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human cervical cancer cell lines hela  (ATCC)


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    ATCC human cervical cancer cell lines hela
    Human Cervical Cancer Cell Lines Hela, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 24175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+cervical+cancer+cell+lines+hela/HeLa/pm41372482-37-0-25
    Average 99 stars, based on 24175 article reviews
    human cervical cancer cell lines hela - by Bioz Stars, 2026-09
    99/100 stars

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    Cell Culture:

    Article Title: Talarindigotin A: a cytotoxic indigotin derivative, from the mangrove endophytic fungus Talaromyces amestolkiae SCNU-F0041.
    Article Snippet: A new indigotin alkaloid, named talarindigotin A (1), along with the analogue 5H, 6H-quinindolin-11-one (2) were isolated from the mangrove endophytic fungus Talaromyces amestolkiae SCNU-F0041.. Their structures were assigned on the basis of NMR, HRMS, and single-crystal X-ray diffraction analysis.. In the cytotoxic bioassay, compound 1 showed great cytotoxicity against HepG2, Hela, HCT116, and Huh7 human cancer cell lines with IC50 values ranging from 2.08 to 4.58 μM.

    Article Title: Protective layer β-cyclodextrin within peanut (Arachis hypogaea L.) shells’ nanoparticles enhances intracellular stable fluorescence for bioimaging applications: An in vitro and in silico study
    Article Snippet: .. Human cervical cancer cell lines (HeLa) were obtained from ATCC and cultured in DMEM with the addition of 10 % FBS that contained 1 % penicillin–streptomycin in a T-75 culture flask at 37◦C in an incubator with 5 % CO2 condition. ..

    Article Title: Identification of circRNA-mediated competing endogenous RNA network involved in the development of cervical cancer.
    Article Snippet: .. Human cervical cancer cell lines HeLa, Siha, C33A, CaSki, and normal cervical epithelial cell line Ect1/E6E7 (ATCC, MD, USA) were cultured with DMEM medium (Procell, Wuhan, China) containing 10% FBS (Procell) and 1% streptomycin-penicillin (Hyclone) at 37◦C and 5% CO2 cultivation environment. ..

    Article Title: Polyelectrolyte nanoparticles derived from durian seed gum modified with chitosan for selective targeting in cancer cells.
    Article Snippet: The synthesis of natural polysaccharides from durian seed gum-modified chitosan as complex nanoparticles was successfully developed.. The complex formation of nanoparticles was confirmed by 1H NMR, indicating the interpenetrating polymer network between the durian seed gum and chitosan.. The material's physical properties were analyzed using ZETA potential, SEM, FTIR, swelling assay, and spectrofluorometer.

    Modification:

    Article Title: Talarindigotin A: a cytotoxic indigotin derivative, from the mangrove endophytic fungus Talaromyces amestolkiae SCNU-F0041.
    Article Snippet: A new indigotin alkaloid, named talarindigotin A (1), along with the analogue 5H, 6H-quinindolin-11-one (2) were isolated from the mangrove endophytic fungus Talaromyces amestolkiae SCNU-F0041.. Their structures were assigned on the basis of NMR, HRMS, and single-crystal X-ray diffraction analysis.. In the cytotoxic bioassay, compound 1 showed great cytotoxicity against HepG2, Hela, HCT116, and Huh7 human cancer cell lines with IC50 values ranging from 2.08 to 4.58 μM.

    Article Title: Polyelectrolyte nanoparticles derived from durian seed gum modified with chitosan for selective targeting in cancer cells.
    Article Snippet: The synthesis of natural polysaccharides from durian seed gum-modified chitosan as complex nanoparticles was successfully developed.. The complex formation of nanoparticles was confirmed by 1H NMR, indicating the interpenetrating polymer network between the durian seed gum and chitosan.. The material's physical properties were analyzed using ZETA potential, SEM, FTIR, swelling assay, and spectrofluorometer.



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    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.
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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