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sf9 insect cells  (ATCC)


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    ATCC sf9 insect cells
    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
    Sf9 Insect Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 2205 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "EZH2 Serine 21 Phosphorylation Restrains Compact-State PRC2 Activation and H3K27me3 Propagation"

    Article Title: EZH2 Serine 21 Phosphorylation Restrains Compact-State PRC2 Activation and H3K27me3 Propagation

    Journal: bioRxiv

    doi: 10.64898/2026.06.02.729660

    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. Sf9-purified PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
    Figure Legend Snippet: A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. Sf9-purified PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.

    Techniques Used: Purification, Recombinant, Phospho-proteomics, High Throughput Screening Assay, In Vitro, Incubation, Serial Dilution, Western Blot, Activity Assay, Sequencing, Residue, Knock-Out, Plasmid Preparation, Control, ChIP-sequencing, Expressing

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    Article Snippet: Non-limiting examples of mammalian helper cells include HEK293 cells, COS cells, HeLa cells, BHK cells, or CHO cells (see, e.g., ATCC® CRL-1573TM, ATCC® CRL-1651TM, ATCC® CRL-1650TM, ATCC® CCL-2, ATCC® CCL-10TM, or ATCC® CCL-61TM).

    Isolation:

    Article Title: Insights into the structure and modulation of human TWIK-2.
    Article Snippet: Briefly, the TWIK-2 expression vector was transformed into chemically competent DH10Bac cells (Thermo Fisher Scientific), and white colonies were selectedongentamicin-kanamycin-tetracycline LB agarplates. .. Isolated Bacmid DNA was used to transfect sf9 cells (ATCC #12659017) with Cellfectin-II reagent (Gibco) per the manufacturer’s protocol to make baculovirus P1. ..

    Suspension:

    Article Title: Selecting Raman spectra filtering based on an exhaustive statistical approach for inline bioprocesses monitoring using Sf9 insect cells
    Article Snippet: .. Sf9 cells, maintained in suspension (ATCC 1711), were cultured in Sf-900TM III serum-free medium (Thermo Fisher Scientific, USA) for the propagation of baculovirus and production of rabies virus-like particles (rabies VLP). .. For viral titration assays, Sf9 ET cells (Easy Titer), kindly provided by Professors Ralph Hopkins and Dominic Esposito from the National Cancer Institute (Frederick, MD, USA), were cultured in Sf-900TM III medium supplemented with 2.5% (v/v) fetal bovine serum (FBS, HyClone ® , Cytiva, USA).

    Cell Culture:

    Article Title: Selecting Raman spectra filtering based on an exhaustive statistical approach for inline bioprocesses monitoring using Sf9 insect cells
    Article Snippet: .. Sf9 cells, maintained in suspension (ATCC 1711), were cultured in Sf-900TM III serum-free medium (Thermo Fisher Scientific, USA) for the propagation of baculovirus and production of rabies virus-like particles (rabies VLP). .. For viral titration assays, Sf9 ET cells (Easy Titer), kindly provided by Professors Ralph Hopkins and Dominic Esposito from the National Cancer Institute (Frederick, MD, USA), were cultured in Sf-900TM III medium supplemented with 2.5% (v/v) fetal bovine serum (FBS, HyClone ® , Cytiva, USA).

    Virus:

    Article Title: Selecting Raman spectra filtering based on an exhaustive statistical approach for inline bioprocesses monitoring using Sf9 insect cells
    Article Snippet: .. Sf9 cells, maintained in suspension (ATCC 1711), were cultured in Sf-900TM III serum-free medium (Thermo Fisher Scientific, USA) for the propagation of baculovirus and production of rabies virus-like particles (rabies VLP). .. For viral titration assays, Sf9 ET cells (Easy Titer), kindly provided by Professors Ralph Hopkins and Dominic Esposito from the National Cancer Institute (Frederick, MD, USA), were cultured in Sf-900TM III medium supplemented with 2.5% (v/v) fetal bovine serum (FBS, HyClone ® , Cytiva, USA).



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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. <t>Sf9-purified</t> PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.
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    Image Search Results


    A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. Sf9-purified PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.

    Journal: bioRxiv

    Article Title: EZH2 Serine 21 Phosphorylation Restrains Compact-State PRC2 Activation and H3K27me3 Propagation

    doi: 10.64898/2026.06.02.729660

    Figure Lengend Snippet: A. Domain schematic of the purified recombinant core PRC2 subunits EZH2, SUZ12, EED, and RBBP4, with annotated phosphorylation sites. Yellow circles denote phosphorylation sites reported in high-throughput proteomic studies, and red circles denote sites reported in low-throughput studies. B. In vitro histone methyltransferase assays comparing untreated recombinant PRC2 and PRC2 dephosphorylated with lambda phosphatase. Sf9-purified PRC2 complexes were incubated with recombinant nucleosomes and a 2-fold serial dilution of stimulatory H3K27me3 peptide, beginning at 40 μM. Reaction products were analyzed by immunoblotting. C. Quantification of PRC2 catalytic activity in response to increasing concentrations of stimulatory H3K27me3 peptide. Untreated or lambda phosphatase-treated recombinant PRC2 was incubated with recombinant nucleosomes, and methyltransferase activity was measured by incorporation of 3 H-SAM. Data are shown as mean ± SEM. D. In vitro methyltransferase activity of recombinant PRC2 complexes containing wild-type EZH2, EZH2 S21D, or EZH2 S21A, assayed before or after lambda phosphatase treatment. Complexes were incubated with recombinant nucleosomes, and activity was quantified by incorporation of 3 H-SAM. Data are shown as mean ± SEM, with individual replicate values indicated. Statistical comparisons are indicated above the bars. E. EZH2 domain schematic and multiple sequence alignment of the conserved N-terminal region surrounding S21. The AKT1 consensus motif and S21 residue are indicated. F. Immunoblot analysis of Ezh2 knockout MEFs reconstituted with FLAG-tagged wild-type EZH2, S21D, S21A, or empty vector. GAPDH serves as a loading control. G. Heatmaps and aggregate profiles showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal centered on H3K27me3 or EZH2 peaks in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. ChIP-seq experiments were normalized using exogenous spike-in chromatin. H. Representative genome browser tracks showing spike-in-normalized H3K27me3 and EZH2 ChIP-seq signal at Polycomb target loci in Ezh2 -knockout MEFs expressing the indicated EZH2 transgenes or empty vector. I. Immunoblot analysis of FLAG coimmunoprecipitation from nuclear extracts of Ezh2 knockout MEFs expressing the indicated FLAG-tagged EZH2 transgenes or empty vector control.

    Article Snippet: Sf9 insect cells were obtained from ATCC (CRL-1711; RRID:CVCL 0549) and were used for baculovirus-mediated expression of recombinant PRC2 complexes.

    Techniques: Purification, Recombinant, Phospho-proteomics, High Throughput Screening Assay, In Vitro, Incubation, Serial Dilution, Western Blot, Activity Assay, Sequencing, Residue, Knock-Out, Plasmid Preparation, Control, ChIP-sequencing, Expressing

    Fig. 4. Morphological observation of Sf9 cells. (a) untreated, (b) treated with D15 , and (c) treated with azadirachtin.

    Journal: Journal of Pesticide Science

    Article Title: Design, synthesis, and insecticidal activity evaluation of piperine-phenylene diamine derivatives

    doi: 10.1584/jpestics.D25-065

    Figure Lengend Snippet: Fig. 4. Morphological observation of Sf9 cells. (a) untreated, (b) treated with D15 , and (c) treated with azadirachtin.

    Article Snippet: Spodoptera exigua were purchased from Henan Jiyuan Baiyun Industry Co., Ltd. Sf9 cells ( S . frugiperda ovary cells), thiazole blue (MTT) and dimethyl sulfoxide (DMSO) were purchased from Wuhan Procell Life Technology Co., Ltd. One Step TUNEL Apoptosis Assay Kit and universal genomic DNA purification mini spin kit were purchased from Shanghai Beyotime Institute of Biotechnology.

    Techniques:

    Fig. 5. Morphological observation of Sf9 cells. (a) untreated, (b) treated with J1 , and (c) treated with azadirachtin.

    Journal: Journal of Pesticide Science

    Article Title: Design, synthesis, and insecticidal activity evaluation of piperine-phenylene diamine derivatives

    doi: 10.1584/jpestics.D25-065

    Figure Lengend Snippet: Fig. 5. Morphological observation of Sf9 cells. (a) untreated, (b) treated with J1 , and (c) treated with azadirachtin.

    Article Snippet: Spodoptera exigua were purchased from Henan Jiyuan Baiyun Industry Co., Ltd. Sf9 cells ( S . frugiperda ovary cells), thiazole blue (MTT) and dimethyl sulfoxide (DMSO) were purchased from Wuhan Procell Life Technology Co., Ltd. One Step TUNEL Apoptosis Assay Kit and universal genomic DNA purification mini spin kit were purchased from Shanghai Beyotime Institute of Biotechnology.

    Techniques:

    Fig. 7. Annexin V-FITC/PI staining of Sf9 cells. (a) untreated, (b) treated with J1 , and (c) treated with azadirachtin.

    Journal: Journal of Pesticide Science

    Article Title: Design, synthesis, and insecticidal activity evaluation of piperine-phenylene diamine derivatives

    doi: 10.1584/jpestics.D25-065

    Figure Lengend Snippet: Fig. 7. Annexin V-FITC/PI staining of Sf9 cells. (a) untreated, (b) treated with J1 , and (c) treated with azadirachtin.

    Article Snippet: Spodoptera exigua were purchased from Henan Jiyuan Baiyun Industry Co., Ltd. Sf9 cells ( S . frugiperda ovary cells), thiazole blue (MTT) and dimethyl sulfoxide (DMSO) were purchased from Wuhan Procell Life Technology Co., Ltd. One Step TUNEL Apoptosis Assay Kit and universal genomic DNA purification mini spin kit were purchased from Shanghai Beyotime Institute of Biotechnology.

    Techniques: Staining

    Fig. 8. Flow cytometry analysis of Sf9 cells. (a) untreated, (b) treated with D15 , and (c) treated with J1 .

    Journal: Journal of Pesticide Science

    Article Title: Design, synthesis, and insecticidal activity evaluation of piperine-phenylene diamine derivatives

    doi: 10.1584/jpestics.D25-065

    Figure Lengend Snippet: Fig. 8. Flow cytometry analysis of Sf9 cells. (a) untreated, (b) treated with D15 , and (c) treated with J1 .

    Article Snippet: Spodoptera exigua were purchased from Henan Jiyuan Baiyun Industry Co., Ltd. Sf9 cells ( S . frugiperda ovary cells), thiazole blue (MTT) and dimethyl sulfoxide (DMSO) were purchased from Wuhan Procell Life Technology Co., Ltd. One Step TUNEL Apoptosis Assay Kit and universal genomic DNA purification mini spin kit were purchased from Shanghai Beyotime Institute of Biotechnology.

    Techniques: Flow Cytometry