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skmes1  (ATCC)


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    ATCC skmes1
    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 <t>(SKMES1,</t> 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 .
    Skmes1, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 648 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/skmes1/pmc13130687-92-0-2?v=ATCC
    Average 96 stars, based on 648 article reviews
    skmes1 - by Bioz Stars, 2026-07
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    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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    skmes1  (ATCC)
    96
    ATCC skmes1
    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 <t>(SKMES1,</t> 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 .
    Skmes1, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Korean Cell Line Bank skmes1 lusc cells
    Dapl1 mRNA in <t>LUSC</t> is highly expressed ( A ) Three out of our four LUSC patients were upregulated in Dapl1 expression compared with adjacent normal (FPKM = fragments per kilobase per million reads). ( B ) Five LUAD have not detected or very low levels of Dapl1 expression in RNA-seq data. ( C ) Twenty-one Human LUSC and ( D ) twenty-one Human LUAD tissues were analyzed to determine Dapl1 expression level by PCR. Dapl1 was upregulated in 11 LUSC (52%), while no expression was observed in LUAD. ( E ) Expression levels of Dapl1 in TCGA (Cancer tissue and nearby normal tissue from the same patient) database, Dapl1 were upregulated in 36 among 51 LUSC (70.6%, mean RSEM 1142), but ( F ) Dapl1 was upregulated in 3 among 57 LUAD (5%, mean RSEM 13), RSEM (RNA-Seq by Expectation–Maximization) reports transcripts per million mapped reads (TPM). ( G ) Graph comparing Dapl1 expression in normal tissue and LUSC, and normal tissue and LUAD from GEPIA2 (GEPIA 2). ( H ) Colony formation assays were done by seeding HCC95 cells (1,000 cells/well) ( H-1 ) Graphing HCC95 colony formation assay results using Clono-counter, and ( I ) <t>SKMES1</t> cells (1,000 cells/well) on 6 well plates. Dapl1 knockdown by siRNA dramatically reduced the colony formation. ( J ) Kaplan–Meier survival curve shows that the higher the Dapl1 expression, the worse the prognosis of lung cancer. Data was drawn from https://kmplot.com
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    ATCC skmes1 human nsclc cell line

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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, 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: SKMES1 , ATCC , HTB-58; RRID: CVCL_0630.

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

    Dapl1 mRNA in LUSC is highly expressed ( A ) Three out of our four LUSC patients were upregulated in Dapl1 expression compared with adjacent normal (FPKM = fragments per kilobase per million reads). ( B ) Five LUAD have not detected or very low levels of Dapl1 expression in RNA-seq data. ( C ) Twenty-one Human LUSC and ( D ) twenty-one Human LUAD tissues were analyzed to determine Dapl1 expression level by PCR. Dapl1 was upregulated in 11 LUSC (52%), while no expression was observed in LUAD. ( E ) Expression levels of Dapl1 in TCGA (Cancer tissue and nearby normal tissue from the same patient) database, Dapl1 were upregulated in 36 among 51 LUSC (70.6%, mean RSEM 1142), but ( F ) Dapl1 was upregulated in 3 among 57 LUAD (5%, mean RSEM 13), RSEM (RNA-Seq by Expectation–Maximization) reports transcripts per million mapped reads (TPM). ( G ) Graph comparing Dapl1 expression in normal tissue and LUSC, and normal tissue and LUAD from GEPIA2 (GEPIA 2). ( H ) Colony formation assays were done by seeding HCC95 cells (1,000 cells/well) ( H-1 ) Graphing HCC95 colony formation assay results using Clono-counter, and ( I ) SKMES1 cells (1,000 cells/well) on 6 well plates. Dapl1 knockdown by siRNA dramatically reduced the colony formation. ( J ) Kaplan–Meier survival curve shows that the higher the Dapl1 expression, the worse the prognosis of lung cancer. Data was drawn from https://kmplot.com

    Journal: Journal of Molecular Medicine (Berlin, Germany)

    Article Title: DAPL1 is activated by Np63 and GRα and regulates lipid metabolism

    doi: 10.1007/s00109-025-02636-8

    Figure Lengend Snippet: Dapl1 mRNA in LUSC is highly expressed ( A ) Three out of our four LUSC patients were upregulated in Dapl1 expression compared with adjacent normal (FPKM = fragments per kilobase per million reads). ( B ) Five LUAD have not detected or very low levels of Dapl1 expression in RNA-seq data. ( C ) Twenty-one Human LUSC and ( D ) twenty-one Human LUAD tissues were analyzed to determine Dapl1 expression level by PCR. Dapl1 was upregulated in 11 LUSC (52%), while no expression was observed in LUAD. ( E ) Expression levels of Dapl1 in TCGA (Cancer tissue and nearby normal tissue from the same patient) database, Dapl1 were upregulated in 36 among 51 LUSC (70.6%, mean RSEM 1142), but ( F ) Dapl1 was upregulated in 3 among 57 LUAD (5%, mean RSEM 13), RSEM (RNA-Seq by Expectation–Maximization) reports transcripts per million mapped reads (TPM). ( G ) Graph comparing Dapl1 expression in normal tissue and LUSC, and normal tissue and LUAD from GEPIA2 (GEPIA 2). ( H ) Colony formation assays were done by seeding HCC95 cells (1,000 cells/well) ( H-1 ) Graphing HCC95 colony formation assay results using Clono-counter, and ( I ) SKMES1 cells (1,000 cells/well) on 6 well plates. Dapl1 knockdown by siRNA dramatically reduced the colony formation. ( J ) Kaplan–Meier survival curve shows that the higher the Dapl1 expression, the worse the prognosis of lung cancer. Data was drawn from https://kmplot.com

    Article Snippet: HCC95 and SKMES1 LUSC cells were purchased from Korean Cell Line Bank (KCLB, cellbank.snu.ac.kr, Seoul Korea).

    Techniques: Expressing, RNA Sequencing, Colony Assay, Knockdown

    Np63, GRα monomer are the transcription factors of DAPL1 and Dapl1 is increased in hypoxia depending on the situation. ( A ) When transcription factor Np63 was knocked out in MG-U74B skin cells, Dapl1 disappeared. (GDS1435/109381,109382, GEO Profiles, NCBI). ( B )( C ) Dapl1, Np63 expression in RNA-seq data of our 4 LUSC patients (cancer tissue and around normal tissue). ( D ) Among lung cancer cell lines, Np63, a transcription factor, was confirmed to be expressed in HCC95, which expresses Dapl1. (L132: Human cervix carcinoma. Originally derived from a human embryonic lung). ( E )( F ) When Transfecting the HCC95 cell with Np63siRNA, the expression of Np63, Dapl1 mRNA is identified by RT-PCR. ( G ) Estimated Np63 binding site in the DAPL1 promoter region based on a recent paper . ( H ) When osteosarcoma cells were transfected with GRα, GRα A, B, C, and D, Dapl1 increased in GRα, GRα A, B, and C over time, but did not increase in D (ID 56855360, GEO Profiles, NCBI). ( I ) The typical GRα dimer binding sequence and the monomer binding site at positions −797 to −810 bp of the DAPL1 promoter, for mutation experiments, mutate TGAA, ACGT. ( J ) Luciferase assay results, empty vector vs DAPL1 promoter vector, ( K ) DAPL1 promoter vector vs mutant vector, ( L ) DAPL1 promoter vector vs mutant vector-Dexamethasone 1uM, 3uM addition. ( M1,2 ) HCC95 and ( M3 , 4 ) HEK293T cells plated in 6 wells were grown under hypoxia conditions (N 2 94%, CO 2 5%, O 2 1%) incubator (Whitley H35 hypoxystation), after 18 h, 24 h, 70 h, it is compared with the control group grown under normal conditions by RT-PCR

    Journal: Journal of Molecular Medicine (Berlin, Germany)

    Article Title: DAPL1 is activated by Np63 and GRα and regulates lipid metabolism

    doi: 10.1007/s00109-025-02636-8

    Figure Lengend Snippet: Np63, GRα monomer are the transcription factors of DAPL1 and Dapl1 is increased in hypoxia depending on the situation. ( A ) When transcription factor Np63 was knocked out in MG-U74B skin cells, Dapl1 disappeared. (GDS1435/109381,109382, GEO Profiles, NCBI). ( B )( C ) Dapl1, Np63 expression in RNA-seq data of our 4 LUSC patients (cancer tissue and around normal tissue). ( D ) Among lung cancer cell lines, Np63, a transcription factor, was confirmed to be expressed in HCC95, which expresses Dapl1. (L132: Human cervix carcinoma. Originally derived from a human embryonic lung). ( E )( F ) When Transfecting the HCC95 cell with Np63siRNA, the expression of Np63, Dapl1 mRNA is identified by RT-PCR. ( G ) Estimated Np63 binding site in the DAPL1 promoter region based on a recent paper . ( H ) When osteosarcoma cells were transfected with GRα, GRα A, B, C, and D, Dapl1 increased in GRα, GRα A, B, and C over time, but did not increase in D (ID 56855360, GEO Profiles, NCBI). ( I ) The typical GRα dimer binding sequence and the monomer binding site at positions −797 to −810 bp of the DAPL1 promoter, for mutation experiments, mutate TGAA, ACGT. ( J ) Luciferase assay results, empty vector vs DAPL1 promoter vector, ( K ) DAPL1 promoter vector vs mutant vector, ( L ) DAPL1 promoter vector vs mutant vector-Dexamethasone 1uM, 3uM addition. ( M1,2 ) HCC95 and ( M3 , 4 ) HEK293T cells plated in 6 wells were grown under hypoxia conditions (N 2 94%, CO 2 5%, O 2 1%) incubator (Whitley H35 hypoxystation), after 18 h, 24 h, 70 h, it is compared with the control group grown under normal conditions by RT-PCR

    Article Snippet: HCC95 and SKMES1 LUSC cells were purchased from Korean Cell Line Bank (KCLB, cellbank.snu.ac.kr, Seoul Korea).

    Techniques: Expressing, RNA Sequencing, Derivative Assay, Reverse Transcription Polymerase Chain Reaction, Binding Assay, Transfection, Sequencing, Mutagenesis, Luciferase, Plasmid Preparation, Control

    DAPL1 changes lipid synthesis enzymes. ( A ) Lipid synthesis pathways related to Fdft1, Pcyt1a, Sptlc1 genes. ( B ) Among the 10 genes, expression comparison of the finally selected Fdft1, Pcyt1a, and Sptlc1 genes in normal and adjacent cancer tissues of four LUSC patients. ( C ) When Dapl1 was overexpressed in HEK293T cells, changes in Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( D ) When Dapl1 was knockdown in HCC95 cells, changes in Dapl1, Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( E ) Schematic diagram of DAPL1 knockout using CRISPER-Cas9 system. 127 bp is deleted between exon2 and intron. The distance between two primers is 406 bp. Figure of genotyping results of generated mice. ( F ) In the kidney tissue of the DAPL1 KO male mouse, Dapl1, Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( G ) In 4 WT, 4 DAPL1 KO female mice’s eyes (high DAPL1 expression), Dapl1, Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( H ) In 3 WT, 3 DAPL1 KO female mice’s large intestines (no DAPL1 expression), Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( I ) After LC/MS analysis of 297 types of lipids in the eyes of male mice 3 WT and 3 DAPL1 KO, the principal component analysis (PCA) plot confirms the division into two groups. ( J ) In Partial least squares-discriminant analysis (PLS-DA), a supervised learning model, it was confirmed that the two groups were clearly divided. ( K ) From the importance scores, lipids of the TG class appeared to act as a major factor in model training. ( L ) In the Volcano plot, 18 types of TG & 2 types of DG have up-regulated (tendency shown in lipid class), TG 53:3, FA 20:4, LPE 18:0, PS 40:6, PS 34:1, PI 38:4, SM 44:2, Cer 40:2, LPC 18:0 were down-regulated (No tendency in lipid class) fold change > 1.5, -log(p) > 1.0. ( M ) In Heatmap analysis, an overall difference between the blue (Ho) and green (WT) groups could be confirmed

    Journal: Journal of Molecular Medicine (Berlin, Germany)

    Article Title: DAPL1 is activated by Np63 and GRα and regulates lipid metabolism

    doi: 10.1007/s00109-025-02636-8

    Figure Lengend Snippet: DAPL1 changes lipid synthesis enzymes. ( A ) Lipid synthesis pathways related to Fdft1, Pcyt1a, Sptlc1 genes. ( B ) Among the 10 genes, expression comparison of the finally selected Fdft1, Pcyt1a, and Sptlc1 genes in normal and adjacent cancer tissues of four LUSC patients. ( C ) When Dapl1 was overexpressed in HEK293T cells, changes in Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( D ) When Dapl1 was knockdown in HCC95 cells, changes in Dapl1, Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( E ) Schematic diagram of DAPL1 knockout using CRISPER-Cas9 system. 127 bp is deleted between exon2 and intron. The distance between two primers is 406 bp. Figure of genotyping results of generated mice. ( F ) In the kidney tissue of the DAPL1 KO male mouse, Dapl1, Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( G ) In 4 WT, 4 DAPL1 KO female mice’s eyes (high DAPL1 expression), Dapl1, Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( H ) In 3 WT, 3 DAPL1 KO female mice’s large intestines (no DAPL1 expression), Fdft1, Pcyt1a, and Sptlc1 mRNA were confirmed by RT-PCR. ( I ) After LC/MS analysis of 297 types of lipids in the eyes of male mice 3 WT and 3 DAPL1 KO, the principal component analysis (PCA) plot confirms the division into two groups. ( J ) In Partial least squares-discriminant analysis (PLS-DA), a supervised learning model, it was confirmed that the two groups were clearly divided. ( K ) From the importance scores, lipids of the TG class appeared to act as a major factor in model training. ( L ) In the Volcano plot, 18 types of TG & 2 types of DG have up-regulated (tendency shown in lipid class), TG 53:3, FA 20:4, LPE 18:0, PS 40:6, PS 34:1, PI 38:4, SM 44:2, Cer 40:2, LPC 18:0 were down-regulated (No tendency in lipid class) fold change > 1.5, -log(p) > 1.0. ( M ) In Heatmap analysis, an overall difference between the blue (Ho) and green (WT) groups could be confirmed

    Article Snippet: HCC95 and SKMES1 LUSC cells were purchased from Korean Cell Line Bank (KCLB, cellbank.snu.ac.kr, Seoul Korea).

    Techniques: Expressing, Comparison, Reverse Transcription Polymerase Chain Reaction, Knockdown, Knock-Out, Generated, Liquid Chromatography with Mass Spectroscopy

    Journal: Cell reports

    Article Title: TGF-β1-mediated intercellular signaling fuels cooperative cellular invasion

    doi: 10.1016/j.celrep.2025.115315

    Figure Lengend Snippet:

    Article Snippet: Similarly, the SKMES1 human NSCLC cell line was also obtained from ATCC, cultured in EMEM medium supplemented with 10% FBS and 1% P/S, and incubated at 37 ◦ C and 5% CO 2 .

    Techniques: Recombinant, Reverse Transcription, Bicinchoninic Acid Protein Assay, Staining, RNA Sequencing