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ATCC human pancreatic cancer cell lines panc 1

Verification of protein tyrosine phosphatase kappa (PTPRK) knockdown in pancreatic cancer cell lines. (A) QPCR results show the PTPRK expression in control cell <t>line</t> <t>PANC-1</t> pEF and PTPRK knockdown cell line PANC-1 PTPRK kd . (B) PTPRK expression in CFPAC-1 pEF and CFPAC-1 PTPRK kd cell lines. (C) Western blot results show the PTPRK protein expression in both PANC-1 and CFPAC-1 cell lines with PTPRK nockdown. * p <0.05, ** p <0.01, *** p <0.001.

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1) Product Images from "Elevated Protein Tyrosine Phosphatase Kappa Expression Is Associated With Disease Progression and Poor Prognosis of Pancreatic Cancer"

Article Title: Elevated Protein Tyrosine Phosphatase Kappa Expression Is Associated With Disease Progression and Poor Prognosis of Pancreatic Cancer

Journal: Cancer Diagnosis & Prognosis

doi: 10.21873/cdp.10560

Figure Legend Snippet: Verification of protein tyrosine phosphatase kappa (PTPRK) knockdown in pancreatic cancer cell lines. (A) QPCR results show the PTPRK expression in control cell line PANC-1 pEF and PTPRK knockdown cell line PANC-1 PTPRK kd . (B) PTPRK expression in CFPAC-1 pEF and CFPAC-1 PTPRK kd cell lines. (C) Western blot results show the PTPRK protein expression in both PANC-1 and CFPAC-1 cell lines with PTPRK nockdown. * p <0.05, ** p <0.01, *** p <0.001.

Techniques Used: Knockdown, Expressing, Control, Western Blot

Protein tyrosine phosphatase kappa (PTPRK) and cell proliferation. (A, B) A proliferation was performed to examine whether PTPRK is associated with pancreatic cell proliferation. (C, D) QPCR results show the expression of CDK6 and CCND1 in control cell lines PANC-1 pEF /CFPAC-1 pEF and PTPRK knockdown cell lines PANC-1 PTPRK kd /CFPAC-1 PTPRK kd . (E) TCGA dataset is used to draw a scatter plot showing the association between CDK6 and PTPRK at transcripts level. (F) In the TCGA dataset, the association between CCND1 and PTPRK transcript levels is shown. * p <0.05, ** p <0.01, *** p <0.001.

Figure Legend Snippet: Protein tyrosine phosphatase kappa (PTPRK) and cell proliferation. (A, B) A proliferation was performed to examine whether PTPRK is associated with pancreatic cell proliferation. (C, D) QPCR results show the expression of CDK6 and CCND1 in control cell lines PANC-1 pEF /CFPAC-1 pEF and PTPRK knockdown cell lines PANC-1 PTPRK kd /CFPAC-1 PTPRK kd . (E) TCGA dataset is used to draw a scatter plot showing the association between CDK6 and PTPRK at transcripts level. (F) In the TCGA dataset, the association between CCND1 and PTPRK transcript levels is shown. * p <0.05, ** p <0.01, *** p <0.001.

Techniques Used: Expressing, Control, Knockdown

Response to cyclin-dependent kinase 6 (CDK6) inhibitors in the protein tyrosine phosphatase kappa (PTPRK) knockdown pancreatic cancer cell line models. Both CFPAC-1 and PANC-1 cell lines were treated with different concentration of the CDK6 inhibitor BSJ-03-123 (A and B), CDK4/6 inhibitor Palbociclib (C and D) and CDK4 inhibitor 3-ATA (E and F). Corresponding IC 50 test results are shown. Cell viability was determined following a 3-day treatment with the inhibitors. * p <0.05, ** p <0.01, *** p <0.001.

Figure Legend Snippet: Response to cyclin-dependent kinase 6 (CDK6) inhibitors in the protein tyrosine phosphatase kappa (PTPRK) knockdown pancreatic cancer cell line models. Both CFPAC-1 and PANC-1 cell lines were treated with different concentration of the CDK6 inhibitor BSJ-03-123 (A and B), CDK4/6 inhibitor Palbociclib (C and D) and CDK4 inhibitor 3-ATA (E and F). Corresponding IC 50 test results are shown. Cell viability was determined following a 3-day treatment with the inhibitors. * p <0.05, ** p <0.01, *** p <0.001.

Techniques Used: Knockdown, Concentration Assay

Protein tyrosine phosphatase kappa (PTPRK) and lymph node metastasis. (A) The scatter plot shows that the lymph angiogenesis marker VEGFC is inversely correlated with PTPRK in the TCGA cohort. QPCR shows the expression of VEGFC in pancreatic cancer cell lines PANC-1 (B) and CFPAC-1 (C) with PTPRK knockdown. * p <0.05, ** p <0.01, *** p <0.001.

Figure Legend Snippet: Protein tyrosine phosphatase kappa (PTPRK) and lymph node metastasis. (A) The scatter plot shows that the lymph angiogenesis marker VEGFC is inversely correlated with PTPRK in the TCGA cohort. QPCR shows the expression of VEGFC in pancreatic cancer cell lines PANC-1 (B) and CFPAC-1 (C) with PTPRK knockdown. * p <0.05, ** p <0.01, *** p <0.001.

Techniques Used: Marker, Expressing, Knockdown

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Journal: Cancer Diagnosis & Prognosis

Article Title: Elevated Protein Tyrosine Phosphatase Kappa Expression Is Associated With Disease Progression and Poor Prognosis of Pancreatic Cancer

doi: 10.21873/cdp.10560

Figure Lengend Snippet: Verification of protein tyrosine phosphatase kappa (PTPRK) knockdown in pancreatic cancer cell lines. (A) QPCR results show the PTPRK expression in control cell line PANC-1 pEF and PTPRK knockdown cell line PANC-1 PTPRK kd . (B) PTPRK expression in CFPAC-1 pEF and CFPAC-1 PTPRK kd cell lines. (C) Western blot results show the PTPRK protein expression in both PANC-1 and CFPAC-1 cell lines with PTPRK nockdown. * p <0.05, ** p <0.01, *** p <0.001.

Article Snippet: Human pancreatic cancer cell lines PANC-1 and CFPAC-1 were purchased from ATCC (American Type Culture Collection, Manassas, VA, USA).

Techniques: Knockdown, Expressing, Control, Western Blot

Journal: Cancer Diagnosis & Prognosis

Article Title: Elevated Protein Tyrosine Phosphatase Kappa Expression Is Associated With Disease Progression and Poor Prognosis of Pancreatic Cancer

doi: 10.21873/cdp.10560

Figure Lengend Snippet: Protein tyrosine phosphatase kappa (PTPRK) and cell proliferation. (A, B) A proliferation was performed to examine whether PTPRK is associated with pancreatic cell proliferation. (C, D) QPCR results show the expression of CDK6 and CCND1 in control cell lines PANC-1 pEF /CFPAC-1 pEF and PTPRK knockdown cell lines PANC-1 PTPRK kd /CFPAC-1 PTPRK kd . (E) TCGA dataset is used to draw a scatter plot showing the association between CDK6 and PTPRK at transcripts level. (F) In the TCGA dataset, the association between CCND1 and PTPRK transcript levels is shown. * p <0.05, ** p <0.01, *** p <0.001.

Article Snippet: Human pancreatic cancer cell lines PANC-1 and CFPAC-1 were purchased from ATCC (American Type Culture Collection, Manassas, VA, USA).

Techniques: Expressing, Control, Knockdown

Journal: Cancer Diagnosis & Prognosis

Article Title: Elevated Protein Tyrosine Phosphatase Kappa Expression Is Associated With Disease Progression and Poor Prognosis of Pancreatic Cancer

doi: 10.21873/cdp.10560

Figure Lengend Snippet: Response to cyclin-dependent kinase 6 (CDK6) inhibitors in the protein tyrosine phosphatase kappa (PTPRK) knockdown pancreatic cancer cell line models. Both CFPAC-1 and PANC-1 cell lines were treated with different concentration of the CDK6 inhibitor BSJ-03-123 (A and B), CDK4/6 inhibitor Palbociclib (C and D) and CDK4 inhibitor 3-ATA (E and F). Corresponding IC 50 test results are shown. Cell viability was determined following a 3-day treatment with the inhibitors. * p <0.05, ** p <0.01, *** p <0.001.

Article Snippet: Human pancreatic cancer cell lines PANC-1 and CFPAC-1 were purchased from ATCC (American Type Culture Collection, Manassas, VA, USA).

Techniques: Knockdown, Concentration Assay

Journal: Cancer Diagnosis & Prognosis

Article Title: Elevated Protein Tyrosine Phosphatase Kappa Expression Is Associated With Disease Progression and Poor Prognosis of Pancreatic Cancer

doi: 10.21873/cdp.10560

Figure Lengend Snippet: Protein tyrosine phosphatase kappa (PTPRK) and lymph node metastasis. (A) The scatter plot shows that the lymph angiogenesis marker VEGFC is inversely correlated with PTPRK in the TCGA cohort. QPCR shows the expression of VEGFC in pancreatic cancer cell lines PANC-1 (B) and CFPAC-1 (C) with PTPRK knockdown. * p <0.05, ** p <0.01, *** p <0.001.

Article Snippet: Human pancreatic cancer cell lines PANC-1 and CFPAC-1 were purchased from ATCC (American Type Culture Collection, Manassas, VA, USA).

Techniques: Marker, Expressing, Knockdown

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: Knockdown of C16orf87 causes minor changes in the host cell protein profile. ( A ) Alignment of human ( Homo sapiens , UniProtKB accession number Q6PH81 ), mouse ( Mus musculus , UniProtKB accession number Q9CR55 ), and zebrafish ( Danio rerio , UniProtKB accession number Q6DGQ4 ) C16orf87 amino acid sequences. Alignment mismatches are indicated in gray boxes. The underlined sequence represents a possible minimal Akt/PKB kinase consensus recognition motif. A Ser91(S91) phosphorylation site is marked with an asterisk. ( B ) Per-residue confidence (pLDDT) coloring of the top-ranked predicted model of C16orf87. In the inset, the predicted zinc-ribbon domain is shown with the zinc-interacting cysteines (Cys16, Cys19, Cys30, and Cys32) indicated around the zinc ion (Zn 2+ ). The position of the phosphorylated serine (Ser91), a putative alpha-helix between amino acid residues Ser-107 and Ala-126, and the confidently predicted C-terminal alpha-helix between amino acid residues Asp-130 and Ile-153 are also highlighted. The ipTM and pTM values are annotated. N, N-terminus; C, C-terminus. Figure was rendered using ChimeraX (version 1.8, https://www.rbvi.ucsf.edu/chimerax ) ( C ) Western blot (WB) analysis of C16orf87 siRNA (siC16) knockdown in Panc-01, MiaPaCa-2, and C2C12 cell lines. A non-specific, scrambled siRNA (siScr) was used as a control; the WB membrane was probed with the antibodies against C16orf87 and actin. MS-based proteomics analysis of siRNA-treated C2C12 ( D ), MiaPaCa-2 ( E ), and Panc-01 ( F ) cells. Data points corresponding to histones are colored in pink, and statistically significant ( P < 0.05, fold-change > 1) proteins are colored in yellow (mouse cell line C2C12) and green (human cell lines, Panc-01 and MiaPaCa-2).

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: Knockdown, Sequencing, Phospho-proteomics, Residue, Western Blot, Control, Membrane

CRISPR-Cas9 knockout of C16orf87 does not affect Panc-01 cell viability. ( A ) Whole-cell lysates of Panc-01 KO and Panc-01 WT cells were analyzed by western blot (WB), and proteins were detected with the antibodies against C16orf87 and actin. An asterisk indicates the migration of the C16orf87 protein. Mw; molecular weight marker. ( B ) MS-based proteomics analysis of Panc-01 KO and Panc-01 WT cell lysates (FDR ≤ 0.05, n = 3). Data points representing histones and proteins of interest are highlighted in red. ( C ) Panc-01 KO and Panc-01 WT cell viability was analyzed by FACS after AnnexinV-FITC (AnnV) and DRAQ7 (Dq7) staining. ( D ) Panc-01 KO and Panc-01 WT cell proliferation was analyzed by FACS after EdU-A647 incorporation into cells. ( E ) Quantification of the FACS analysis ( P < 0.01 (**)).

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: CRISPR-Cas9 knockout of C16orf87 does not affect Panc-01 cell viability. ( A ) Whole-cell lysates of Panc-01 KO and Panc-01 WT cells were analyzed by western blot (WB), and proteins were detected with the antibodies against C16orf87 and actin. An asterisk indicates the migration of the C16orf87 protein. Mw; molecular weight marker. ( B ) MS-based proteomics analysis of Panc-01 KO and Panc-01 WT cell lysates (FDR ≤ 0.05, n = 3). Data points representing histones and proteins of interest are highlighted in red. ( C ) Panc-01 KO and Panc-01 WT cell viability was analyzed by FACS after AnnexinV-FITC (AnnV) and DRAQ7 (Dq7) staining. ( D ) Panc-01 KO and Panc-01 WT cell proliferation was analyzed by FACS after EdU-A647 incorporation into cells. ( E ) Quantification of the FACS analysis ( P < 0.01 (**)).

Techniques: CRISPR, Knock-Out, Western Blot, Migration, Molecular Weight, Marker, Staining

CRISPR-Cas9 knockout of C16orf87 reduces Panc-01 cell migration. ( A ) Microscopy images of the in vitro scratch assay in Panc-01 KO and Panc-01 WT cells. Images were taken at 0, 6, 12, and 24 h after scratches were applied. ( B ) The cell migration rate was calculated based on the extent of cell coverage within the scratched area ( P < 0.05 (*) and P < 0.01 (**)).

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: CRISPR-Cas9 knockout of C16orf87 reduces Panc-01 cell migration. ( A ) Microscopy images of the in vitro scratch assay in Panc-01 KO and Panc-01 WT cells. Images were taken at 0, 6, 12, and 24 h after scratches were applied. ( B ) The cell migration rate was calculated based on the extent of cell coverage within the scratched area ( P < 0.05 (*) and P < 0.01 (**)).

Techniques: CRISPR, Knock-Out, Migration, Microscopy, In Vitro, Wound Healing Assay

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.

Techniques: Protein-Protein interactions, Immunoprecipitation, Transfection, Isolation, Migration, In Vitro, Control, Purification

Lack of C16orf87 alters chromatin accessibility. ( A ) Distribution of the more accessible chromatin genomic features identified by ATAC-seq in Panc-01 WT and Panc-01 KO cells. The X-axis shows values in percentage. Gene locus diagrams showing genomic regions near the WWOX ( B ) and NCOA7-HINT3 ( C ) genes, with peaks representing ATAC-seq reads indicating chromatin accessibility. Data were aligned to available tracks (ChIP-Atlas) of HDAC1 , HDAC2 , MIER1 , MIER2 , MIER3 , and H3K27ac markers. Panc-01 WT and Panc-01 KO peaks are shown in blue and green, respectively, and significant differences (FDR threshold: 0.05) in read quantities (peaks), observed in genomic intervals, are shown in red bars on the third track (top to bottom). WWOX represents one of the genes with a higher peak on the Panc-01 WT compared to Panc-01 KO . NCOA7-HINT3 represents one of the genes with higher peaks on the Panc-01 KO . ( D ) qRT-PCR analysis of the NCOA7 , HINT3 , WWOX , and C16orf87 mRNA expression. Relative mRNA expression in Panc-01 WT and Panc-01 KO cells after normalization to 18S rRNA and considering mRNA levels in Panc-01 WT cells as 1.

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: Lack of C16orf87 alters chromatin accessibility. ( A ) Distribution of the more accessible chromatin genomic features identified by ATAC-seq in Panc-01 WT and Panc-01 KO cells. The X-axis shows values in percentage. Gene locus diagrams showing genomic regions near the WWOX ( B ) and NCOA7-HINT3 ( C ) genes, with peaks representing ATAC-seq reads indicating chromatin accessibility. Data were aligned to available tracks (ChIP-Atlas) of HDAC1 , HDAC2 , MIER1 , MIER2 , MIER3 , and H3K27ac markers. Panc-01 WT and Panc-01 KO peaks are shown in blue and green, respectively, and significant differences (FDR threshold: 0.05) in read quantities (peaks), observed in genomic intervals, are shown in red bars on the third track (top to bottom). WWOX represents one of the genes with a higher peak on the Panc-01 WT compared to Panc-01 KO . NCOA7-HINT3 represents one of the genes with higher peaks on the Panc-01 KO . ( D ) qRT-PCR analysis of the NCOA7 , HINT3 , WWOX , and C16orf87 mRNA expression. Relative mRNA expression in Panc-01 WT and Panc-01 KO cells after normalization to 18S rRNA and considering mRNA levels in Panc-01 WT cells as 1.

Techniques: Quantitative RT-PCR, Expressing

Expression of EN2 in human pancreatic cancer tissues. (A, B), Pancreatic Tissue Arrays containing normal and cancerous tissues were purchased from Biomax. EN2 expression was measured by IHC. Representative photographs of 60 pancreatic tissues from various stages of pancreatic cancer. Blue = nuclei, Brown/pink colour = EN2. * = significantly different from normal, p = < 0.01. (C) TCGA data on the expression of EN2 mRNA. * = significantly different from normal.

Journal: Journal of Cellular and Molecular Medicine

Article Title: EN2 Regulates Pancreatic Cancer Initiation, Progression, and Epithelial‐Mesenchymal Transition Through the Notch Signalling Pathway

doi: 10.1111/jcmm.71158

Figure Lengend Snippet: Expression of EN2 in human pancreatic cancer tissues. (A, B), Pancreatic Tissue Arrays containing normal and cancerous tissues were purchased from Biomax. EN2 expression was measured by IHC. Representative photographs of 60 pancreatic tissues from various stages of pancreatic cancer. Blue = nuclei, Brown/pink colour = EN2. * = significantly different from normal, p = < 0.01. (C) TCGA data on the expression of EN2 mRNA. * = significantly different from normal.

Article Snippet: Human pancreatic cancer cell lines (PANC‐1 and AsPC‐1) and human normal pancreatic ductal epithelial cells (HPNE) were purchased from the American Type Culture Collection (ATCC, Manassas, VA).

Techniques: Expressing

The expression of EN2 in HPNE, pancreatic cancer cell lines, and pancreatic CSCs. (A), Protein expression of EN2 in HPNE, pancreatic cancer cell lines, and pancreatic CSCs. Crude proteins were isolated, and EN2 expression was measured by Western blot analysis. β‐Actin was used as a loading control. (B), Expression of EN2 mRNA in HPNE, pancreatic cancer cell lines, and pancreatic CSCs. RNA was isolated, and EN2 expression was measured by q‐RT‐PCR. GAPDH was used as an internal control. Data represent mean ( n = 4) ± SD. *, # and % = significantly different from HPNE ( p < 0.05). (C), Expression of EN2. Immunocytochemistry was performed to examine EN2 expression in HPNE, PANC‐1, and AsPC‐1 cells.

Journal: Journal of Cellular and Molecular Medicine

Article Title: EN2 Regulates Pancreatic Cancer Initiation, Progression, and Epithelial‐Mesenchymal Transition Through the Notch Signalling Pathway

doi: 10.1111/jcmm.71158

Figure Lengend Snippet: The expression of EN2 in HPNE, pancreatic cancer cell lines, and pancreatic CSCs. (A), Protein expression of EN2 in HPNE, pancreatic cancer cell lines, and pancreatic CSCs. Crude proteins were isolated, and EN2 expression was measured by Western blot analysis. β‐Actin was used as a loading control. (B), Expression of EN2 mRNA in HPNE, pancreatic cancer cell lines, and pancreatic CSCs. RNA was isolated, and EN2 expression was measured by q‐RT‐PCR. GAPDH was used as an internal control. Data represent mean ( n = 4) ± SD. *, # and % = significantly different from HPNE ( p < 0.05). (C), Expression of EN2. Immunocytochemistry was performed to examine EN2 expression in HPNE, PANC‐1, and AsPC‐1 cells.

Techniques: Expressing, Isolation, Western Blot, Control, Reverse Transcription Polymerase Chain Reaction, Immunocytochemistry

EN2 knockdown reduces motility, migration, invasion, and EMT marker expression in pancreatic cancer cells. (A) Cell Motility Assay. Pancreatic cancer cells expressing scrambled or EN2 shRNA were cultured in petri dishes. After 18 h, a linear scratch was generated using a fine pipette tip, and phase‐contrast images were captured at 0 and 48 h to assess wound closure. (B) Cell Migration Assay. Cells expressing scrambled or EN2 shRNA were seeded in six‐well plates, and migration was quantified as described in the Materials and Methods. Data represent mean ( n = 4) ± SD. * p < 0.05 compared with the scrambled control. (C) Cell Invasion Assay. Cells expressing scrambled or EN2 shRNA were seeded in six‐well plates, and invasion was measured as described in the Materials and Methods. Data represent mean ( n = 4) ± SD. * p < 0.05 compared with the scrambled control. (D, E) Total RNA was isolated, and the expression of E‐cadherin, N‐cadherin, Snail, Slug, and Zeb1 was quantified by qRT‐PCR. GAPDH served as the internal control. Data represent mean ( n = 4) ± SD. * p < 0.05 between groups.

Journal: Journal of Cellular and Molecular Medicine

Article Title: EN2 Regulates Pancreatic Cancer Initiation, Progression, and Epithelial‐Mesenchymal Transition Through the Notch Signalling Pathway

doi: 10.1111/jcmm.71158

Figure Lengend Snippet: EN2 knockdown reduces motility, migration, invasion, and EMT marker expression in pancreatic cancer cells. (A) Cell Motility Assay. Pancreatic cancer cells expressing scrambled or EN2 shRNA were cultured in petri dishes. After 18 h, a linear scratch was generated using a fine pipette tip, and phase‐contrast images were captured at 0 and 48 h to assess wound closure. (B) Cell Migration Assay. Cells expressing scrambled or EN2 shRNA were seeded in six‐well plates, and migration was quantified as described in the Materials and Methods. Data represent mean ( n = 4) ± SD. * p < 0.05 compared with the scrambled control. (C) Cell Invasion Assay. Cells expressing scrambled or EN2 shRNA were seeded in six‐well plates, and invasion was measured as described in the Materials and Methods. Data represent mean ( n = 4) ± SD. * p < 0.05 compared with the scrambled control. (D, E) Total RNA was isolated, and the expression of E‐cadherin, N‐cadherin, Snail, Slug, and Zeb1 was quantified by qRT‐PCR. GAPDH served as the internal control. Data represent mean ( n = 4) ± SD. * p < 0.05 between groups.

Techniques: Knockdown, Migration, Marker, Expressing, Motility Assay, shRNA, Cell Culture, Generated, Transferring, Cell Migration Assay, Control, Invasion Assay, Isolation, Quantitative RT-PCR

EN2 shRNA inhibits Notch‐target genes and Nanog expression and RBP JK transcription in pancreatic cancer cells. (A, B), Expression of Notch target genes. RNA was isolated, and the expression of cMyc, Cyclin D1, Bcl‐2, Hes 1 and Nanog was measured in cells by q‐RT‐PCR. GAPDH was used as an internal control. Data represent mean ( n = 4) ± SD. * = significantly different between groups ( p < 0.05). (C), RBP JK transcription. PANC‐1 and AsPC‐1 cells were transduced with RBP JK ‐responsive GFP/firefly luciferase viral particles (pGreen Fire1‐ RBP JK with EF1, System Biosciences) along with EN2/scrambled or EN2 shRNA viral particles. RBP JK reporter activity was measured as we described . Data represent mean ( n = 4) ± SD. * = significantly different from scrambled control group ( p < 0.05).

Journal: Journal of Cellular and Molecular Medicine

Article Title: EN2 Regulates Pancreatic Cancer Initiation, Progression, and Epithelial‐Mesenchymal Transition Through the Notch Signalling Pathway

doi: 10.1111/jcmm.71158

Figure Lengend Snippet: EN2 shRNA inhibits Notch‐target genes and Nanog expression and RBP JK transcription in pancreatic cancer cells. (A, B), Expression of Notch target genes. RNA was isolated, and the expression of cMyc, Cyclin D1, Bcl‐2, Hes 1 and Nanog was measured in cells by q‐RT‐PCR. GAPDH was used as an internal control. Data represent mean ( n = 4) ± SD. * = significantly different between groups ( p < 0.05). (C), RBP JK transcription. PANC‐1 and AsPC‐1 cells were transduced with RBP JK ‐responsive GFP/firefly luciferase viral particles (pGreen Fire1‐ RBP JK with EF1, System Biosciences) along with EN2/scrambled or EN2 shRNA viral particles. RBP JK reporter activity was measured as we described . Data represent mean ( n = 4) ± SD. * = significantly different from scrambled control group ( p < 0.05).

Techniques: shRNA, Expressing, Isolation, Reverse Transcription Polymerase Chain Reaction, Control, Transduction, Luciferase, Activity Assay

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