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OriGene goat anti rabbit immunoglobulin gamma secondary antibody
The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, <t>Bcl2</t> , and Caspase 3 in E.tenella host cells.
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The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, <t>Bcl2</t> , and Caspase 3 in E.tenella host cells.
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Cell Signaling Technology Inc anti caspase 3 rabbit polyclonal ab
(A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
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Image Search Results


The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Article Snippet: p-p65 Rabbit Ab , Bioss , bs-0982R , 1: 1500.

Techniques: Expressing

The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Article Snippet: p-p65 Rabbit Ab , Bioss , bs-0982R , 1: 1500.

Techniques: Activity Assay

The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The mRNA expression of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2 , and Caspase 3 in E.tenella host cells.

Article Snippet: Bcl2 Rabbit Ab , Bioss , bs-0032R , 1: 1500.

Techniques: Expressing

The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Journal: Poultry Science

Article Title: Pathogenic mechanism of Eimeria tenella Et MIC2 promotes Eimeria tenella invasion and inhibits host cell apoptosis through binding to the ITGAV receptor

doi: 10.1016/j.psj.2026.106922

Figure Lengend Snippet: The protein activity changes of ITGAV, FAK, PLC, PKC, p65, ERK, JNK, p38, PI3K, Akt, Bax, Bcl2, and Caspase 3 in E.tenella host cells.

Article Snippet: Bcl2 Rabbit Ab , Bioss , bs-0032R , 1: 1500.

Techniques: Activity Assay

(A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) Caspase-3/7 activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.

Journal: bioRxiv

Article Title: Quinolinic acid phosphoribosyl transferase moonlights as an apoptosis regulator to empower lung cancer progression

doi: 10.64898/2026.04.01.715697

Figure Lengend Snippet: (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) Caspase-3/7 activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.

Article Snippet: For anti-Caspase-3 rabbit polyclonal Ab (Cell Signaling Technology, 9662S) 5% BSA in TBST was used to block the membranes instead of milk.

Techniques: Staining, Knockdown, Cell Culture, Western Blot, Co-Immunoprecipitation Assay, Activity Assay, Purification, Immunoprecipitation

In NSCLC cells as diagrammed in de novo NAD + biosynthesis is inactive, and NAD + pools are fueled by the salvage pathways and by the Preiss-Handler pathway. Instead, QPRT functions as an apoptosis inhibitor by interacting with caspase 3 and preventing its activation thereby conferring NSCLC resistance to apoptosis and enabling them to thrive through the stresses of tumor progression (2) .

Journal: bioRxiv

Article Title: Quinolinic acid phosphoribosyl transferase moonlights as an apoptosis regulator to empower lung cancer progression

doi: 10.64898/2026.04.01.715697

Figure Lengend Snippet: In NSCLC cells as diagrammed in de novo NAD + biosynthesis is inactive, and NAD + pools are fueled by the salvage pathways and by the Preiss-Handler pathway. Instead, QPRT functions as an apoptosis inhibitor by interacting with caspase 3 and preventing its activation thereby conferring NSCLC resistance to apoptosis and enabling them to thrive through the stresses of tumor progression (2) .

Article Snippet: For anti-Caspase-3 rabbit polyclonal Ab (Cell Signaling Technology, 9662S) 5% BSA in TBST was used to block the membranes instead of milk.

Techniques: Activation Assay