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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
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human cervical cancer cell line hela s3 - by Bioz Stars, 2026-05
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97
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: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cervical cancer cell line hela - by Bioz Stars, 2026-05
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95
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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human cervical cancer cell lines - by Bioz Stars, 2026-05
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99
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
99/100 stars
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99
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
99/100 stars
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ATCC human cervical cancer cell line siha
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 Siha, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/human cervical cancer cell line siha/product/ATCC
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human cervical cancer cell line siha - by Bioz Stars, 2026-05
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ATCC cervical cancer kb 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.
Cervical Cancer Kb 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
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cervical cancer kb 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

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