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Cell Signaling Technology Inc anti cd276
Anti Cd276, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/14058s/B7-H3+XP+Rabbit+mAb/pm41819470-134-32-34
Average 96 stars, based on 128 article reviews

anti cd276 - by Bioz Stars, 2026-10

96/100 stars

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Article Title: TNF-α-mediated epithelial-to-mesenchymal transition regulates expression of immune checkpoint molecules in hepatocellular carcinoma
Article Snippet: B7-H3 , 14058S , Cell Signaling Technology, Inc. , 1:1,000 , –.

Article Title: Extramammary Paget disease shows differential expression of B7 family members B7-H3, B7-H4, PD-L1, PD-L2 and cancer/testis antigens NY-ESO-1 and MAGE-A
Article Snippet: B7-H3 , D9M2L , Cell Signaling Technology , 14058S , 0.125.

Staining:

Article Title: Evaluation of PD-L1 and B7-H3 expression as a predictor of response to adjuvant chemotherapy in bladder cancer
Article Snippet: .. B7-H3 staining was conducted in our laboratory (D9M2L clone, Cell Signaling Technology, #14058S) and antibody specificity was validated using B7-H3 expressing and B7H3-knockout RH30 (rhabdomyosarcoma) tumor xenografts (Additional file : Fig. S1A). .. PD-L1 staining was performed by the Mayo Clinic Pathology Research Core (PRC) using the PD-L1 antibody E1L3N clone (Cell Signaling Technology, #13684S).

Article Title: Do we need B7-H3 immunohistochemistry for the inclusion of children with high-grade central nervous system tumors in clinical trials targeting B7-H3?
Article Snippet: Background: Pediatric high-grade central nervous system (pHG-CNS) tumors are the leading cause of childhood cancer-related deaths, partly due to poor response to standard treatments.. B7-H3 is reportedly expressed in pHGCNS tumors, making antigen-targeting therapies, including anti-B7-H3 chimeric antigen receptor T-cell (CAR-T) therapy, promising.. However, given substantial inter-tumoral protein expression diversity in CNS tumors, it’s unclear which patients might benefit from these treatments.

Expressing:

Polymer:

Article Title: HS-20093, a B7-H3-targeted antibody-drug conjugate in lung cancer: Results from the ARTEMIS-001 phase 1a/b trial.
Article Snippet: .. REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies B7-H3 (D9M2L)XP® Rabbit mAb Cell Signaling Technology Cat14058S; RRID: AB_2750877 Rabbit IgG, monoclonal [EPR25A] antibody Abcam Cat#ab172730; RRID: AB_2687931 Chemicals, peptides, and recombinant proteins HS-20093 Shanghai Hansoh Biomedical R&D Inc. Changzhou Hengbang Pharmaceutical CO., Ltd. N/A Critical commercial assays BONDTM Polymer Refine Detection Kit Leica Cat#DS9800-CN Software and algorithms SAS vision 9.4 SAS Institute https://www.sas.com/ Phoenix 8.3.5 Certara https://www.certara.com.cn/ software/phoenix-pkpd/ ll OPEN ACCESSArticle Cancer Cell 44, 1–12.e1–e3, April 13, 2026 e1 Please cite this article in press as: Duan et al., HS-20093, a B7-H3-targeted antibody-drug conjugate in lung cancer: Results from the ARTEMIS-001 phase 1a/b trial, Cancer Cell (2026), https://doi.org/10.1016/j.ccell.2026.02.006 ..

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Identification of downstream signaling pathways of ATIC using isobaric labeling with tandem mass tags and liquid chromatography tandem mass spectrometry proteomics analysis in BFTC909 cells transfected with negative control siRNA or ATIC siRNA. (A) In the volcano plot, scattered points represent the differential fold changes of various proteins. The x-axis shows the log2 fold change, while the y-axis displays the −log10-adjusted p-Values. Blue indicates a significant decrease, and red indicates a significant increase (p<0.05). (B) Differentially expressed protein (DEP) rank plot depicting the fold change between samples against the rank of the protein expression value. The highest fold change corresponds to rank 1 (left x-axis), while the lowest corresponds to the last rank (right x-axis). (C) Western blot analysis showed that the knockdown of ATIC reduced B7-H3, prion protein, RAC2, and NT5E protein expression in BFTC909 cells. (D) Quantification of the protein levels of ATIC, B7-H3, prion protein, RAC2, and NT5E from (C) (n=3). Results are shown as the mean±standard deviation (SD); *p<0.05 and **p<0.01 using two‐tailed t‐test for (D).

Journal: Cancer Genomics & Proteomics

Article Title: ATIC Knockdown Reduces B7-H3 Expression and Oncogenic Signaling in Upper Tract Urothelial Carcinoma Cells

doi: 10.21873/cgp.20575

Figure Lengend Snippet: Identification of downstream signaling pathways of ATIC using isobaric labeling with tandem mass tags and liquid chromatography tandem mass spectrometry proteomics analysis in BFTC909 cells transfected with negative control siRNA or ATIC siRNA. (A) In the volcano plot, scattered points represent the differential fold changes of various proteins. The x-axis shows the log2 fold change, while the y-axis displays the −log10-adjusted p-Values. Blue indicates a significant decrease, and red indicates a significant increase (p<0.05). (B) Differentially expressed protein (DEP) rank plot depicting the fold change between samples against the rank of the protein expression value. The highest fold change corresponds to rank 1 (left x-axis), while the lowest corresponds to the last rank (right x-axis). (C) Western blot analysis showed that the knockdown of ATIC reduced B7-H3, prion protein, RAC2, and NT5E protein expression in BFTC909 cells. (D) Quantification of the protein levels of ATIC, B7-H3, prion protein, RAC2, and NT5E from (C) (n=3). Results are shown as the mean±standard deviation (SD); *p<0.05 and **p<0.01 using two‐tailed t‐test for (D).

Article Snippet: Membranes were incubated overnight at 4°C with anti-ATIC (MA1-086, Invitrogen, Waltham, MA, USA), β-actin (#3700, Cell Signaling Technology, Danvers, MA, USA), α-tubulin (NB100-690, Novus Biologicals, Centennial, CO, USA), B7-H3 (#14058, Cell Signaling Technology), Prion Protein (A18058, ABclonalbio, New Taipei, Taiwan, ROC), RAC2 (A1139, ABclonalbio), NT5E (A25914, ABclonalbio), Fibronectin 1 (#26836, Cell Signaling Technology), Slug (NBP2-52570, Novus), Cyclin A2 (#4656, Cell Signaling Technology), Cyclin B1 (#4138, Cell Signaling Technology), p57 (NBP1-89917, Novus), phospho-mTOR (Ser2448) (SAB4504476, Sigma-Aldrich), mTOR (#2983, Cell Signaling Technology), phospho-AKT (Thr308) (#9275, Cell Signaling Technology), AKT (#9272, Cell Signaling Technology), phospho-p38 MAPK (Thr180/Tyr182) (#9211, Cell Signaling Technology), p38 MAPK (#9212, Cell Signaling Technology), phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (#9101, Cell Signaling Technology), and p44/42 MAPK (Erk1/2) (#9102, Cell Signaling Technology).

Techniques: Protein-Protein interactions, Labeling, Liquid Chromatography, Mass Spectrometry, Transfection, Negative Control, Expressing, Western Blot, Knockdown, Standard Deviation, Two Tailed Test

Functional characterization of ATIC downstream targets in BFTC909 cells. (A, B) Western blot validation of siRNA-mediated knockdown efficiency for B7-H3, prion protein, RAC2, and NT5E in BFTC909 cells (n=3). (C) Silencing of B7-H3, RAC2, or NT5E significantly reduced cell proliferation, as assessed using cell viability assays (n=4). (D, E) Knockdown of B7-H3, prion protein, RAC2, or NT5E markedly suppressed BFTC909 cell migration and invasion (n=3). (F) Knockdown of B7-H3 decreased fibronectin 1, slug, cyclin A2, and cyclin B1 expression while increasing p57 levels (n=3). (G) Silencing of prion protein reduced fibronectin 1 and cyclin A2 expression while upregulating p57 expression (n=3). (H) Suppression of RAC2 diminished fibronectin 1 and slug expression with a concomitant increase in p57 levels (n=3). (I) Depletion of NT5E decreased fibronectin 1 and elevated p57 expression levels (n=3). The results are shown as the mean±standard deviation (SD); *p<0.05, **p<0.01, and ***p<0.001; NS: Nonsignificant using two‐tailed t‐test for (B), (F), (G), (H) and (I), and ANOVA followed by Fisher’s LSD test for (C), (D) and (E).

Journal: Cancer Genomics & Proteomics

Article Title: ATIC Knockdown Reduces B7-H3 Expression and Oncogenic Signaling in Upper Tract Urothelial Carcinoma Cells

doi: 10.21873/cgp.20575

Figure Lengend Snippet: Functional characterization of ATIC downstream targets in BFTC909 cells. (A, B) Western blot validation of siRNA-mediated knockdown efficiency for B7-H3, prion protein, RAC2, and NT5E in BFTC909 cells (n=3). (C) Silencing of B7-H3, RAC2, or NT5E significantly reduced cell proliferation, as assessed using cell viability assays (n=4). (D, E) Knockdown of B7-H3, prion protein, RAC2, or NT5E markedly suppressed BFTC909 cell migration and invasion (n=3). (F) Knockdown of B7-H3 decreased fibronectin 1, slug, cyclin A2, and cyclin B1 expression while increasing p57 levels (n=3). (G) Silencing of prion protein reduced fibronectin 1 and cyclin A2 expression while upregulating p57 expression (n=3). (H) Suppression of RAC2 diminished fibronectin 1 and slug expression with a concomitant increase in p57 levels (n=3). (I) Depletion of NT5E decreased fibronectin 1 and elevated p57 expression levels (n=3). The results are shown as the mean±standard deviation (SD); *p<0.05, **p<0.01, and ***p<0.001; NS: Nonsignificant using two‐tailed t‐test for (B), (F), (G), (H) and (I), and ANOVA followed by Fisher’s LSD test for (C), (D) and (E).

Techniques: Functional Assay, Western Blot, Biomarker Discovery, Knockdown, Migration, Expressing, Standard Deviation, Two Tailed Test

Interactions among ATIC-associated downstream molecules in UTUC cells. (A) Western blot analysis showed that the knockdown of B7-H3 markedly reduced prion protein and RAC2 protein expression in BFTC909 cells (n=3). (B) Silencing of prion protein decreased RAC2 protein expression in BFTC909 cells (n=3). (C) Knockdown of RAC2 did not significantly alter NT5E protein levels in BFTC909 cells (n=3). The results are shown as the mean±standard deviation (SD); **p<0.01, ***p<0.001, NS: Nonsignificant, using two-tailed t-test.

Journal: Cancer Genomics & Proteomics

Article Title: ATIC Knockdown Reduces B7-H3 Expression and Oncogenic Signaling in Upper Tract Urothelial Carcinoma Cells

doi: 10.21873/cgp.20575

Figure Lengend Snippet: Interactions among ATIC-associated downstream molecules in UTUC cells. (A) Western blot analysis showed that the knockdown of B7-H3 markedly reduced prion protein and RAC2 protein expression in BFTC909 cells (n=3). (B) Silencing of prion protein decreased RAC2 protein expression in BFTC909 cells (n=3). (C) Knockdown of RAC2 did not significantly alter NT5E protein levels in BFTC909 cells (n=3). The results are shown as the mean±standard deviation (SD); **p<0.01, ***p<0.001, NS: Nonsignificant, using two-tailed t-test.

Techniques: Western Blot, Knockdown, Expressing, Standard Deviation, Two Tailed Test

The ATIC/B7-H3 axis modulates mTOR, AKT, ERK, and p38 signaling in BFTC909 cells. (A) Western blot analysis showing that ATIC knockdown reduces the phosphorylation of mTOR, AKT, ERK, and p38, and decreases total mTOR expression in BFTC909 cells (n=3). (B) Silencing of B7-H3 reduced total and phosphorylated mTOR levels, and decreased the phosphorylation of AKT, ERK, and p38 (n=3). (C) Prion protein knockdown decreased total and phosphorylated mTOR levels, and reduced the activation of AKT, ERK, and p38 (n=3). (D) RAC2 silencing primarily reduced total and phosphorylated mTOR expression. (E) NT5E knockdown had no significant effect on mTOR, AKT, ERK, or p38 activity (n=3). The results are shown as the mean±standard deviation (SD); *p<0.05, **p<0.01, ***p<0.001, NS: Nonsignificant, using two-tailed t-test.

Journal: Cancer Genomics & Proteomics

Article Title: ATIC Knockdown Reduces B7-H3 Expression and Oncogenic Signaling in Upper Tract Urothelial Carcinoma Cells

doi: 10.21873/cgp.20575

Figure Lengend Snippet: The ATIC/B7-H3 axis modulates mTOR, AKT, ERK, and p38 signaling in BFTC909 cells. (A) Western blot analysis showing that ATIC knockdown reduces the phosphorylation of mTOR, AKT, ERK, and p38, and decreases total mTOR expression in BFTC909 cells (n=3). (B) Silencing of B7-H3 reduced total and phosphorylated mTOR levels, and decreased the phosphorylation of AKT, ERK, and p38 (n=3). (C) Prion protein knockdown decreased total and phosphorylated mTOR levels, and reduced the activation of AKT, ERK, and p38 (n=3). (D) RAC2 silencing primarily reduced total and phosphorylated mTOR expression. (E) NT5E knockdown had no significant effect on mTOR, AKT, ERK, or p38 activity (n=3). The results are shown as the mean±standard deviation (SD); *p<0.05, **p<0.01, ***p<0.001, NS: Nonsignificant, using two-tailed t-test.

Techniques: Western Blot, Knockdown, Phospho-proteomics, Expressing, Activation Assay, Activity Assay, Standard Deviation, Two Tailed Test

The ATIC/B7-H3 axis regulates cisplatin sensitivity in BFTC909 cells. (A) Western blot analysis showing the protein expression of ATIC, B7-H3, prion protein, RAC2, and NT5E in BFTC909 cells after 48 h of treatment with cisplatin (0–20 μM). (B) Cell viability assays showing that the knockdown of ATIC, B7-H3, prion protein, RAC2, or NT5E significantly enhanced cisplatin-induced cytotoxicity in BFTC909 cells after 48 h of treatment (n=3). The results are shown as the mean±standard deviation (SD); **p<0.01 (vs. si-Control non-treatment); #p<0.05 (vs. si-Control CDDP 20 μM); ##p<0.01 (vs. si-Control CDDP 20 μM) using ANOVA followed by Fisher’s LSD test.

Journal: Cancer Genomics & Proteomics

Article Title: ATIC Knockdown Reduces B7-H3 Expression and Oncogenic Signaling in Upper Tract Urothelial Carcinoma Cells

doi: 10.21873/cgp.20575

Figure Lengend Snippet: The ATIC/B7-H3 axis regulates cisplatin sensitivity in BFTC909 cells. (A) Western blot analysis showing the protein expression of ATIC, B7-H3, prion protein, RAC2, and NT5E in BFTC909 cells after 48 h of treatment with cisplatin (0–20 μM). (B) Cell viability assays showing that the knockdown of ATIC, B7-H3, prion protein, RAC2, or NT5E significantly enhanced cisplatin-induced cytotoxicity in BFTC909 cells after 48 h of treatment (n=3). The results are shown as the mean±standard deviation (SD); **p<0.01 (vs. si-Control non-treatment); #p<0.05 (vs. si-Control CDDP 20 μM); ##p<0.01 (vs. si-Control CDDP 20 μM) using ANOVA followed by Fisher’s LSD test.

Techniques: Western Blot, Expressing, Knockdown, Standard Deviation, Control

The staining intensity within the germinal center decreased as the concentrations of B7-H3 protein increased. The concentration of the B7-H3(36H7) antibody is 1.0 μg/mL. All of the slides Staining by BOND III. (a) No B7-H3 protein added, (b) The concentration of B7-H3 protein is 0.05 μg/mL, (c) 0.1 μg/mL, (d) 0.5 μg/mL. When the concentration is increased to (d) 0.5 μg/mL, the antibody binding site is occupied by the B7-H3 protein, which loses the ability to detect the sample. The results confirming the binding specificity of the antibody B7-H3(36H7). scale bar 50 μm. Original magnification, ×400.

Journal: Frontiers in Pharmacology

Article Title: Development and characterization of a novel B7-H3 rabbit monoclonal antibody for glioma diagnosis

doi: 10.3389/fphar.2026.1736583

Figure Lengend Snippet: The staining intensity within the germinal center decreased as the concentrations of B7-H3 protein increased. The concentration of the B7-H3(36H7) antibody is 1.0 μg/mL. All of the slides Staining by BOND III. (a) No B7-H3 protein added, (b) The concentration of B7-H3 protein is 0.05 μg/mL, (c) 0.1 μg/mL, (d) 0.5 μg/mL. When the concentration is increased to (d) 0.5 μg/mL, the antibody binding site is occupied by the B7-H3 protein, which loses the ability to detect the sample. The results confirming the binding specificity of the antibody B7-H3(36H7). scale bar 50 μm. Original magnification, ×400.

Article Snippet: For immunohistochemistry (IHC) analysis, we selected B7-H3 Rabbit Monoclonal Antibody (D9M2L, CST: 14058) and anti-CD276 antibody (SP206, Abcam: ab227670) as benchmarks, both of which are well-established clones suitable for IHC applications and are frequently cited in the literature.

Techniques: Staining, Concentration Assay, Binding Assay

The affinity constant of the B7-H3 peptide binding to the B7-H3(36H7) antibody was measured to be 2.10 × 10 −9 mol/L. B7-H3(36H7) antibody has a high affinity for antigens.

Journal: Frontiers in Pharmacology

Article Title: Development and characterization of a novel B7-H3 rabbit monoclonal antibody for glioma diagnosis

doi: 10.3389/fphar.2026.1736583

Figure Lengend Snippet: The affinity constant of the B7-H3 peptide binding to the B7-H3(36H7) antibody was measured to be 2.10 × 10 −9 mol/L. B7-H3(36H7) antibody has a high affinity for antigens.

Techniques: Binding Assay

The B7-H3 (36H7) antibody consistently exhibits specific recognition of the B7-H3 antigen across multiple assay platforms. (a) Western blot (WB) result of B7-H3 antibody. lane 1 and 2: B7-H3 protein (B73-H52E2 29–245); lane 3 and 4: Lysates of U251 cells; lane 5 and 6: Lysates of Jurkat cells. The 36H7 antibody clone demonstrated specific immunoreactivity with U251 positive control cells, while showing no detectable cross-reactivity with negative cellular components. (b) The results of ELISA showed that the B7-H3(36H7) antibody had high sensitivity, and the concentration for 50% of maximal effect (EC50) was 2.474 ng/mL. (c) The B7-H3(36H7) antibody does not bind to other proteins within the same family (B7-H1, B7-H2, B7-H4), only binding to B7-H3 protein. (d) Fluorescence detection in glioma paraffin-embedded sections using the B7-H3 (36H7) antibody paired with HRP-conjugated goat anti-rabbit secondary antibody (G2-1234) and TSA570 dye. Clear membrane staining is observed. (e) Immunofluorescence detection in tonsil paraffin-embedded sections using the B7-H3 (36H7) antibody paired with Alexa Fluor 647-conjugated goat anti-rabbit secondary antibody, showing specific recognition in the germinal centers.

Journal: Frontiers in Pharmacology

Article Title: Development and characterization of a novel B7-H3 rabbit monoclonal antibody for glioma diagnosis

doi: 10.3389/fphar.2026.1736583

Figure Lengend Snippet: The B7-H3 (36H7) antibody consistently exhibits specific recognition of the B7-H3 antigen across multiple assay platforms. (a) Western blot (WB) result of B7-H3 antibody. lane 1 and 2: B7-H3 protein (B73-H52E2 29–245); lane 3 and 4: Lysates of U251 cells; lane 5 and 6: Lysates of Jurkat cells. The 36H7 antibody clone demonstrated specific immunoreactivity with U251 positive control cells, while showing no detectable cross-reactivity with negative cellular components. (b) The results of ELISA showed that the B7-H3(36H7) antibody had high sensitivity, and the concentration for 50% of maximal effect (EC50) was 2.474 ng/mL. (c) The B7-H3(36H7) antibody does not bind to other proteins within the same family (B7-H1, B7-H2, B7-H4), only binding to B7-H3 protein. (d) Fluorescence detection in glioma paraffin-embedded sections using the B7-H3 (36H7) antibody paired with HRP-conjugated goat anti-rabbit secondary antibody (G2-1234) and TSA570 dye. Clear membrane staining is observed. (e) Immunofluorescence detection in tonsil paraffin-embedded sections using the B7-H3 (36H7) antibody paired with Alexa Fluor 647-conjugated goat anti-rabbit secondary antibody, showing specific recognition in the germinal centers.

Techniques: Western Blot, Positive Control, Enzyme-linked Immunosorbent Assay, Concentration Assay, Binding Assay, Fluorescence, Membrane, Staining, Immunofluorescence

The germinal center and crypt epithelium exhibited positivity for B7-H3 expression, the interfollicular regions were negative.

Journal: Frontiers in Pharmacology

Article Title: Development and characterization of a novel B7-H3 rabbit monoclonal antibody for glioma diagnosis

doi: 10.3389/fphar.2026.1736583

Figure Lengend Snippet: The germinal center and crypt epithelium exhibited positivity for B7-H3 expression, the interfollicular regions were negative.

Techniques: Expressing

Different IHC staining patterns of B7-H3(36H7) antibody on glioma sections. The antibody demonstrated high sensitivity, enabling robust discrimination between samples with differential target expression levels. (a) Normal brain, no background color. (b) Negative. (c) and (g) Strongly positive cell membrane staining. (d) Moderately positive cytoplasmic and cell membrane staining. (e) and (f) Weakly positive cytoplasmic staining. (h) Strong positive cytoplasmic and cell membrane staining. Scale bar 50 μm. Original magnification, ×400.

Journal: Frontiers in Pharmacology

Article Title: Development and characterization of a novel B7-H3 rabbit monoclonal antibody for glioma diagnosis

doi: 10.3389/fphar.2026.1736583

Figure Lengend Snippet: Different IHC staining patterns of B7-H3(36H7) antibody on glioma sections. The antibody demonstrated high sensitivity, enabling robust discrimination between samples with differential target expression levels. (a) Normal brain, no background color. (b) Negative. (c) and (g) Strongly positive cell membrane staining. (d) Moderately positive cytoplasmic and cell membrane staining. (e) and (f) Weakly positive cytoplasmic staining. (h) Strong positive cytoplasmic and cell membrane staining. Scale bar 50 μm. Original magnification, ×400.

Techniques: Immunohistochemistry, Expressing, Membrane, Staining

The B7-H3 protein exhibits differential expression levels in the vasculature of gliomas. (a) Vessel positive, surrounding tissue negative. (b,c) Both vessels and surrounding tissue are positive. (d) Vessels are negative while surrounding tissues are positive. Corresponding HE at right corner of each image. Scale bar 50 μm. Original magnification, ×400. (e) Among the 200 samples with positive B7-H3 protein detection, 93.5% of the tumor blood vessels and 1.5% of the non-tumor blood vessels were observed. Additionally, the blood vessels in 5% of the samples were difficult to identify or had poor tissue morphology. Among the tumor blood vessels, the proportions of different intensities of B7-H3 protein expression were as follows: 6% were negative, 22% were weakly positive, 6% were from weakly positive to moderately positive, 23% were moderately positive, 7% were from moderately positive to strongly positive, and 36% were strongly positive.

Journal: Frontiers in Pharmacology

Article Title: Development and characterization of a novel B7-H3 rabbit monoclonal antibody for glioma diagnosis

doi: 10.3389/fphar.2026.1736583

Figure Lengend Snippet: The B7-H3 protein exhibits differential expression levels in the vasculature of gliomas. (a) Vessel positive, surrounding tissue negative. (b,c) Both vessels and surrounding tissue are positive. (d) Vessels are negative while surrounding tissues are positive. Corresponding HE at right corner of each image. Scale bar 50 μm. Original magnification, ×400. (e) Among the 200 samples with positive B7-H3 protein detection, 93.5% of the tumor blood vessels and 1.5% of the non-tumor blood vessels were observed. Additionally, the blood vessels in 5% of the samples were difficult to identify or had poor tissue morphology. Among the tumor blood vessels, the proportions of different intensities of B7-H3 protein expression were as follows: 6% were negative, 22% were weakly positive, 6% were from weakly positive to moderately positive, 23% were moderately positive, 7% were from moderately positive to strongly positive, and 36% were strongly positive.

Techniques: Quantitative Proteomics, Expressing

(A) Immunohistochemistry (IHC) staining for B7-H3 on FFPE primary tumor tissue, and (B) semi-quantitative scoring of B7-H3 expression. 20X magnification, n=8. (C) AT/RT cell line B7-H3 expression. Isotype-stained samples are shown in the histograms directly below each B7-H3-stained sample. (D) B7-H3 surface molecules per cell quantified by molecules of equivalent soluble fluorochrome (MESF) flow cytometry assay. Each dot representative of technical replicates. (E) Total B7-H3 protein expression with or without deglycosylation assessed by western blot.

Journal: bioRxiv

Article Title: B7-H3-targeted natural killer cells effectively kill atypical teratoid / rhabdoid tumors and extend survival in orthotopic xenografts

doi: 10.64898/2026.01.15.699746

Figure Lengend Snippet: (A) Immunohistochemistry (IHC) staining for B7-H3 on FFPE primary tumor tissue, and (B) semi-quantitative scoring of B7-H3 expression. 20X magnification, n=8. (C) AT/RT cell line B7-H3 expression. Isotype-stained samples are shown in the histograms directly below each B7-H3-stained sample. (D) B7-H3 surface molecules per cell quantified by molecules of equivalent soluble fluorochrome (MESF) flow cytometry assay. Each dot representative of technical replicates. (E) Total B7-H3 protein expression with or without deglycosylation assessed by western blot.

Article Snippet: Briefly, 4 μm sections were stained with an anti-human B7-H3 primary antibody (clone D9M2L, Cell Signaling Technology 14058) on the Ventana Benchmark immunostaining system (Roche Diagnostics).

Techniques: Immunohistochemistry, Expressing, Staining, Flow Cytometry, Western Blot

(A) CARs consisting of Hu8H9 scFv and various affinity mutants, 2B4 (CD244) hinge (H), transmembrane (TM), and intracellular domains (IC), and CD3ζ signaling domain. (B) Representative primary NK-cell CAR expression. (C) CAR expression (n=4 healthy donors, 4-9 separate experiments). (D) Fold expansion of CAR-NK cells starting at day of transduction (n=4 healthy donors). (E) Representative CAR transduced NK-cell B7-H3 expression 2-4 days post-transduction. (F) B7-H3 expression on CAR-NK cells. (n = 3 healthy donors). *** = p<0.001 UTD vs. all others. (G) Representative measurement of CAR-NK cell degranulation post 2-hour co-culture with CHLA-06 AT/RT cells detected by CD107a staining.

Journal: bioRxiv

Article Title: B7-H3-targeted natural killer cells effectively kill atypical teratoid / rhabdoid tumors and extend survival in orthotopic xenografts

doi: 10.64898/2026.01.15.699746

Figure Lengend Snippet: (A) CARs consisting of Hu8H9 scFv and various affinity mutants, 2B4 (CD244) hinge (H), transmembrane (TM), and intracellular domains (IC), and CD3ζ signaling domain. (B) Representative primary NK-cell CAR expression. (C) CAR expression (n=4 healthy donors, 4-9 separate experiments). (D) Fold expansion of CAR-NK cells starting at day of transduction (n=4 healthy donors). (E) Representative CAR transduced NK-cell B7-H3 expression 2-4 days post-transduction. (F) B7-H3 expression on CAR-NK cells. (n = 3 healthy donors). *** = p<0.001 UTD vs. all others. (G) Representative measurement of CAR-NK cell degranulation post 2-hour co-culture with CHLA-06 AT/RT cells detected by CD107a staining.

Techniques: Expressing, Transduction, Co-Culture Assay, Staining

(A) CHLA-06.ffLuc (25k cells) were injected into caudate putamen of NSG mice at day 0. Randomization/cohorting was performed at day 2, and intratumoral NK cell treatment (3 million cells per treatment) was started on day 3 and repeated on days 10 and 17. (B) Tumor radiance measured by IVIS Spectrum bioluminescent imaging and analyzed using Living Image software. (C) tumor radiance over time of CHLA-06.ffLuc bearing mice (n=8-9 per condition). (D) Kaplan-Meier survival curve. ***= p<0.001. (E) Brain tissue harvested at endpoint (D23 post-tumor, D6 post-third NK-cell treatment for both samples), representative slides from UTD NK treated and CAR-NK treated mice stained for human B7-H3 and CD45. 40X magnification.

Journal: bioRxiv

Article Title: B7-H3-targeted natural killer cells effectively kill atypical teratoid / rhabdoid tumors and extend survival in orthotopic xenografts

doi: 10.64898/2026.01.15.699746

Figure Lengend Snippet: (A) CHLA-06.ffLuc (25k cells) were injected into caudate putamen of NSG mice at day 0. Randomization/cohorting was performed at day 2, and intratumoral NK cell treatment (3 million cells per treatment) was started on day 3 and repeated on days 10 and 17. (B) Tumor radiance measured by IVIS Spectrum bioluminescent imaging and analyzed using Living Image software. (C) tumor radiance over time of CHLA-06.ffLuc bearing mice (n=8-9 per condition). (D) Kaplan-Meier survival curve. ***= p<0.001. (E) Brain tissue harvested at endpoint (D23 post-tumor, D6 post-third NK-cell treatment for both samples), representative slides from UTD NK treated and CAR-NK treated mice stained for human B7-H3 and CD45. 40X magnification.

Techniques: Injection, Imaging, Software, Staining

(A) BT12.ffLuc (100k cells) were injected into the right lateral ventricle of NSG mice at day 0. Randomization/cohorting was performed at day 2, and ICV NK cell treatment was started on day 3 and repeated on days 10 and 17. (B) Kaplan-Meier survival curve, and (C) percent weight change over time of ICV BT12.ffLuc bearing mice. Each dotted line represents an individual animal. Representative histology of endpoint brain and spinal tissue from (D) UTD NK treated, and (E) CAR-NK treated mice with corresponding human B7-H3 and CD45 IHC stains. Animal endpoints = 31, 62 days post-tumor injection, respectively. 200X magnification. (F) Quantification of tumor associated human NK cells. n = 5-7 per condition.

Journal: bioRxiv

Article Title: B7-H3-targeted natural killer cells effectively kill atypical teratoid / rhabdoid tumors and extend survival in orthotopic xenografts

doi: 10.64898/2026.01.15.699746

Figure Lengend Snippet: (A) BT12.ffLuc (100k cells) were injected into the right lateral ventricle of NSG mice at day 0. Randomization/cohorting was performed at day 2, and ICV NK cell treatment was started on day 3 and repeated on days 10 and 17. (B) Kaplan-Meier survival curve, and (C) percent weight change over time of ICV BT12.ffLuc bearing mice. Each dotted line represents an individual animal. Representative histology of endpoint brain and spinal tissue from (D) UTD NK treated, and (E) CAR-NK treated mice with corresponding human B7-H3 and CD45 IHC stains. Animal endpoints = 31, 62 days post-tumor injection, respectively. 200X magnification. (F) Quantification of tumor associated human NK cells. n = 5-7 per condition.

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