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ht29  (ATCC)


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    Structured Review

    ATCC ht29
    Inhibition of cologenecity in colorectal cancer cells by NVD. (Clonogenic assay; 7 days). a , b NVD administration (40 and 60 μM) of HCT116 and <t>HT29</t> cells inhibiting colony formation. Each value represents a mean ± SD (n = 3)
    Ht29, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 2950 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+tissue+expression+pattern/HT-29/pmc06359839-49-8-37
    Average 99 stars, based on 2950 article reviews
    ht29 - by Bioz Stars, 2026-11
    99/100 stars

    Images

    1) Product Images from "Growth inhibition and apoptosis in colorectal cancer cells induced by Vitamin D-Nanoemulsion (NVD): involvement of Wnt/β-catenin and other signal transduction pathways"

    Article Title: Growth inhibition and apoptosis in colorectal cancer cells induced by Vitamin D-Nanoemulsion (NVD): involvement of Wnt/β-catenin and other signal transduction pathways

    Journal: Cell & Bioscience

    doi: 10.1186/s13578-019-0277-z

    Inhibition of cologenecity in colorectal cancer cells by NVD. (Clonogenic assay; 7 days). a , b NVD administration (40 and 60 μM) of HCT116 and HT29 cells inhibiting colony formation. Each value represents a mean ± SD (n = 3)
    Figure Legend Snippet: Inhibition of cologenecity in colorectal cancer cells by NVD. (Clonogenic assay; 7 days). a , b NVD administration (40 and 60 μM) of HCT116 and HT29 cells inhibiting colony formation. Each value represents a mean ± SD (n = 3)

    Techniques Used: Inhibition, Clonogenic Assay

    a , b NVD treatment on HCT116 and HT29 cells resulted in accumulation of cells at the G2-phase and growth inhibition and apoptosis. After 24 h incubation of NVD treated cells and staining with propidium iodide, DNA content was analyzed by flow cytometry. c , d NVD treatment on HCT116 and HT29 cells resulted in accumulation of cells at the G2-phase. After 24 h incubation of NVD treated cells and staining with propidium iodide, DNA content was analyzed by flow cytometry. Percentage of cell population in G2-phase of the cell cycle is shown. Experiments were performed in triplicate
    Figure Legend Snippet: a , b NVD treatment on HCT116 and HT29 cells resulted in accumulation of cells at the G2-phase and growth inhibition and apoptosis. After 24 h incubation of NVD treated cells and staining with propidium iodide, DNA content was analyzed by flow cytometry. c , d NVD treatment on HCT116 and HT29 cells resulted in accumulation of cells at the G2-phase. After 24 h incubation of NVD treated cells and staining with propidium iodide, DNA content was analyzed by flow cytometry. Percentage of cell population in G2-phase of the cell cycle is shown. Experiments were performed in triplicate

    Techniques Used: Inhibition, Incubation, Staining, Flow Cytometry

    Percentage of cell population after administration of NVD
    Figure Legend Snippet: Percentage of cell population after administration of NVD

    Techniques Used:

    Effect of NVD treatment of HCT116 and HT29 ( a , b ) cells on protein expression of cdc2, WAF1/p21, cdk 2, 4 cyclin A, B1, E2 and ( c , d ) showing active Caspase 3, 7, 9 and PARP. Cells were administrated with NVD (20, 40 and 60 μM) for 24 h and 48 h and harvested. Total cell lysates were prepared and 40 μM proteins was subjected to SDS page followed by immunoblot analysis and chemiluminescence detection. Equal loading of protein was verified by stripping the Immunoblot and again probing it for Actin. The immunoblots shown here are representative of three individual experiments with similar results
    Figure Legend Snippet: Effect of NVD treatment of HCT116 and HT29 ( a , b ) cells on protein expression of cdc2, WAF1/p21, cdk 2, 4 cyclin A, B1, E2 and ( c , d ) showing active Caspase 3, 7, 9 and PARP. Cells were administrated with NVD (20, 40 and 60 μM) for 24 h and 48 h and harvested. Total cell lysates were prepared and 40 μM proteins was subjected to SDS page followed by immunoblot analysis and chemiluminescence detection. Equal loading of protein was verified by stripping the Immunoblot and again probing it for Actin. The immunoblots shown here are representative of three individual experiments with similar results

    Techniques Used: Expressing, SDS Page, Western Blot, Stripping Membranes

    a Effect of treatment of NVD to HCT116 and HT29 cell lines on protein expression of Bax, Bcl2, Bak and Bcl-X L . b Immunoblot analysis of β-catenin expression of HCT116 and HT29 in NVD treated group as compared to control group. The cells were administrated with NVD for 48 h and harvested and cell lysates prepared. The data are representative of three independent experiments with similar results
    Figure Legend Snippet: a Effect of treatment of NVD to HCT116 and HT29 cell lines on protein expression of Bax, Bcl2, Bak and Bcl-X L . b Immunoblot analysis of β-catenin expression of HCT116 and HT29 in NVD treated group as compared to control group. The cells were administrated with NVD for 48 h and harvested and cell lysates prepared. The data are representative of three independent experiments with similar results

    Techniques Used: Expressing, Western Blot, Control

    a Modulation of β -catenin expression by NVD treatment in HCT116 ( a ) and HT29 ( b ) cells. mRNA expression of β-catenin in NVD treated HCT116 and HT29 cells (RT-PCR), experiment performed in triplicate (mean ± SD), **p < 0.01. b Effect of NVD on protein expression of β-catenin, Survivin and phosphorylation of Akt at Ser473 in HCT116 and HT29 cells., Total cell lysate were prepared and 40 μM proteins was subjected to SDS-page followed by Immunoblot analysis and chemiluminescence detection. Equal loading of protein was confirmed by stripping the immunoblot and reprobing it for β-Actin
    Figure Legend Snippet: a Modulation of β -catenin expression by NVD treatment in HCT116 ( a ) and HT29 ( b ) cells. mRNA expression of β-catenin in NVD treated HCT116 and HT29 cells (RT-PCR), experiment performed in triplicate (mean ± SD), **p < 0.01. b Effect of NVD on protein expression of β-catenin, Survivin and phosphorylation of Akt at Ser473 in HCT116 and HT29 cells., Total cell lysate were prepared and 40 μM proteins was subjected to SDS-page followed by Immunoblot analysis and chemiluminescence detection. Equal loading of protein was confirmed by stripping the immunoblot and reprobing it for β-Actin

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Phospho-proteomics, SDS Page, Western Blot, Stripping Membranes

    Imunofluorescence staining of HCT116 ( b ) and HT29 ( d ) demonstrating expression of β-catenin in both NVD treated (60 µM) as compared to control HCT116 ( a ) and HT29 ( c ) cells (untreated). Alexa fluor staining of β-catenin of both cell lines (green fluorescence) and counter stained with DAPI (blue fluorescence) were observed
    Figure Legend Snippet: Imunofluorescence staining of HCT116 ( b ) and HT29 ( d ) demonstrating expression of β-catenin in both NVD treated (60 µM) as compared to control HCT116 ( a ) and HT29 ( c ) cells (untreated). Alexa fluor staining of β-catenin of both cell lines (green fluorescence) and counter stained with DAPI (blue fluorescence) were observed

    Techniques Used: Staining, Expressing, Control, Fluorescence

    Western blot analysis of cellular lysates prepared from HCT116 and HT29 cells. Lysates prepared from HCT116 and HT29 cells, initially seeded at density of 1.5 × 10 4 cells were administrated with 20, 40 and 60 µM concentrations of NVD. The blots probed with CK2 αα’, PI3-K, STAT3, STAT P-Try705, NFκB p65 P-S529, IκBα P-S32/36 and xIAP antibodies were shown. Actin blots are shown as loading controls. Data based on three different experiments, each carried out in triplicate
    Figure Legend Snippet: Western blot analysis of cellular lysates prepared from HCT116 and HT29 cells. Lysates prepared from HCT116 and HT29 cells, initially seeded at density of 1.5 × 10 4 cells were administrated with 20, 40 and 60 µM concentrations of NVD. The blots probed with CK2 αα’, PI3-K, STAT3, STAT P-Try705, NFκB p65 P-S529, IκBα P-S32/36 and xIAP antibodies were shown. Actin blots are shown as loading controls. Data based on three different experiments, each carried out in triplicate

    Techniques Used: Western Blot

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    Article Snippet: 17632/dkhzjnzxp5.1 The mass spectrometry raw files and the MaxQuant search results files This paper PRIDE: PXD065587 Experimental models: Cell lines Human: HEK293T cells ATCC CRL-3216 Human: HT29 cells CRUK Scotland Institute stocks (obtained from ATCC) N/A Human: hTERT-HPNE cells ATCC CRL-4023 Human: IMR-90 cells CRUK Scotland Institute stocks (obtained from ATCC) N/A Human: LNCaP cells CRUK Scotland Institute stocks (obtained from ATCC) N/A Human: MCF-7 cells CRUK Scotland Institute stocks (obtained from ATCC) N/A Human: MRC-5 cells CRUK Scotland Institute stocks (obtained from ATCC) N/A Human: Phoenix-ECO cells ATCC Cat# CRL-3214 Human: Phoenix-AMPHO cells ATCC Cat# CRL-3213 Human: hTERT RPE-1 cells CRUK Scotland Institute stocks (obtained from ATCC) N/A Human: p62 knockout LNCap cells This article N/A Human: p62 knockout LNCap cells with an empty vector This article N/A Human: p62 knockout LNCap cells overexpressing p62 WT This article N/A Human: p62 knockout LNCap cells overexpressing p62 D329* This article N/A Human: p62 knockout LNCap cells overexpressing p62 D329E This article N/A Human: p62 knockout LNCap cells overexpressing p62 D329G This article N/A Human: p62 knockout LNCap cells overexpressing p62 D329N This article N/A Human: p62 knockout HT29 cells with an empty vector This article N/A Human: p62 knockout HT29 cells overexpressing p62 WT This article N/A Human: p62 knockout HT29 cells overexpressing p62 D329* This article N/A Human: p62 knockout HT29 cells overexpressing p62 D329G This article N/A Mouse: MEF p62G331D/G331D This article N/A (Continued on next page) ll OPEN ACCESS Article e3 Molecular Cell 86, 1–13.e1–e11, April 16, 2026

    Article Title: Mechanism-based prediction of drug synergy via network controllability analysis of therapeutic pathways in intractable diseases
    Article Snippet: The HT-29 cell line was purchased directly from the American Type Culture Collection (ATCC) in 2021.

    Mutagenesis:

    Article Title: 4-Acetylantrocamol LT3 suppresses colorectal cancer growth and metastasis via PI3K/AKT and MAPK pathway modulation
    Article Snippet: .. Human CRC cell lines, HCT116 (KRAS mutant), HT-29 and Caco-2, were purchased from the American Type Culture Collection (ATCC; HCT116, CCL-247; HT-29, HTB-38; Caco-2, HTB-37). .. Cells were cultured in Dulbecco's Modified Eagle Medium (Gibco; Thermo Fisher Scientific, Inc.) supplemented with 10% fetal bovine serum (Gibco; Thermo Fisher Scientific, Inc.) and 1% penicillin-streptomycin and maintained in a humidified incubator at 37°C with 5% CO 2 .

    Cell Culture:

    Article Title: Long noncoding RNA AC007637.1 inhibits tumorigenesis by regulating the Trim25/PCNA axis in colorectal cancer.
    Article Snippet: .. Materials and methods Cell lines Caco2, DLD1, LoVo, HCT116, HCT8, HT29, SW480 and RKO cells were purchased from ATCC and cultured according to the manufacturer's instructions. ..

    Article Title: Distinct membrane interaction mechanisms of gramicidin A and S in mammalian cells: A combined experimental and molecular dynamics study.
    Article Snippet: Gramicidins, a class of ionophores, with a well-known antimicrobial activity against bacteria, and more recently against cancer cells, present two distinct structure types: linear peptides for Gramicidin A, B and C and cyclic peptide for Gramicidin S. Independent of their structure, the first stage of their action mechanism involves their interaction with the plasma membrane of the cells.. Considering this, we were interested to study how the peptide structure affects cell properties (cell viability, LDH release, etc) and how it correlates with membrane fluidity parameters (GP , ΔSr, Rs) and molecular simulation parameters (APL, bilayer thickness, and GA membrane permeation).. We demonstrated different action mechanisms for the two Gramicidins when applied to mammalian cells: a decrease in cell viability and an increase in LDH release, which correlate well with changes at the plasma membrane level.

    Article Title: Autophagy-associated marker and stress-response changes in ASA- and 5-FU-treated 3D colorectal cancer spheroid models exposed to 3-MA or CQ
    Article Snippet: .. Cell lines and cell culture The HT29 human colorectal adenocarcinoma cell line and the HCT116 human colorectal carcinoma cell line are established continuous cell lines originally procured from the American Type Culture Collection (ATCC) and maintained as in-house departmental stocks. ..

    Modification:

    Article Title: Distinct membrane interaction mechanisms of gramicidin A and S in mammalian cells: A combined experimental and molecular dynamics study.
    Article Snippet: Gramicidins, a class of ionophores, with a well-known antimicrobial activity against bacteria, and more recently against cancer cells, present two distinct structure types: linear peptides for Gramicidin A, B and C and cyclic peptide for Gramicidin S. Independent of their structure, the first stage of their action mechanism involves their interaction with the plasma membrane of the cells.. Considering this, we were interested to study how the peptide structure affects cell properties (cell viability, LDH release, etc) and how it correlates with membrane fluidity parameters (GP , ΔSr, Rs) and molecular simulation parameters (APL, bilayer thickness, and GA membrane permeation).. We demonstrated different action mechanisms for the two Gramicidins when applied to mammalian cells: a decrease in cell viability and an increase in LDH release, which correlate well with changes at the plasma membrane level.



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