50010-M08H Search Results


mouse pd l1  (Sino Biological)
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Mechanism of PBAP‐gE Complex Combined with LZ901 Vaccine in Enhancing NK Cell‐Mediated Antitumor Efficacy. The PBAP‐gE complex specifically binds <t>to</t> <t>PD‐L1</t> on PD‐L1‐positive tumor cells via its sPD‐L1 domain, thereby labeling these cells with the gE antigen. Subsequently, the LZ901 vaccine activates the immune system to produce gE—specific antibodies (anti‐gE antibodies), which exert their effects through two distinct pathways. First, these antibodies directly bind to the FcγRIIIa receptors on NK cells, providing activation signals. Second, they specifically bind to the PBAP‐gE complex already present on tumor cells. Together, these dual actions trigger NK cell‐mediated ADCC, significantly augmenting NK cells’ ability to target and destroy PD‐L1‐positive tumor cells. Created with BioRender.com.
Mouse Pd L1, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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china mouse pd l1 his protein 50010 m08h b sino biological  (Sino Biological)
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Sino Biological china mouse pd l1 his protein 50010 m08h b sino biological
Mechanism of PBAP‐gE Complex Combined with LZ901 Vaccine in Enhancing NK Cell‐Mediated Antitumor Efficacy. The PBAP‐gE complex specifically binds <t>to</t> <t>PD‐L1</t> on PD‐L1‐positive tumor cells via its sPD‐L1 domain, thereby labeling these cells with the gE antigen. Subsequently, the LZ901 vaccine activates the immune system to produce gE—specific antibodies (anti‐gE antibodies), which exert their effects through two distinct pathways. First, these antibodies directly bind to the FcγRIIIa receptors on NK cells, providing activation signals. Second, they specifically bind to the PBAP‐gE complex already present on tumor cells. Together, these dual actions trigger NK cell‐mediated ADCC, significantly augmenting NK cells’ ability to target and destroy PD‐L1‐positive tumor cells. Created with BioRender.com.
China Mouse Pd L1 His Protein 50010 M08h B Sino Biological, supplied by Sino Biological, 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/product/50010-M08H/pmc10935467__mmc1-38-23-28?v=Sino+Biological
Average 91 stars, based on 1 article reviews
china mouse pd l1 his protein 50010 m08h b sino biological - by Bioz Stars, 2026-08
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Mechanism of PBAP‐gE Complex Combined with LZ901 Vaccine in Enhancing NK Cell‐Mediated Antitumor Efficacy. The PBAP‐gE complex specifically binds to PD‐L1 on PD‐L1‐positive tumor cells via its sPD‐L1 domain, thereby labeling these cells with the gE antigen. Subsequently, the LZ901 vaccine activates the immune system to produce gE—specific antibodies (anti‐gE antibodies), which exert their effects through two distinct pathways. First, these antibodies directly bind to the FcγRIIIa receptors on NK cells, providing activation signals. Second, they specifically bind to the PBAP‐gE complex already present on tumor cells. Together, these dual actions trigger NK cell‐mediated ADCC, significantly augmenting NK cells’ ability to target and destroy PD‐L1‐positive tumor cells. Created with BioRender.com.

Journal: Advanced Science

Article Title: PD‐L1‐Binding Antigen Presenters: Redirecting Vaccine‐Induced Antibodies for Cancer Immunotherapy

doi: 10.1002/advs.202519574

Figure Lengend Snippet: Mechanism of PBAP‐gE Complex Combined with LZ901 Vaccine in Enhancing NK Cell‐Mediated Antitumor Efficacy. The PBAP‐gE complex specifically binds to PD‐L1 on PD‐L1‐positive tumor cells via its sPD‐L1 domain, thereby labeling these cells with the gE antigen. Subsequently, the LZ901 vaccine activates the immune system to produce gE—specific antibodies (anti‐gE antibodies), which exert their effects through two distinct pathways. First, these antibodies directly bind to the FcγRIIIa receptors on NK cells, providing activation signals. Second, they specifically bind to the PBAP‐gE complex already present on tumor cells. Together, these dual actions trigger NK cell‐mediated ADCC, significantly augmenting NK cells’ ability to target and destroy PD‐L1‐positive tumor cells. Created with BioRender.com.

Article Snippet: For the ELISA blocking activity detection of PBAP‐gE, the same procedure was followed with the following modifications: human PD‐L1 (ECD, His Tag, SinoBiological, 10084‐H08H) protein was replaced with mouse PD‐L1 (ECD, His Tag, SinoBiological, 50010‐M08H), PBAP‐HER2 (1 μg/well and 10 μg/well) was replaced with PBAP‐gE (1 μg/well and 10 μg/well), PD‐L1 monoclonal antibody (SinoBiological, 10084‐MM33) was replaced with PD‐L1 monoclonal antibody (SinoBiological, B50010 ‐R678), and Goat anti‐Mouse IgG, HRP secondary antibody (SinoBiological, SSA007) was replaced with Goat anti‐Rabbit IgG, HRP secondary antibody (SinoBiological, SSA004).

Techniques: Labeling, Activation Assay

Serum from Herpes Zoster Vaccine (LZ901)‐immunized Mice Enhances PBAP‐Mediated ADCC Against PD‐L1 + Tumor Cells In Vitro. (A) Schematic diagram of the sPD‐1‐gE and PBAP‐gE fusion protein. The sPD‐1‐gE construct consists of sPD‐1 fused to gE. The PBAP‐gE construct comprises sPD‐1‐gE fused with an Fc domain (sPD‐1‐gE‐Fc). (B) Structural modeling of PBAP‐gE with AlphaFold 3. (C) Pharmacokinetic profiles of sPD‐1‐gE and PBAP‐gE following intravenous injection into C57BL/6J mice (n=3 mice/group, 100 µg/mice). Data are presented as the mean ± SD (n = 3). (D) The binding inhibition of PBAP‐gE on PD‐L1/PD‐1 interaction was assessed by ELISA. The absorbance was measured at 450 nm to determine the blocking effect. (E) The fluorescence intensity of the antibody‐cell binding was analyzed using a flow cytometry to assess the blocking effect on the PD‐1/PD‐L1 pathway. Data are presented as the mean ± SD (n = 3). (F) In vitro cytotoxicity assay. KIL C.2 cells were co‐incubated with PBAP‐gE and serum from LZ901‐immunized mice, against 4T1‐IFNγ (IFN‐γ‐induced, PD‐L1 + ) tumor cells and 4T1‐WT cells. KIL C.2 cells, KIL C.2 cells co‐incubated with gE and serum from LZ901‐immunized mice, KIL C.2 cells co‐incubated with PBAP‐gE and serum from saline vaccine‐immunized mice and all groups treated with anti‐FcγRIII blocking antibody were used as controls. Data are presented as mean ± SD of 3 independent experiments, each performed in triplicate. (G) Flow cytometry analysis of perforin, granzyme B, IFN‐γ and CD107a in KIL C.2 cells. Representative of 3 independent experiments.

Journal: Advanced Science

Article Title: PD‐L1‐Binding Antigen Presenters: Redirecting Vaccine‐Induced Antibodies for Cancer Immunotherapy

doi: 10.1002/advs.202519574

Figure Lengend Snippet: Serum from Herpes Zoster Vaccine (LZ901)‐immunized Mice Enhances PBAP‐Mediated ADCC Against PD‐L1 + Tumor Cells In Vitro. (A) Schematic diagram of the sPD‐1‐gE and PBAP‐gE fusion protein. The sPD‐1‐gE construct consists of sPD‐1 fused to gE. The PBAP‐gE construct comprises sPD‐1‐gE fused with an Fc domain (sPD‐1‐gE‐Fc). (B) Structural modeling of PBAP‐gE with AlphaFold 3. (C) Pharmacokinetic profiles of sPD‐1‐gE and PBAP‐gE following intravenous injection into C57BL/6J mice (n=3 mice/group, 100 µg/mice). Data are presented as the mean ± SD (n = 3). (D) The binding inhibition of PBAP‐gE on PD‐L1/PD‐1 interaction was assessed by ELISA. The absorbance was measured at 450 nm to determine the blocking effect. (E) The fluorescence intensity of the antibody‐cell binding was analyzed using a flow cytometry to assess the blocking effect on the PD‐1/PD‐L1 pathway. Data are presented as the mean ± SD (n = 3). (F) In vitro cytotoxicity assay. KIL C.2 cells were co‐incubated with PBAP‐gE and serum from LZ901‐immunized mice, against 4T1‐IFNγ (IFN‐γ‐induced, PD‐L1 + ) tumor cells and 4T1‐WT cells. KIL C.2 cells, KIL C.2 cells co‐incubated with gE and serum from LZ901‐immunized mice, KIL C.2 cells co‐incubated with PBAP‐gE and serum from saline vaccine‐immunized mice and all groups treated with anti‐FcγRIII blocking antibody were used as controls. Data are presented as mean ± SD of 3 independent experiments, each performed in triplicate. (G) Flow cytometry analysis of perforin, granzyme B, IFN‐γ and CD107a in KIL C.2 cells. Representative of 3 independent experiments.

Article Snippet: For the ELISA blocking activity detection of PBAP‐gE, the same procedure was followed with the following modifications: human PD‐L1 (ECD, His Tag, SinoBiological, 10084‐H08H) protein was replaced with mouse PD‐L1 (ECD, His Tag, SinoBiological, 50010‐M08H), PBAP‐HER2 (1 μg/well and 10 μg/well) was replaced with PBAP‐gE (1 μg/well and 10 μg/well), PD‐L1 monoclonal antibody (SinoBiological, 10084‐MM33) was replaced with PD‐L1 monoclonal antibody (SinoBiological, B50010 ‐R678), and Goat anti‐Mouse IgG, HRP secondary antibody (SinoBiological, SSA007) was replaced with Goat anti‐Rabbit IgG, HRP secondary antibody (SinoBiological, SSA004).

Techniques: In Vitro, Construct, Injection, Binding Assay, Inhibition, Enzyme-linked Immunosorbent Assay, Blocking Assay, Fluorescence, Flow Cytometry, Cytotoxicity Assay, Incubation, Saline

Trop2‐CAR‐T Cells Coexpressing PBAP‐gE or Combined with Intratumoral Injection of PBAP‐gE Induces Tumor Regression in LZ901‐Vaccinated Mice. (A) Schematic of CAR constructs. The control CAR fuses scFv VH/VL domains to the CD28 transmembrane (TM) and CD3ζ signaling domains. The experimental CAR adds a C‐terminal PBAP‐gE module under NFAT promoter control for tumor‐inducible expression. (B) Schematic of the CAR‐T‐PBAP system. Upon tumor antigen recognition by the CAR ectodomain, NFAT‐driven expression and secretion of PBAP‐gE recruits vaccine‐elicited or virus‐induced antibodies to FcγRIIIa + NK cells, bridging them to PD‐L1 + tumor cells to trigger ADCC‐mediated lysis. Created with BioRender.com. (C) Experimental Design. C57BL/6J mice (n = 8 mice/group) received LZ901 vaccine (5 µg/dose) on days 0 and 21; Serum was collected on day 27 for anti‐gE IgG detection. B16‐Trop2 cells (5 × 10 5 ) were subcutaneously implanted On day 28. When tumors reached ∼100 mm 3 (day 35), mice were treated with a single infusion of CAR‐T cells (± PBAP‐gE) via intravenous ( i.v .), intraperitoneal ( i.p .), or intratumoral ( i.t .) injection. Endpoint serum samples were collected on day 42 for anti‐gE IgG analysis. Created with BioRender.com. (D) Tumor volumes were measured every 1‐2 days from day 35 to day 41 in all groups, and all mice were euthanized on day 41. Tumor growth curves were plotted for the five experimental groups: CD19‐CAR, Trop2‐CAR, Trop2‐CAR‐PBAP, Trop2‐CAR + PBAP ( i . v .), Trop2‐CAR + PBAP ( i . p .), Trop2‐CAR + PBAP ( i . t .). (E) Representative tumor images are shown in the left panel, and tumor volumes at the experimental endpoint are presented in the right panel. The PBAP‐coexpressing CAR‐T cell group exhibited tumor regression that was not statistically different from that in the intratumoral injection group. Data are presented as the mean ± SD, (n = 6–8). Statistical significance was determined using one‐way ANOVA. ns indicates not significant (p > 0.05). (F) Flow cytometric analysis of tumor‐infiltrating immune cells revealed that both the Trop2‐CAR‐PBAP and Trop2‐CAR + PBAP ( i . t .) groups exhibited significantly elevated frequencies of B cells and NK cells. Data are presented as the mean ± SD, (n = 8). Statistical significance was determined using one‐way ANOVA. ns indicates not significant (p > 0.05). (G) ELISA was used to analyze the binding affinity of serum (collected on days 27 and 42) from LZ901‐vaccinated mice to gE in both the Trop2‐CAR‐PBAP and Trop2‐CAR + PBAP treatment groups. Data are presented as the mean ± SD (n = 8). (H) Correlation analysis was performed to examine the relationship between tumor volume and gE‐specific IgG antibody levels (endpoint titer) at days 27 and 42 in the Trop2‐CAR‐PBAP and Trop2‐CAR + PBAP‐gE ( i . t .) treatment groups.

Journal: Advanced Science

Article Title: PD‐L1‐Binding Antigen Presenters: Redirecting Vaccine‐Induced Antibodies for Cancer Immunotherapy

doi: 10.1002/advs.202519574

Figure Lengend Snippet: Trop2‐CAR‐T Cells Coexpressing PBAP‐gE or Combined with Intratumoral Injection of PBAP‐gE Induces Tumor Regression in LZ901‐Vaccinated Mice. (A) Schematic of CAR constructs. The control CAR fuses scFv VH/VL domains to the CD28 transmembrane (TM) and CD3ζ signaling domains. The experimental CAR adds a C‐terminal PBAP‐gE module under NFAT promoter control for tumor‐inducible expression. (B) Schematic of the CAR‐T‐PBAP system. Upon tumor antigen recognition by the CAR ectodomain, NFAT‐driven expression and secretion of PBAP‐gE recruits vaccine‐elicited or virus‐induced antibodies to FcγRIIIa + NK cells, bridging them to PD‐L1 + tumor cells to trigger ADCC‐mediated lysis. Created with BioRender.com. (C) Experimental Design. C57BL/6J mice (n = 8 mice/group) received LZ901 vaccine (5 µg/dose) on days 0 and 21; Serum was collected on day 27 for anti‐gE IgG detection. B16‐Trop2 cells (5 × 10 5 ) were subcutaneously implanted On day 28. When tumors reached ∼100 mm 3 (day 35), mice were treated with a single infusion of CAR‐T cells (± PBAP‐gE) via intravenous ( i.v .), intraperitoneal ( i.p .), or intratumoral ( i.t .) injection. Endpoint serum samples were collected on day 42 for anti‐gE IgG analysis. Created with BioRender.com. (D) Tumor volumes were measured every 1‐2 days from day 35 to day 41 in all groups, and all mice were euthanized on day 41. Tumor growth curves were plotted for the five experimental groups: CD19‐CAR, Trop2‐CAR, Trop2‐CAR‐PBAP, Trop2‐CAR + PBAP ( i . v .), Trop2‐CAR + PBAP ( i . p .), Trop2‐CAR + PBAP ( i . t .). (E) Representative tumor images are shown in the left panel, and tumor volumes at the experimental endpoint are presented in the right panel. The PBAP‐coexpressing CAR‐T cell group exhibited tumor regression that was not statistically different from that in the intratumoral injection group. Data are presented as the mean ± SD, (n = 6–8). Statistical significance was determined using one‐way ANOVA. ns indicates not significant (p > 0.05). (F) Flow cytometric analysis of tumor‐infiltrating immune cells revealed that both the Trop2‐CAR‐PBAP and Trop2‐CAR + PBAP ( i . t .) groups exhibited significantly elevated frequencies of B cells and NK cells. Data are presented as the mean ± SD, (n = 8). Statistical significance was determined using one‐way ANOVA. ns indicates not significant (p > 0.05). (G) ELISA was used to analyze the binding affinity of serum (collected on days 27 and 42) from LZ901‐vaccinated mice to gE in both the Trop2‐CAR‐PBAP and Trop2‐CAR + PBAP treatment groups. Data are presented as the mean ± SD (n = 8). (H) Correlation analysis was performed to examine the relationship between tumor volume and gE‐specific IgG antibody levels (endpoint titer) at days 27 and 42 in the Trop2‐CAR‐PBAP and Trop2‐CAR + PBAP‐gE ( i . t .) treatment groups.

Article Snippet: For the ELISA blocking activity detection of PBAP‐gE, the same procedure was followed with the following modifications: human PD‐L1 (ECD, His Tag, SinoBiological, 10084‐H08H) protein was replaced with mouse PD‐L1 (ECD, His Tag, SinoBiological, 50010‐M08H), PBAP‐HER2 (1 μg/well and 10 μg/well) was replaced with PBAP‐gE (1 μg/well and 10 μg/well), PD‐L1 monoclonal antibody (SinoBiological, 10084‐MM33) was replaced with PD‐L1 monoclonal antibody (SinoBiological, B50010 ‐R678), and Goat anti‐Mouse IgG, HRP secondary antibody (SinoBiological, SSA007) was replaced with Goat anti‐Rabbit IgG, HRP secondary antibody (SinoBiological, SSA004).

Techniques: Injection, Construct, Control, Expressing, Virus, Lysis, Enzyme-linked Immunosorbent Assay, Binding Assay

PBAP Conjugated with Tumor‐Specific Antigens Enhances Synergistic Anti‐Tumor Activity When Combined with Clinical Antibodies and Antibody‐Drug Conjugates (ADCs) In Vitro. A) Schematic representation of the design of sPD‐1‐HER2 and PBAP‐HER2 (sPD‐1‐HER2‐Fc). PBAP‐HER2 was engineered via the fusion of extracellular domain of human PD‐1 (sPD‐1) with Domain IV of HER2 protein, followed by the incorporation of an Fc region to enhance protein stability and prolong in vivo half‐life. vB) Structural modeling of PBAP‐HER2 with AlphaFold 3. (C) Pharmacokinetic profiles of sPD‐1‐HER2 and PBAP‐HER2 following intravenous injection into C57BL/6J mice (n=3 mice/group, 100 µg/mice). Data are presented as the mean ± SD (n = 3). (D) The binding inhibition of PBAP‐HER2 on PD‐L1/PD‐1 interaction was assessed by ELISA. The absorbance was measured at 450 nm to determine the blocking effect. Data are presented as the mean ± SD (n = 3). (E) The fluorescence intensity of the antibody‐cell binding was analyzed using a flow cytometry to assess the blocking effect on the PD‐1/PD‐L1 pathway. (F) Diagram illustrating the mechanism by which PBAP‐HER2 synergizes with Herceptin and Kadcyla to kill PD‐L1‐positive target cells. Created with BioRender.com. (G) ADCC and ADCP activities were assessed using Jurkat‐FcγR reporter systems: ADCC (FcγRIIIa‐V158 variant) and ADCP (FcγRIIa‐R131 variant) in response to PBAP‐HER2/PBAP‐gE combined with Herceptin. PBAP‐HER2 in combination with Herceptin significantly enhanced ADCC and ADCP activities against HER2‐negative MDA‐MB‐231 cells. Representative of 3 independent experiments. Data are presented as mean ± SD (n = 3). (H) NK cells were co‐incubated with PBAP‐Her2 and Herceptin, against MDA‐MB‐231‐IFN‐γ (IFN‐γ induced, PD‐L1 + ) tumor cells and MDA‐MB‐231‐WT cells. NK cells, NK cells co‐incubated with PBAP‐Her2, NK cells co‐incubated with Herceptin, and all groups treated with anti‐FcγRIII blocking antibody were used as controls. Data are presented as mean ± SD of 3 independent experiments, each performed in triplicate. (I) Flow cytometry analysis of perforin, granzyme B, IFN‐γ and CD107a in NK cells. Representative of 3 independent experiments. (J) The CCK8 assay was used to evaluate the cytotoxicity of commercial ADCs (Kadcyla and Adcetris) combined with PBAP‐HER2. MDA‐MB‐231‐PD‐L1‐OE cells were treated with PBAP‐HER2 (10 µg/well) for 4 h, followed by ADC drugs (Kadcyla or Adcetris) at various concentrations (0.1, 1, 10, 100, 1000 ng/mL). After 24 h of incubation, cell viability was measured using the CCK8 assay. PBAP‐HER2 with Adcetris and HER2 protein with Kadcyla were used as controls. Representative of 3 independent experiments. Data are presented as mean ± SD (n = 3).

Journal: Advanced Science

Article Title: PD‐L1‐Binding Antigen Presenters: Redirecting Vaccine‐Induced Antibodies for Cancer Immunotherapy

doi: 10.1002/advs.202519574

Figure Lengend Snippet: PBAP Conjugated with Tumor‐Specific Antigens Enhances Synergistic Anti‐Tumor Activity When Combined with Clinical Antibodies and Antibody‐Drug Conjugates (ADCs) In Vitro. A) Schematic representation of the design of sPD‐1‐HER2 and PBAP‐HER2 (sPD‐1‐HER2‐Fc). PBAP‐HER2 was engineered via the fusion of extracellular domain of human PD‐1 (sPD‐1) with Domain IV of HER2 protein, followed by the incorporation of an Fc region to enhance protein stability and prolong in vivo half‐life. vB) Structural modeling of PBAP‐HER2 with AlphaFold 3. (C) Pharmacokinetic profiles of sPD‐1‐HER2 and PBAP‐HER2 following intravenous injection into C57BL/6J mice (n=3 mice/group, 100 µg/mice). Data are presented as the mean ± SD (n = 3). (D) The binding inhibition of PBAP‐HER2 on PD‐L1/PD‐1 interaction was assessed by ELISA. The absorbance was measured at 450 nm to determine the blocking effect. Data are presented as the mean ± SD (n = 3). (E) The fluorescence intensity of the antibody‐cell binding was analyzed using a flow cytometry to assess the blocking effect on the PD‐1/PD‐L1 pathway. (F) Diagram illustrating the mechanism by which PBAP‐HER2 synergizes with Herceptin and Kadcyla to kill PD‐L1‐positive target cells. Created with BioRender.com. (G) ADCC and ADCP activities were assessed using Jurkat‐FcγR reporter systems: ADCC (FcγRIIIa‐V158 variant) and ADCP (FcγRIIa‐R131 variant) in response to PBAP‐HER2/PBAP‐gE combined with Herceptin. PBAP‐HER2 in combination with Herceptin significantly enhanced ADCC and ADCP activities against HER2‐negative MDA‐MB‐231 cells. Representative of 3 independent experiments. Data are presented as mean ± SD (n = 3). (H) NK cells were co‐incubated with PBAP‐Her2 and Herceptin, against MDA‐MB‐231‐IFN‐γ (IFN‐γ induced, PD‐L1 + ) tumor cells and MDA‐MB‐231‐WT cells. NK cells, NK cells co‐incubated with PBAP‐Her2, NK cells co‐incubated with Herceptin, and all groups treated with anti‐FcγRIII blocking antibody were used as controls. Data are presented as mean ± SD of 3 independent experiments, each performed in triplicate. (I) Flow cytometry analysis of perforin, granzyme B, IFN‐γ and CD107a in NK cells. Representative of 3 independent experiments. (J) The CCK8 assay was used to evaluate the cytotoxicity of commercial ADCs (Kadcyla and Adcetris) combined with PBAP‐HER2. MDA‐MB‐231‐PD‐L1‐OE cells were treated with PBAP‐HER2 (10 µg/well) for 4 h, followed by ADC drugs (Kadcyla or Adcetris) at various concentrations (0.1, 1, 10, 100, 1000 ng/mL). After 24 h of incubation, cell viability was measured using the CCK8 assay. PBAP‐HER2 with Adcetris and HER2 protein with Kadcyla were used as controls. Representative of 3 independent experiments. Data are presented as mean ± SD (n = 3).

Article Snippet: For the ELISA blocking activity detection of PBAP‐gE, the same procedure was followed with the following modifications: human PD‐L1 (ECD, His Tag, SinoBiological, 10084‐H08H) protein was replaced with mouse PD‐L1 (ECD, His Tag, SinoBiological, 50010‐M08H), PBAP‐HER2 (1 μg/well and 10 μg/well) was replaced with PBAP‐gE (1 μg/well and 10 μg/well), PD‐L1 monoclonal antibody (SinoBiological, 10084‐MM33) was replaced with PD‐L1 monoclonal antibody (SinoBiological, B50010 ‐R678), and Goat anti‐Mouse IgG, HRP secondary antibody (SinoBiological, SSA007) was replaced with Goat anti‐Rabbit IgG, HRP secondary antibody (SinoBiological, SSA004).

Techniques: Activity Assay, In Vitro, In Vivo, Injection, Binding Assay, Inhibition, Enzyme-linked Immunosorbent Assay, Blocking Assay, Fluorescence, Flow Cytometry, Variant Assay, Incubation, CCK-8 Assay

PBAP‐HER2 Synergizes with Antibody‐Drug Conjugates to Enhance Anti‐tumor Efficacy in NSG Mice Bearing Subcutaneous Tumors. (A) Overview of Experimental Design. NSG mice were subcutaneously inoculated with MDA‐MB‐231 cells. Once the tumors reached approximately 100 mm 3 , mice were assigned to one of four treatment groups (n=5 mice/group): PBAP‐HER2 alone, Kadcyla alone, PBAP‐HER2 + Adcetris, and PBAP‐HER2 + Kadcyla. PBAP‐HER2 (150 µg/mouse) was administered intraperitoneally, followed by tail vein injections of Kadcyla (3 mg/kg) or Adcetris (3 mg/kg) 24 h later. Treatments were administered once a week for two consecutive cycles, with tumor growth monitored throughout the study. At the experimental endpoint, mice were euthanized, and tumor and tissue samples were collected for further analysis. Created with BioRender.com. (B) Representative tumor images for each experimental group are displayed in the left panel, with tumor volumes at the experimental endpoint shown in the right panel. Notably, the PBAP‐HER2 + Kadcyla group exhibited the most significant tumor regression, accompanied by robust tumor control, relative to all other groups. Data are presented as the mean ± SD (n = 5). Statistical significance was determined using one‐way ANOVA. Statistically significant differences were observed (p < 0.05). (C) Immunohistochemistry (IHC) analysis was performed to evaluate the intratumoral infiltration of PBAP‐HER2 and ADC drugs. The results demonstrated that PBAP‐HER2 effectively infiltrated the tumor tissue. Furthermore, Kadcyla was found to exhibit intratumoral infiltration exclusively when co‐administered with PBAP‐HER2. In contrast, Adcetris failed to infiltrate tumor tissues in the PBAP‐HER2 plus Adcetris combination group. Scale bars, 50 µm. (D) Immunofluorescence analysis further confirmed the specific efficacy of the PBAP‐HER2 + Kadcyla combination. Tumor sections revealed clear co‐localization of PBAP‐HER2 with PD‐L1 on tumor cells. Kadcyla was observed to enter tumor cells exclusively in the PBAP‐HER2 + Kadcyla group. In contrast, no intracellular ADC uptake was detected in the control groups (PBAP‐HER2 + Adcetris or Kadcyla only). Scale bars, 20 µm. (E) H&E staining showed no significant histopathological damage to major organs (heart, liver, spleen, lungs) in the experimental group, indicating a favorable safety profile. An increased presence of multinucleated giant cells was observed in the spleens, particularly in the PBAP‐HER2 + Kadcyla group, as indicated by white arrows. Scale bars, 60 µm.

Journal: Advanced Science

Article Title: PD‐L1‐Binding Antigen Presenters: Redirecting Vaccine‐Induced Antibodies for Cancer Immunotherapy

doi: 10.1002/advs.202519574

Figure Lengend Snippet: PBAP‐HER2 Synergizes with Antibody‐Drug Conjugates to Enhance Anti‐tumor Efficacy in NSG Mice Bearing Subcutaneous Tumors. (A) Overview of Experimental Design. NSG mice were subcutaneously inoculated with MDA‐MB‐231 cells. Once the tumors reached approximately 100 mm 3 , mice were assigned to one of four treatment groups (n=5 mice/group): PBAP‐HER2 alone, Kadcyla alone, PBAP‐HER2 + Adcetris, and PBAP‐HER2 + Kadcyla. PBAP‐HER2 (150 µg/mouse) was administered intraperitoneally, followed by tail vein injections of Kadcyla (3 mg/kg) or Adcetris (3 mg/kg) 24 h later. Treatments were administered once a week for two consecutive cycles, with tumor growth monitored throughout the study. At the experimental endpoint, mice were euthanized, and tumor and tissue samples were collected for further analysis. Created with BioRender.com. (B) Representative tumor images for each experimental group are displayed in the left panel, with tumor volumes at the experimental endpoint shown in the right panel. Notably, the PBAP‐HER2 + Kadcyla group exhibited the most significant tumor regression, accompanied by robust tumor control, relative to all other groups. Data are presented as the mean ± SD (n = 5). Statistical significance was determined using one‐way ANOVA. Statistically significant differences were observed (p < 0.05). (C) Immunohistochemistry (IHC) analysis was performed to evaluate the intratumoral infiltration of PBAP‐HER2 and ADC drugs. The results demonstrated that PBAP‐HER2 effectively infiltrated the tumor tissue. Furthermore, Kadcyla was found to exhibit intratumoral infiltration exclusively when co‐administered with PBAP‐HER2. In contrast, Adcetris failed to infiltrate tumor tissues in the PBAP‐HER2 plus Adcetris combination group. Scale bars, 50 µm. (D) Immunofluorescence analysis further confirmed the specific efficacy of the PBAP‐HER2 + Kadcyla combination. Tumor sections revealed clear co‐localization of PBAP‐HER2 with PD‐L1 on tumor cells. Kadcyla was observed to enter tumor cells exclusively in the PBAP‐HER2 + Kadcyla group. In contrast, no intracellular ADC uptake was detected in the control groups (PBAP‐HER2 + Adcetris or Kadcyla only). Scale bars, 20 µm. (E) H&E staining showed no significant histopathological damage to major organs (heart, liver, spleen, lungs) in the experimental group, indicating a favorable safety profile. An increased presence of multinucleated giant cells was observed in the spleens, particularly in the PBAP‐HER2 + Kadcyla group, as indicated by white arrows. Scale bars, 60 µm.

Article Snippet: For the ELISA blocking activity detection of PBAP‐gE, the same procedure was followed with the following modifications: human PD‐L1 (ECD, His Tag, SinoBiological, 10084‐H08H) protein was replaced with mouse PD‐L1 (ECD, His Tag, SinoBiological, 50010‐M08H), PBAP‐HER2 (1 μg/well and 10 μg/well) was replaced with PBAP‐gE (1 μg/well and 10 μg/well), PD‐L1 monoclonal antibody (SinoBiological, 10084‐MM33) was replaced with PD‐L1 monoclonal antibody (SinoBiological, B50010 ‐R678), and Goat anti‐Mouse IgG, HRP secondary antibody (SinoBiological, SSA007) was replaced with Goat anti‐Rabbit IgG, HRP secondary antibody (SinoBiological, SSA004).

Techniques: Control, Immunohistochemistry, Immunofluorescence, Staining