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mda231  (ATCC)


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    Structured Review

    ATCC mda231
    Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, <t>MDA231,</t> and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .
    Mda231, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 28313 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mda231/product/ATCC
    Average 99 stars, based on 28313 article reviews
    mda231 - by Bioz Stars, 2026-05
    99/100 stars

    Images

    1) Product Images from "Early-stage multi-cancer detection through a plasma extracellular vesicle protein signature"

    Article Title: Early-stage multi-cancer detection through a plasma extracellular vesicle protein signature

    Journal: Cell Reports Medicine

    doi: 10.1016/j.xcrm.2026.102694

    Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, MDA231, and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .
    Figure Legend Snippet: Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, MDA231, and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .

    Techniques Used: Transformation Assay, Derivative Assay, Isolation, Transmission Assay, Electron Microscopy, Tunable Resistive Pulse Sensing, Western Blot, Marker, Mass Spectrometry, Enzyme-linked Immunosorbent Assay, Expressing



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    Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, <t>MDA231,</t> and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .
    Mda231, 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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    Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, <t>MDA231,</t> and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .
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    Migration assays were performed using the Boyden chamber method. After transfection of each siRNA into the (A) A549 and (B) <t>MDA231</t> cells, the cells were incubated for 48 h before the migration assay. The cells that had migrated to the outer side of the membranes within 24 h were fixed and stained. A representative image of a triplicate analysis of each siRNA is shown. Scale bar, 20 µm. siRNA, small interfering RNA; Ctrl, control siRNA; SERF2, small EDRK-rich factor 2; PRKDC, DNA-dependent protein kinase catalytic subunit; S100A6, S100 calcium-binding protein A6; SH3GLB1, SH3-domain GRB2-like endophilin B1; CAPNS1, calpain, small subunit 1; PSMB4, proteasome subunit β type-4; RPL11, ribosomal protein L11; RPS7, ribosomal protein S7.
    Mda231 Breast 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
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    Image Search Results


    Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, MDA231, and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .

    Journal: Cell Reports Medicine

    Article Title: Early-stage multi-cancer detection through a plasma extracellular vesicle protein signature

    doi: 10.1016/j.xcrm.2026.102694

    Figure Lengend Snippet: Transformation-induced changes to the protein composition of cell-derived sEVs (A) The morphology of isolated sEVs was assessed using transmission electron microscopy. Images of normal and transformed HBEC-derived sEVs (scale bars, 200 nm). (B) Nanoparticle analysis using tunable resistive pulse sensing of sEVs isolated from HBECs demonstrates that the majority of sEVs have a size range between 30 and 150 nm, and that transformation does not result in an increase in sEV secretion. (C) Western blot of sEVs from HBECs demonstrating the presence of sEV proteins HSP70 and CD63 and the absence of the cell marker calnexin. (D) Label-free mass spectrometry identified 148 proteins with greater abundance in sEVs derived from transformed HBECs (FDR <0.02), of which 15 were annotated as extracellular proteins. (E) Mass spectrometry results were confirmed using ELISA for THBS1, NID1, PTX3, and VCAN in sEVs derived from normal and transformed HBECs. (F) sEVs derived from 22 cancer cell lines including NSCLC (SKMES1, H1650, HCC4006, and H2170), glioblastoma ([GBM], D54, D270, U87, and U118), colorectal cancer ([CRC], HT29 and SW620), breast cancer ([BCa], BT549, MDA231, and MDA436), prostate cancer ([PCa], PC3 and LNCaP), melanoma ([MEL], A375, MAMEL65, and SKMEL28), esophageal cancer ([ECa], OE19), and ovarian cancer ([OVA], A2780, CAOV3, IGROV1, and OVCAR8) showed a clear increase in expression of THBS1, NID1, PTX3, and VCAN in relation to the average levels of sEVs from normal cells ([HBEC] 30KT, HOSE 6.3, and HOSE 17.1). Samples in mass spectrometry and ELISA were measured in triplicate. See also and .

    Article Snippet: MDA231 , ATCC , HTB-26; RRID: CVCL_0062.

    Techniques: Transformation Assay, Derivative Assay, Isolation, Transmission Assay, Electron Microscopy, Tunable Resistive Pulse Sensing, Western Blot, Marker, Mass Spectrometry, Enzyme-linked Immunosorbent Assay, Expressing

    Migration assays were performed using the Boyden chamber method. After transfection of each siRNA into the (A) A549 and (B) MDA231 cells, the cells were incubated for 48 h before the migration assay. The cells that had migrated to the outer side of the membranes within 24 h were fixed and stained. A representative image of a triplicate analysis of each siRNA is shown. Scale bar, 20 µm. siRNA, small interfering RNA; Ctrl, control siRNA; SERF2, small EDRK-rich factor 2; PRKDC, DNA-dependent protein kinase catalytic subunit; S100A6, S100 calcium-binding protein A6; SH3GLB1, SH3-domain GRB2-like endophilin B1; CAPNS1, calpain, small subunit 1; PSMB4, proteasome subunit β type-4; RPL11, ribosomal protein L11; RPS7, ribosomal protein S7.

    Journal: Oncology Reports

    Article Title: Exploration of genes related to the development of cancer of unknown primary

    doi: 10.3892/or.2025.8905

    Figure Lengend Snippet: Migration assays were performed using the Boyden chamber method. After transfection of each siRNA into the (A) A549 and (B) MDA231 cells, the cells were incubated for 48 h before the migration assay. The cells that had migrated to the outer side of the membranes within 24 h were fixed and stained. A representative image of a triplicate analysis of each siRNA is shown. Scale bar, 20 µm. siRNA, small interfering RNA; Ctrl, control siRNA; SERF2, small EDRK-rich factor 2; PRKDC, DNA-dependent protein kinase catalytic subunit; S100A6, S100 calcium-binding protein A6; SH3GLB1, SH3-domain GRB2-like endophilin B1; CAPNS1, calpain, small subunit 1; PSMB4, proteasome subunit β type-4; RPL11, ribosomal protein L11; RPS7, ribosomal protein S7.

    Article Snippet: The A549 human lung cancer cell line (cat. no. CCL-185) and the MDA231 breast cancer cell line (cat. no. HTB-26) were procured from American Type Culture Collection, and cultured in DMEM (Thermo Fisher Scientific, Inc.) with 10% FBS (MilliporeSigma) in accordance with the instructions provided by the suppliers.

    Techniques: Migration, Transfection, Incubation, Staining, Small Interfering RNA, Control, Binding Assay

    Western blotting showing the reduction in protein expression following siRNA-induced knockdown of PRKDC and PSMB4. (Top) Protein expression was reduced after transfection of the cells with siRNA for PRKDC (left) and PSMB4 (right) in both the A549 and MDA231 cells. β-actin was used as the loading control, whereas si-NC was used as the negative control. (Bottom) Relative reductions in PRKDC or PSMB4 protein expression were determined using western blot analysis conducted in triplicate. Data are presented as the mean and standard deviation. *P<0.05; **P<0.01. siRNA/si, small interfering RNA; si-NC, siRNA universal negative control; PRKDC, DNA-dependent protein kinase catalytic subunit; PSMB4, proteasome subunit β type-4.

    Journal: Oncology Reports

    Article Title: Exploration of genes related to the development of cancer of unknown primary

    doi: 10.3892/or.2025.8905

    Figure Lengend Snippet: Western blotting showing the reduction in protein expression following siRNA-induced knockdown of PRKDC and PSMB4. (Top) Protein expression was reduced after transfection of the cells with siRNA for PRKDC (left) and PSMB4 (right) in both the A549 and MDA231 cells. β-actin was used as the loading control, whereas si-NC was used as the negative control. (Bottom) Relative reductions in PRKDC or PSMB4 protein expression were determined using western blot analysis conducted in triplicate. Data are presented as the mean and standard deviation. *P<0.05; **P<0.01. siRNA/si, small interfering RNA; si-NC, siRNA universal negative control; PRKDC, DNA-dependent protein kinase catalytic subunit; PSMB4, proteasome subunit β type-4.

    Article Snippet: The A549 human lung cancer cell line (cat. no. CCL-185) and the MDA231 breast cancer cell line (cat. no. HTB-26) were procured from American Type Culture Collection, and cultured in DMEM (Thermo Fisher Scientific, Inc.) with 10% FBS (MilliporeSigma) in accordance with the instructions provided by the suppliers.

    Techniques: Western Blot, Expressing, Knockdown, Transfection, Control, Negative Control, Standard Deviation, Small Interfering RNA