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human cervical cancer cell line hela s3  (ATCC)


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    Structured Review

    ATCC human cervical cancer cell line hela s3
    C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in <t>HeLa</t> cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.
    Human Cervical Cancer Cell Line Hela S3, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 23706 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "The C16orf87 protein is a subunit of the MIER corepressor complex controlling embryonic development and cell migration"

    Article Title: The C16orf87 protein is a subunit of the MIER corepressor complex controlling embryonic development and cell migration

    Journal: Scientific Reports

    doi: 10.1038/s41598-026-50740-7

    C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in HeLa cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.
    Figure Legend Snippet: C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in HeLa cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.

    Techniques Used: Protein-Protein interactions, Immunoprecipitation, Transfection, Isolation, Migration, In Vitro, Control, Purification



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    ATCC human cervical cancer cell line hela s3
    C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in <t>HeLa</t> cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.
    Human Cervical Cancer Cell Line Hela S3, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human cervical cancer cell line hela s3/product/ATCC
    Average 99 stars, based on 1 article reviews
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    ATCC cervical cancer cell line hela
    C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in <t>HeLa</t> cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.
    Cervical Cancer Cell Line Hela, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cervical cancer cell line hela/product/ATCC
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    ATCC human cervical cancer cell lines
    C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in <t>HeLa</t> cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.
    Human Cervical Cancer Cell Lines, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human cervical cancer cell lines/product/ATCC
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    ATCC cervical cancer cell line caski
    a , MYC ORF-based overexpression <t>sensitizes</t> <t>cervical</t> cancer cells to T cell cytotoxicity. The fraction of surviving HPV + cervical cancer cells ( y axis) in coculture with E7 TCR T cells (1:1, 48 h), is shown for <t>CaSki</t> cells transduced to express a control, BID or MYC ORF (mean ± s.d., n = 3 technical replicates per ORF). **** P < 0.001, ordinary one-way ANOVA, Dunnett’s multiple-comparison test. b , Fold-change in A375 cell viability after 24-h treatment with FasL (200 ng ml −1 ), shown for A375 cells with ORF-based overexpression of different sensitizing hits compared to A375 cells with a control ORF (mean ± s.d., n = 3–6 technical replicates per ORF). **** P < 0.0001, ** P < 0.01, ordinary one-way ANOVA, Dunnett’s multiple-comparison test, compared to control cells. c , UMAP of Perturb-seq data of control (NTC) and MYC CRISPRa cells, colored based on: (1) culture conditions, (2) sgRNA and MYC expression level, (3) the expression of the MYC GA signature and (4) the expression of the CRISPRa-resistance hit GAS7 (log 2 1p-transformed tp100k). d , Expression of MYC GA signature in control (NTC) cells and cells with MYC CRISPRa sgRNAs, further stratified based on MYC expression in monoculture (left) and coculture (right). The number of cells in each group is shown in parentheses ( n ). Boxplots: the middle line shows the median, the box edges show the 25th and 75th percentiles and the whiskers show the most extreme points that do not exceed ±1.5× the interquartile range (IQR). Further outliers are marked individually with circles (minima or maxima). **** P < 0.0001, one-tailed Student’s t -test.
    Cervical Cancer Cell Line Caski, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC human cervical cancer cell line hela
    Cleaved IL‐18 induction by 5‐FU in cancer cells other than pancreatic cancer cells. (A) Representative images <t>of</t> <t>HCT116</t> and <t>HeLa</t> cells treated with 5‐FU for 48 h in low‐nutrient culture medium (×10). 5‐FU was used at 10 μg/mL for HCT116 cells and 50 μg/mL for HeLa cells. Detached HCT116 cells were observed only after 5‐FU treatment. (B) HCT116 cells treated with 5‐FU were collected as attached or detached fractions; all other samples were collected as whole cells. Lysates were analyzed by western blotting with the indicated antibodies. β‐Actin was used as a loading control.
    Human Cervical Cancer Cell Line Hela, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human cervical cancer cell line hela/product/ATCC
    Average 99 stars, based on 1 article reviews
    human cervical cancer cell line hela - by Bioz Stars, 2026-05
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    ATCC human cervical cancer cell line
    Cleaved IL‐18 induction by 5‐FU in cancer cells other than pancreatic cancer cells. (A) Representative images <t>of</t> <t>HCT116</t> and <t>HeLa</t> cells treated with 5‐FU for 48 h in low‐nutrient culture medium (×10). 5‐FU was used at 10 μg/mL for HCT116 cells and 50 μg/mL for HeLa cells. Detached HCT116 cells were observed only after 5‐FU treatment. (B) HCT116 cells treated with 5‐FU were collected as attached or detached fractions; all other samples were collected as whole cells. Lysates were analyzed by western blotting with the indicated antibodies. β‐Actin was used as a loading control.
    Human Cervical Cancer Cell Line, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human cervical cancer cell line/product/ATCC
    Average 99 stars, based on 1 article reviews
    human cervical cancer cell line - by Bioz Stars, 2026-05
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    Image Search Results


    C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in HeLa cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.

    Journal: Scientific Reports

    Article Title: The C16orf87 protein is a subunit of the MIER corepressor complex controlling embryonic development and cell migration

    doi: 10.1038/s41598-026-50740-7

    Figure Lengend Snippet: C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in HeLa cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.

    Article Snippet: Human pancreatic cancer cell lines Panc-01 (ATCC, CRL-1469) and MiaPaCa-2 (ATCC, CRL-1420), mouse skeletal muscle cell line C2C12 (ATCC, CRL-1772), and human cervical cancer cell line HeLa S3 (ATCC, CCL-2.2) were used in this study.

    Techniques: Protein-Protein interactions, Immunoprecipitation, Transfection, Isolation, Migration, In Vitro, Control, Purification

    a , MYC ORF-based overexpression sensitizes cervical cancer cells to T cell cytotoxicity. The fraction of surviving HPV + cervical cancer cells ( y axis) in coculture with E7 TCR T cells (1:1, 48 h), is shown for CaSki cells transduced to express a control, BID or MYC ORF (mean ± s.d., n = 3 technical replicates per ORF). **** P < 0.001, ordinary one-way ANOVA, Dunnett’s multiple-comparison test. b , Fold-change in A375 cell viability after 24-h treatment with FasL (200 ng ml −1 ), shown for A375 cells with ORF-based overexpression of different sensitizing hits compared to A375 cells with a control ORF (mean ± s.d., n = 3–6 technical replicates per ORF). **** P < 0.0001, ** P < 0.01, ordinary one-way ANOVA, Dunnett’s multiple-comparison test, compared to control cells. c , UMAP of Perturb-seq data of control (NTC) and MYC CRISPRa cells, colored based on: (1) culture conditions, (2) sgRNA and MYC expression level, (3) the expression of the MYC GA signature and (4) the expression of the CRISPRa-resistance hit GAS7 (log 2 1p-transformed tp100k). d , Expression of MYC GA signature in control (NTC) cells and cells with MYC CRISPRa sgRNAs, further stratified based on MYC expression in monoculture (left) and coculture (right). The number of cells in each group is shown in parentheses ( n ). Boxplots: the middle line shows the median, the box edges show the 25th and 75th percentiles and the whiskers show the most extreme points that do not exceed ±1.5× the interquartile range (IQR). Further outliers are marked individually with circles (minima or maxima). **** P < 0.0001, one-tailed Student’s t -test.

    Journal: Nature Genetics

    Article Title: High-content CRISPR activation screens identify synthetically lethal RNA-based mechanisms to sensitize cancer cells to targeted T cell cytotoxicity

    doi: 10.1038/s41588-026-02561-7

    Figure Lengend Snippet: a , MYC ORF-based overexpression sensitizes cervical cancer cells to T cell cytotoxicity. The fraction of surviving HPV + cervical cancer cells ( y axis) in coculture with E7 TCR T cells (1:1, 48 h), is shown for CaSki cells transduced to express a control, BID or MYC ORF (mean ± s.d., n = 3 technical replicates per ORF). **** P < 0.001, ordinary one-way ANOVA, Dunnett’s multiple-comparison test. b , Fold-change in A375 cell viability after 24-h treatment with FasL (200 ng ml −1 ), shown for A375 cells with ORF-based overexpression of different sensitizing hits compared to A375 cells with a control ORF (mean ± s.d., n = 3–6 technical replicates per ORF). **** P < 0.0001, ** P < 0.01, ordinary one-way ANOVA, Dunnett’s multiple-comparison test, compared to control cells. c , UMAP of Perturb-seq data of control (NTC) and MYC CRISPRa cells, colored based on: (1) culture conditions, (2) sgRNA and MYC expression level, (3) the expression of the MYC GA signature and (4) the expression of the CRISPRa-resistance hit GAS7 (log 2 1p-transformed tp100k). d , Expression of MYC GA signature in control (NTC) cells and cells with MYC CRISPRa sgRNAs, further stratified based on MYC expression in monoculture (left) and coculture (right). The number of cells in each group is shown in parentheses ( n ). Boxplots: the middle line shows the median, the box edges show the 25th and 75th percentiles and the whiskers show the most extreme points that do not exceed ±1.5× the interquartile range (IQR). Further outliers are marked individually with circles (minima or maxima). **** P < 0.0001, one-tailed Student’s t -test.

    Article Snippet: The cervical cancer cell line CaSki (ATCC, cat. no. CRL-1550) was cultured in Roswell Park Memorial Institute (RPMI) medium with GlutaMAX (Gibco, cat. no. 72400-047) supplemented with 10% FBS and 1× Pen–Strep.

    Techniques: Over Expression, Control, Comparison, Expressing, Transformation Assay, One-tailed Test

    Cleaved IL‐18 induction by 5‐FU in cancer cells other than pancreatic cancer cells. (A) Representative images of HCT116 and HeLa cells treated with 5‐FU for 48 h in low‐nutrient culture medium (×10). 5‐FU was used at 10 μg/mL for HCT116 cells and 50 μg/mL for HeLa cells. Detached HCT116 cells were observed only after 5‐FU treatment. (B) HCT116 cells treated with 5‐FU were collected as attached or detached fractions; all other samples were collected as whole cells. Lysates were analyzed by western blotting with the indicated antibodies. β‐Actin was used as a loading control.

    Journal: Genes to Cells

    Article Title: Molecular Mechanism of Caspase‐8–Dependent Interleukin‐18 Activation in Pancreatic Cancer Cells Induced by 5‐Fluorouracil and Nutrient Starvation

    doi: 10.1111/gtc.70111

    Figure Lengend Snippet: Cleaved IL‐18 induction by 5‐FU in cancer cells other than pancreatic cancer cells. (A) Representative images of HCT116 and HeLa cells treated with 5‐FU for 48 h in low‐nutrient culture medium (×10). 5‐FU was used at 10 μg/mL for HCT116 cells and 50 μg/mL for HeLa cells. Detached HCT116 cells were observed only after 5‐FU treatment. (B) HCT116 cells treated with 5‐FU were collected as attached or detached fractions; all other samples were collected as whole cells. Lysates were analyzed by western blotting with the indicated antibodies. β‐Actin was used as a loading control.

    Article Snippet: Human pancreatic cancer cell lines (MIA PaCa‐2 and Panc‐1), human colorectal cancer cell line (HCT116), and human cervical cancer cell line (HeLa) were purchased from the American Type Culture Collection.

    Techniques: Western Blot, Control