UTR interaction. (a) CRL-2467 murine microglial cells, phase contrast 20×. (b) TREM2-mRNA-3′-UTR expression vector luciferase reporter assay (pLightSwitch-3′UTR; Cat #S801178; Switchgear Genomics). In this vector, the entire 299 nucleotide TREM2 3′-UTR was ligated into the unique Nhe1-Xho1 site. The transfected cells were treated exogenously with a control LNA-protected miRNA-183 or miRNA-34a and/or anti-miRNA-183 (AM-183), anti-miRNA-34a (AM-34a), or a scrambled anti-miRNA-34a (AMsc-34a) [18,19]. (c) Although the control vector ACTB-3′-UTR showed no significant effects on the relative luciferase signal yield after treatment with either miRNA-183 or miRNA-34a (dashed horizontal line set to 1.0), the TREM2-mRNA-3′-UTR vector exhibited reduced luciferase signal to a mean of 0.22-fold over controls. An exogenously added anti-miRNA-183 (AM-183) control or a scrambled anti-miRNA-34a (AMsc-34a; data not shown) showed no effect on the luciferase signal, whereas an anti-miRNA-34a (AM-34a) restored luciferase expression to near homeostatic levels; N = 3; *P<0.01 (analysis of variance). The results suggest an miRNA-34a-mediated downregulation of TREM2 expression in stressed microglial cells may be related to the downregulation of other immune system genes by proinflammatory miRNAs (such as complement factor H) [8,9,14] and/or an impairment in cellular phagocytosis or related signaling [5–7,20,21].

Article Snippet: Western analysis of TREM2 and β-actin in brain tissues and microglial cells Western immunoblotting was performed for quantification of TREM2 and β-actin protein using human-specific primary antibodies directed against the control protein marker β-actin (3598–100; Sigma-Aldrich Chemical Company) or human or murine TREM2 (B3; sc-373828, H160; sc-49764 or M227; sc-48765; Santa Cruz Biotechnologies, Santa Cruz, California, USA) [ 9 , 11 ].

Techniques: Functional Assay, Biomarker Discovery, Expressing, Plasmid Preparation, Luciferase, Reporter Assay, Transfection, Control

Journal: EMBO Molecular Medicine

Article Title: TREM2 deficiency reduces the efficacy of immunotherapeutic amyloid clearance

doi: 10.15252/emmm.201606370

Figure Lengend Snippet: Schematic of the mouse Trem2 locus and the TREM2 protein. Sequence alignment of wild‐type N9 (N9 wt) and TREM2 mutant N9 (N9 mu) surrounding the gRNA target site. The gRNA sequence is in cyan, and protospacer‐adjacent motif (PAM) is marked with a line. The single nucleotide insertion is labeled in red. Schematic representation of wild‐type TREM2 (NP_112544.1) and CRISPR/Cas9‐modified TREM2 (N9 mu). TM, transmembrane domain; SP, signal peptide. Western blot analysis of lysates and media from wt and mutant N9 cells (N9 wt /mu) using the antibody anti‐murine TREM2 (clone 5F4), which is raised against the murine TREM2 extracellular domain. sTREM2, soluble TREM2. *indicate unspecific bands. Calnexin was used as a loading control. Phagocytosis of 1 μM HiLyte ™ Fluor 488 Aβ 1‐42 (fAβ 42 ) by N9 wt and N9 mu in the presence or absence of antibody 2D8 or the non‐binding antibody 6687. Cytochalasin D (CytoD, 10 mM) was used as control to verify phagocytic uptake. ( n = 4, ± SEM; two‐way ANOVA, interaction P = 0.61, genotype P < 0.0001, treatment P = 0.0001; post hoc tests wt vs. mu for the following conditions: fAβ 42 P = 0.0043, fAβ 42 ‐2D8 P = 0.0436). Western blot of BMDM derived from wt and Trem2 knockout (ko) animals using antibody 5F4. *indicate unspecific bands. Phagocytosis of fAβ 42 by BMDM from wt and Trem2 ko animals in the presence or absence of 2D8, or the non‐binding control antibody 6687. ( n = 3, ± SEM; two‐way ANOVA, interaction P = 0.0005, genotype P < 0.0001, treatment P < 0.0001; post hoc tests wt vs. ko for the following conditions: fAβ 42 P = 0.0021, fAβ 42 ‐2D8 1 μg/ml P < 0.0001, fAβ 42 ‐2D8 5 μg/ml P < 0.0001, fAβ 42 ‐2D8 10 μg/ml P < 0.0001, fAβ 42 /6687 10 μg/ml P = 0.0007). Quantification of relative fAβ 42 uptake to lowest antibody concentration used ( n = 3, ± SEM). Phagocytosis of fAβ 42 by BMDM from wt and Trem2 ko animals in the presence or absence of mAb11, or an isotype control antibody (IC). ( n = 4, ± SEM; two‐way ANOVA, interaction P = 0.0223, genotype P < 0.0001, treatment P < 0.0001; post hoc tests wt vs. ko for the following conditions: fAβ 42 ‐mAb11 1 μg/ml P = 0.0391, fAβ 42 ‐mAb11 5 μg/ml P = 0.0069, fAβ 42 ‐mAb11 10 μg/ml P < 0.0001, fAβ 42 ‐mAb11 20 μg/ml P = 0.0001, fAβ 42 ‐mAb11 50 μg/ml P < 0.0001). Quantification of relative fAβ 42 uptake to lowest antibody concentration used ( n = 4, ± SEM). Recombinant mouse sTREM2 does not rescue fAβ 42 uptake in Trem2 ‐deficient BMDM. Increasing amounts of sTREM2 were added to the media of wt or Trem2 ko BMDM in the presence or absence of mAb11 (10 μg/ml) ( n = 4, ± SEM). Western blot of primary microglia from wt or Trem2 ko animals using antibody 5F4. *indicate unspecific bands. Phagocytosis of fAβ 42 by primary microglia from wt and Trem2 ko animals in the presence or absence of mAb11, or an isotype control antibody (IC). ( n = 5, ± SEM; two‐way ANOVA, interaction P = 0.4797, genotype P < 0.0001, treatment P < 0.0001; post hoc tests wt vs. ko for the following conditions: fAβ 42 ‐mAb11 5 μg/ml P = 0.0449, fAβ 42 ‐mAb11 10 μg/ml P = 0.0370, fAβ 42 ‐mAb11 20 μg/ml P = 0.0299, fAβ 42 ‐mAb11 50 μg/ml P = 0.0120). Quantification of relative fAβ 42 uptake to lowest antibody concentration used ( n = 5, ± SEM). Data information: (C, E, G, K) Quantification of internalized fAβ 42 was normalized to wt without antibody. Bonferroni‐corrected pair‐wise post hoc tests were used. Source data are available online for this figure.

Article Snippet: For Western blotting of TREM2, we raised a rat monoclonal antibody (clone 5F4; 1:50) against the extracellular domain of murine TREM2 (Creative Biomart; Trem2‐3276M).

Techniques: Sequencing, Mutagenesis, Labeling, CRISPR, Modification, Western Blot, Control, Binding Assay, Derivative Assay, Knock-Out, Concentration Assay, Recombinant

Journal: EMBO Molecular Medicine

Article Title: TREM2 deficiency reduces the efficacy of immunotherapeutic amyloid clearance

doi: 10.15252/emmm.201606370

Figure Lengend Snippet: Representative histograms for Fcγ‐receptors‐PE (FcγR‐PE) expression levels as used for quantification. Stacked histograms for log PE fluorescence intensity of wt and Trem2 ko BMDM are shown for the respective FcγR (I, IIB/III, and IV). Relative quantification of cell surface levels of FcγR molecules. Absolute number of cell surface FcγR‐PE molecules was determined by the BD QuantiBRITE® method (see methods section for details) and normalized to expression levels of the respective wt control. ( n = 4, ± SEM, t ‐test, two‐tailed; wt vs. ko: FcγRI‐PE P = 0.0008, FcγRIIB/III‐PE P = 0.0033, FcγRIV‐PE P = 0.7001). mRNA levels of FcγR are increased in Trem2 ko BMDM. Fold changes of the respective FcγR (I, IIB, III, IV) mRNA levels in Trem2 ko BMDM were determined by quantitative real‐time PCR. ( n = 6, ± SEM; one‐sample t ‐test, two‐tailed; wt vs. ko: FcγRI P = 0.0118, FcγRIIB P = 0.0006, FcγRIII P = 0.0004, FcγRIV P = 0.0284) Phosphorylated Syk (P‐Syk) and total Syk (T‐Syk) levels were determined by Western blotting in lysates from wt and Trem2 ko BMDM after 1 h treatment with Aβ alone, together with antibody 2D8 (Aβ‐2D8), or an isotype control (Aβ‐IC). Actin was used as a loading control. Quantification of P‐Syk normalized to T‐Syk. ( n = 4, ± SEM; 2 way ANOVA, interaction P = 0.0490, genotype P = 0.0898, treatment P < 0.0001. Bonferroni‐corrected pair‐wise post hoc tests, ** P = 0.0075 vs. wt). Source data are available online for this figure.

Article Snippet: For Western blotting of TREM2, we raised a rat monoclonal antibody (clone 5F4; 1:50) against the extracellular domain of murine TREM2 (Creative Biomart; Trem2‐3276M).

Techniques: Expressing, Fluorescence, Quantitative Proteomics, Control, Two Tailed Test, Real-time Polymerase Chain Reaction, Western Blot

Journal: EMBO Molecular Medicine

Article Title: TREM2 deficiency reduces the efficacy of immunotherapeutic amyloid clearance

doi: 10.15252/emmm.201606370

Figure Lengend Snippet: A BMDM from wt or Trem2 ko mice were cultured on APP/PS1 mice brain cryosections incubated with or without mAb11 (1 μg/ml) or an isotype control (IC; 1 μg/ml) for 24 h. Sections were then probed with methoxy‐X04. Scale bar, 500 μm. B The amyloid plaque load was quantified from the entire sagittal section. Sections incubated with medium (no cell) were set as baseline. ( n = 6, ± SEM; two‐way ANOVA, interaction P < 0.0001, genotype P < 0.0001, treatment P < 0.0001; Tukey's multiple comparisons tests; wt vs. ko for the following conditions: no antibody P = 0.0304, IC P = 0.0049, mAb11 P = 0.0212; wt: IC vs. wt: mAb11 P = 0.0008; ko: IC vs. ko: mAb11 P = 0.0001). C, D Equal numbers of wt and Trem2 ko BMDM were added, and cell numbers were analyzed after termination of experiments by quantifying the CD68‐positive cells on top of the sections. ( n = 4, ± SEM; t ‐test; n.s., non‐significant, P = 0.5004). Scale bar, 200 μm. E Aβ was extracted by urea buffer from replicate slices of the experiment shown in (A), and total Aβ was identified by Western blotting. Source data are available online for this figure.

Article Snippet: For Western blotting of TREM2, we raised a rat monoclonal antibody (clone 5F4; 1:50) against the extracellular domain of murine TREM2 (Creative Biomart; Trem2‐3276M).

Techniques: Cell Culture, Incubation, Control, Western Blot

Journal: EMBO Molecular Medicine

Article Title: TREM2 deficiency reduces the efficacy of immunotherapeutic amyloid clearance

doi: 10.15252/emmm.201606370

Figure Lengend Snippet: Cryosections from unfixed brain of 6‐month‐old APP/PS1 mice were pre‐incubated with increasing concentrations of mAb11 (0.001, 0.01, 0.1, 1, 5 μg/ml). BMDM from wt or Trem2 ko mice were added for 24 h. Sections were stained with methoxy‐X04. Scale bar, 500 μm. Methoxy‐X04 signals were quantified from the entire sagittal section. ( n = 5, ± SEM; two‐way ANOVA, interaction P = 0.0082, genotype P < 0.0001, treatment P < 0.0001. Fisher's LSD post hoc comparisons; * show statistics between wt and ko under the same experimental condition. # in black shows wt compares to no‐antibody stimulation; # in gray shows ko compares to no‐antibody stimulation; wt vs. ko for the following conditions: no antibody P = 0.0053, mAb11 0.001 μg/ml P = 0.0003, mAb11 0.01 μg/ml P < 0.0001, mAb11 0.1 μg/ml P = 0.0001, mAb11 1 μg/ml P = 0.0007, mAb11 5 μg/ml P = 0.0011; following conditions compare to wt/no antibody: wt/mAb11 0.01 μg/ml P = 0.0166, wt/mAb11 0.1 μg/ml P = 0.0002, wt/mAb11 1 μg/ml P < 0.0001, wt/mAb11 5 μg/ml P < 0.0001; following conditions compare to ko/no antibody: ko/mAb11 0.1 μg/ml P = 0.0099, ko/mAb11 1 μg/ml P < 0.0001, ko/mAb11 5 μg/ml P < 0.0001.

Article Snippet: For Western blotting of TREM2, we raised a rat monoclonal antibody (clone 5F4; 1:50) against the extracellular domain of murine TREM2 (Creative Biomart; Trem2‐3276M).

Techniques: Incubation, Staining