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ht1376 cells  (ATCC)


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    Structured Review

    ATCC ht1376 cells
    Spheroids representing three bladder cancer cell lines (HCV29, T24, <t>HT1376)</t> were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).
    Ht1376 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 435 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ht1376+cells/HT-1376/bio_rxiv__64898__2025__12__03__692076-141-38-32
    Average 96 stars, based on 435 article reviews
    ht1376 cells - by Bioz Stars, 2026-09
    96/100 stars

    Images

    1) Product Images from "Matrix mechanics governs mechano-metabolic adaptation across cancer grades in bladder spheroids"

    Article Title: Matrix mechanics governs mechano-metabolic adaptation across cancer grades in bladder spheroids

    Journal: bioRxiv

    doi: 10.64898/2025.12.03.692076

    Spheroids representing three bladder cancer cell lines (HCV29, T24, HT1376) were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).
    Figure Legend Snippet: Spheroids representing three bladder cancer cell lines (HCV29, T24, HT1376) were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).

    Techniques Used: Control

    Related Articles

    Cell Culture:

    Article Title: Transcriptional-translational conflict is a barrier to cellular transformation and cancer progression.
    Article Snippet: .. HT1197 and HT1376 cells were cultured in Eagle’s Minimum Essential Medium (ATCC, 30–2003) supplemented with 10% fetal bovine serum (Cytiva, SH3039603s), and 1%penicillin/streptomycin (Gibco, 15140-122). .. KU1919 cells were cultured in RPMI1640 (Gibco, 11875-119) supplemented with 10% fetal bovine serum, and 1% e6 Cancer Cell 41, 853–870.e1–e13, May 8, 2023 penicillin/streptomycin.

    Transplantation Assay:

    Article Title: Insights into the Safety and Versatility of 4D Printed Intravesical Drug Delivery Systems.
    Article Snippet: .. HT1376 cells were obtained by American Type Culture Collection (ATCC), while THP-1 cells were kindly provided by Dr. Irma Saulle, Department of Pathophysiology and Transplantation, Università degli Studi di Milano. ..

    Article Title: Insights into the Safety and Versatility of 4D Printed Intravesical Drug Delivery Systems
    Article Snippet: .. HT1376 cells were obtained by American Type Culture Collection (ATCC), while THP-1 cells were kindly provided by Dr. Irma Saulle, Department of Pathophysiology and Transplantation, Università degli Studi di Milano. ..

    other:

    Article Title: Transcriptional-translational conflict is a barrier to cellular transformation and cancer progression.
    Article Snippet: UMUC11 cells were cultured in DMEM (Gibco, 11965-092) supplemented with 10% fetal bovine serum, and 1% penicillin/streptomycin.



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    Spheroids representing three bladder cancer cell lines (HCV29, T24, <t>HT1376)</t> were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).
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    Spheroids representing three bladder cancer cell lines (HCV29, T24, <t>HT1376)</t> were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).
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    Figure 1. HEK293, T24, and <t>HT1376</t> cell lines were subjected to survival assays to assess their responses to varying extracellular pH levels. Cells were plated in 96-well plates at a density of 2 × 104 cells/mL and incubated for 72 h under different pH conditions. Low pH significantly inhibited the growth of normal HEK293 cells, while bladder cancer (BC) cells exhibited resistance to low pH. Notably, HT1376 cells were less sensitive to pH changes compared to T24 cells. Data are presented as mean ± SD from four independent experiments.
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    Figure 1. HEK293, T24, and <t>HT1376</t> cell lines were subjected to survival assays to assess their responses to varying extracellular pH levels. Cells were plated in 96-well plates at a density of 2 × 104 cells/mL and incubated for 72 h under different pH conditions. Low pH significantly inhibited the growth of normal HEK293 cells, while bladder cancer (BC) cells exhibited resistance to low pH. Notably, HT1376 cells were less sensitive to pH changes compared to T24 cells. Data are presented as mean ± SD from four independent experiments.
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    ATCC bladder cancer cell line ht1376
    Figure 1. Discovery and characterization of the PSCA antibody fab G7.(a) fab G7 binding to recombinant PSCA-Fc protein measured by ELISA. Bovine serum albumin (BSA) was used as a negative control. Experiments were performed in duplicate and the error bars denote ± SD, n = 2. (b) Kinetics of fab G7 binding to PSCA-Fc, as measured by Blitz. (c) Fab G7 binding to PSCA positive (PC-3-PSCA, Du-145-PSCA and <t>HT1376</t> cells) and PSCA negative cells (PC-3, Du-145 and CHO-K1 cells) as tested by flow cytometry. An irrelevant fab (anti-SARS-CoV-2 fab ab1) was used as the isotype control. Fab G7 at the concentration of 500 nM was incubated with cells. (d-g) competition of fab G7 and fab F12 binding to HT1376 cell surface-associated PSCA by the recombinant PSCA-Fc protein (d and f) and by the murine PSCA antibody 7F5 (e and g). 500 nM of fab G7 or 200 nM of F12 was incubated with cells in the presence of gradient concentration of competitors. The bound fab G7 or F12 was detected by the pe-conjugated anti-flag tag antibody.
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    Image Search Results


    Spheroids representing three bladder cancer cell lines (HCV29, T24, HT1376) were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).

    Journal: bioRxiv

    Article Title: Matrix mechanics governs mechano-metabolic adaptation across cancer grades in bladder spheroids

    doi: 10.64898/2025.12.03.692076

    Figure Lengend Snippet: Spheroids representing three bladder cancer cell lines (HCV29, T24, HT1376) were embedded in collagen–hyaluronan (Col–HA) hydrogels. Relative expressions of E-cadherin, N-cadherin, hexokinase 2 (HK2), and syndecan-4 (SDC4) were normalized to control (i.e., expressions in spheroids grown only in culture medium, n = 3) and converted to fold change. Statistical significance was obtained by unpaired Student’s t-test at the level of 0.05 (* p < 0.01, **p <0.001, ***p <0.0001).

    Article Snippet: Roswell Park Memorial Institute 1640 culture medium (RPMI, Merck, Poland) supplemented with 10% Fetal Bovine Serum (FBS, ATCC, USA) was used for HCV29 and T24 cells, and Eagle’s Minimum Essential Medium (EMEM, ATCC, USA) with 10% FBS for HT1376 cells.

    Techniques: Control

    Figure 1. HEK293, T24, and HT1376 cell lines were subjected to survival assays to assess their responses to varying extracellular pH levels. Cells were plated in 96-well plates at a density of 2 × 104 cells/mL and incubated for 72 h under different pH conditions. Low pH significantly inhibited the growth of normal HEK293 cells, while bladder cancer (BC) cells exhibited resistance to low pH. Notably, HT1376 cells were less sensitive to pH changes compared to T24 cells. Data are presented as mean ± SD from four independent experiments.

    Journal: Current issues in molecular biology

    Article Title: Acidic Microenvironment Enhances Cisplatin Resistance in Bladder Cancer via Bcl-2 and XIAP.

    doi: 10.3390/cimb47010043

    Figure Lengend Snippet: Figure 1. HEK293, T24, and HT1376 cell lines were subjected to survival assays to assess their responses to varying extracellular pH levels. Cells were plated in 96-well plates at a density of 2 × 104 cells/mL and incubated for 72 h under different pH conditions. Low pH significantly inhibited the growth of normal HEK293 cells, while bladder cancer (BC) cells exhibited resistance to low pH. Notably, HT1376 cells were less sensitive to pH changes compared to T24 cells. Data are presented as mean ± SD from four independent experiments.

    Article Snippet: We used the BC cell lines HT1376 and T24, as well as human embryonic kidney 293 (HEK293) cells, purchased from the American Type Culture Collection (ATCC, Manassas, VA, USA).

    Techniques: Incubation

    Figure 3. Effects of combinatory treatment with cisplatin (CDDP) and autophagy inhibitor chloro- quine, or BCL-2 inhibitor navitoclax, at varying pH levels on cell viability. The time-dependent changes at 0 h, 24 h, 48 h, and 72 h of culturing are shown in each graph. CDDP was used at a concen- tration of 2 µM. Relative cell viability was assessed using the MTS assay after 72 h. Two asterisks (**) indicate that the p-value is less than 0.01, ns indicates no significant difference. (a) Chloroquine was administered at concentrations of 15 µM and 30 µM. Under neutral pH conditions, chloroquine inhib- ited HT1376 growth in a concentration-dependent manner, both with and without CDDP; this effect was not observed in an acidic environment. (b) Navitoclax was administered at concentrations of 2 µM and 4 µM. Bladder cancer (BC) cells cultured under acidic conditions showed reduced survival with navitoclax treatment, while no significant effect was noted under neutral pH conditions.

    Journal: Current issues in molecular biology

    Article Title: Acidic Microenvironment Enhances Cisplatin Resistance in Bladder Cancer via Bcl-2 and XIAP.

    doi: 10.3390/cimb47010043

    Figure Lengend Snippet: Figure 3. Effects of combinatory treatment with cisplatin (CDDP) and autophagy inhibitor chloro- quine, or BCL-2 inhibitor navitoclax, at varying pH levels on cell viability. The time-dependent changes at 0 h, 24 h, 48 h, and 72 h of culturing are shown in each graph. CDDP was used at a concen- tration of 2 µM. Relative cell viability was assessed using the MTS assay after 72 h. Two asterisks (**) indicate that the p-value is less than 0.01, ns indicates no significant difference. (a) Chloroquine was administered at concentrations of 15 µM and 30 µM. Under neutral pH conditions, chloroquine inhib- ited HT1376 growth in a concentration-dependent manner, both with and without CDDP; this effect was not observed in an acidic environment. (b) Navitoclax was administered at concentrations of 2 µM and 4 µM. Bladder cancer (BC) cells cultured under acidic conditions showed reduced survival with navitoclax treatment, while no significant effect was noted under neutral pH conditions.

    Article Snippet: We used the BC cell lines HT1376 and T24, as well as human embryonic kidney 293 (HEK293) cells, purchased from the American Type Culture Collection (ATCC, Manassas, VA, USA).

    Techniques: MTS Assay, Inhibition, Concentration Assay, Cell Culture

    Figure 1. Discovery and characterization of the PSCA antibody fab G7.(a) fab G7 binding to recombinant PSCA-Fc protein measured by ELISA. Bovine serum albumin (BSA) was used as a negative control. Experiments were performed in duplicate and the error bars denote ± SD, n = 2. (b) Kinetics of fab G7 binding to PSCA-Fc, as measured by Blitz. (c) Fab G7 binding to PSCA positive (PC-3-PSCA, Du-145-PSCA and HT1376 cells) and PSCA negative cells (PC-3, Du-145 and CHO-K1 cells) as tested by flow cytometry. An irrelevant fab (anti-SARS-CoV-2 fab ab1) was used as the isotype control. Fab G7 at the concentration of 500 nM was incubated with cells. (d-g) competition of fab G7 and fab F12 binding to HT1376 cell surface-associated PSCA by the recombinant PSCA-Fc protein (d and f) and by the murine PSCA antibody 7F5 (e and g). 500 nM of fab G7 or 200 nM of F12 was incubated with cells in the presence of gradient concentration of competitors. The bound fab G7 or F12 was detected by the pe-conjugated anti-flag tag antibody.

    Journal: mAbs

    Article Title: Discovery of a novel highly specific, fully human PSCA antibody and its application as an antibody-drug conjugate in prostate cancer.

    doi: 10.1080/19420862.2024.2387240

    Figure Lengend Snippet: Figure 1. Discovery and characterization of the PSCA antibody fab G7.(a) fab G7 binding to recombinant PSCA-Fc protein measured by ELISA. Bovine serum albumin (BSA) was used as a negative control. Experiments were performed in duplicate and the error bars denote ± SD, n = 2. (b) Kinetics of fab G7 binding to PSCA-Fc, as measured by Blitz. (c) Fab G7 binding to PSCA positive (PC-3-PSCA, Du-145-PSCA and HT1376 cells) and PSCA negative cells (PC-3, Du-145 and CHO-K1 cells) as tested by flow cytometry. An irrelevant fab (anti-SARS-CoV-2 fab ab1) was used as the isotype control. Fab G7 at the concentration of 500 nM was incubated with cells. (d-g) competition of fab G7 and fab F12 binding to HT1376 cell surface-associated PSCA by the recombinant PSCA-Fc protein (d and f) and by the murine PSCA antibody 7F5 (e and g). 500 nM of fab G7 or 200 nM of F12 was incubated with cells in the presence of gradient concentration of competitors. The bound fab G7 or F12 was detected by the pe-conjugated anti-flag tag antibody.

    Article Snippet: The prostate cancer cell lines PC-3 and Du-145 and the bladder cancer cell-line HT1376 were purchased from the American Type Culture Collection (ATCC).

    Techniques: Binding Assay, Recombinant, Enzyme-linked Immunosorbent Assay, Negative Control, Flow Cytometry, Control, Concentration Assay, Incubation, FLAG-tag