Review

a431 parental cells (OriGene)

OriGene is a verified supplier

OriGene manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

OriGene a431 parental cells
A431 Parental Cells, supplied by OriGene, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/a431+parental+cells/A431+(Human+epithelial+carcinoma+cell+line)+Whole+Cell+Lysate/10__1074_slash_jbc__m115__679217-69-9-16
Average 93 stars, based on 10 article reviews

a431 parental cells - by Bioz Stars, 2026-10

93/100 stars

Images

Plasmid Preparation:

Article Title: Inhibition of Oncogenic Epidermal Growth Factor Receptor Kinase Triggers Release of Exosome-like Extracellular Vesicles and Impacts Their Phosphoprotein and DNA Content
Article Snippet: Cell lines were cultured in DMEM (Invitrogen), supplemented with 10% fetal bovine serum (FBS) (Multicell Wisent, Inc., St-Bruno, Quebec, Canada), and penicillin/streptomycin (Invitrogen). .. The clonal A431-CD63/GFP cell line was prepared by transfecting A431 parental cells with the plasmid pCMV6-AC-GFP (OriGene, Rockville, MD), clone RG 201733, encoding the CD63-GFP fusion protein. ..

Image Search Results

Fig. 1 – Expression levels of RPS12 and c-Myc were analysed in A431-III and A431-P cells. A. Western blot analyses of RPS12 and c-Myc expressions were conducted using speciﬁc antibodies. The multiples of change on the western blots shown in (B) were analysed using ImageJ software.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 1 – Expression levels of RPS12 and c-Myc were analysed in A431-III and A431-P cells. A. Western blot analyses of RPS12 and c-Myc expressions were conducted using speciﬁc antibodies. The multiples of change on the western blots shown in (B) were analysed using ImageJ software.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: Expressing, Western Blot, Software

Fig. 2 – Cell viability analysis of A431-III cells treated with ﬂavonoids and inhibitors using an MTT assay. The structures of luteolin and quercetin are shown in A and B. A431-III cell viability was analysed after treatment with different concentrations of luteolin (Lu) and quercetin (Qu) (A), rapamycin (C), LY294002 (D), and 10058-F4 (E) for 24 h via the MTT assay.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 2 – Cell viability analysis of A431-III cells treated with ﬂavonoids and inhibitors using an MTT assay. The structures of luteolin and quercetin are shown in A and B. A431-III cell viability was analysed after treatment with different concentrations of luteolin (Lu) and quercetin (Qu) (A), rapamycin (C), LY294002 (D), and 10058-F4 (E) for 24 h via the MTT assay.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: MTT Assay

Fig. 3 – c-Myc expression is inhibited by luteolin and quercetin through Akt/mTOR signalling. A. A431-III cells were treated with control (DMSO), luteolin (10 µM, 20 µM), and quercetin (20 µM, 40 µM) for 24 h. Cell lysates of A431-P cells and A431-III cells treated with different concentrations of luteolin and quercetin were collected and analysed by western blotting using speciﬁc antibodies. B. A431-III cells were treated with DMSO, 5 or 10 nM rapamycin, or 5 or 10 µM LY294002 for 24 h. Cell lysates of A431-P cells and A431-III cells were treated with different concentration of rapamycin or LY294002 were collected, and the expressions were detected by western blotting using speciﬁc antibodies.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 3 – c-Myc expression is inhibited by luteolin and quercetin through Akt/mTOR signalling. A. A431-III cells were treated with control (DMSO), luteolin (10 µM, 20 µM), and quercetin (20 µM, 40 µM) for 24 h. Cell lysates of A431-P cells and A431-III cells treated with different concentrations of luteolin and quercetin were collected and analysed by western blotting using speciﬁc antibodies. B. A431-III cells were treated with DMSO, 5 or 10 nM rapamycin, or 5 or 10 µM LY294002 for 24 h. Cell lysates of A431-P cells and A431-III cells were treated with different concentration of rapamycin or LY294002 were collected, and the expressions were detected by western blotting using speciﬁc antibodies.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: Expressing, Control, Western Blot, Concentration Assay

Fig. 4 – Ribosomal protein S12 (RPS12) expression is inhibited by luteolin and quercetin through Akt/mTOR signalling. A. A431-III cells were treated with DMSO, 10 or 20 µM luteolin, or 20 or 40 µM quercetin for 24 h. Cell lysates of A431-P cells and A431-III cells were collected and analysed by western blotting using an RPS12 antibody. B. Changes in RPS12 expression after treatment with luteolin and quercetin were analysed using ImageJ software. C. A431-III cells were treated with DMSO, 5, 10 nM rapamycin, or 5, 10 µM LY294002 for 24 h. Cell lysates of A431-P and A431-III cells were collected and analysed by western blotting using an RPS12 antibody. D. Changes in RPS12 expression after treatment with rapamycin and LY294002 were analysed using ImageJ software.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 4 – Ribosomal protein S12 (RPS12) expression is inhibited by luteolin and quercetin through Akt/mTOR signalling. A. A431-III cells were treated with DMSO, 10 or 20 µM luteolin, or 20 or 40 µM quercetin for 24 h. Cell lysates of A431-P cells and A431-III cells were collected and analysed by western blotting using an RPS12 antibody. B. Changes in RPS12 expression after treatment with luteolin and quercetin were analysed using ImageJ software. C. A431-III cells were treated with DMSO, 5, 10 nM rapamycin, or 5, 10 µM LY294002 for 24 h. Cell lysates of A431-P and A431-III cells were collected and analysed by western blotting using an RPS12 antibody. D. Changes in RPS12 expression after treatment with rapamycin and LY294002 were analysed using ImageJ software.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: Expressing, Western Blot, Software

Fig. 5 – c-Myc regulates ribosomal protein S12 (RPS12) expression. A. A431-III cells were treated with DMSO, or 100, 200, and 400 µM 10058-F4 for 24 h. Cell lysates of A431-P and A431-III cells were collected and analysed by western blotting using a RPS12 antibody. B. Changes in RPS12 expression after treatment with 10058-F3 were analysed using ImageJ software. C. The pcDNA3-cMyc-HA plasmid at 0.5, 1, or 1.5 µg was transfected into A431-P cells for 48 h. Cell lysates were collected and analysed by western blotting using c-Myc and RPS12 antibodies. D. Changes in RPS12 expression after transfection with the pcDNA3-cMyc-HA plasmid were analysed using ImageJ software.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 5 – c-Myc regulates ribosomal protein S12 (RPS12) expression. A. A431-III cells were treated with DMSO, or 100, 200, and 400 µM 10058-F4 for 24 h. Cell lysates of A431-P and A431-III cells were collected and analysed by western blotting using a RPS12 antibody. B. Changes in RPS12 expression after treatment with 10058-F3 were analysed using ImageJ software. C. The pcDNA3-cMyc-HA plasmid at 0.5, 1, or 1.5 µg was transfected into A431-P cells for 48 h. Cell lysates were collected and analysed by western blotting using c-Myc and RPS12 antibodies. D. Changes in RPS12 expression after transfection with the pcDNA3-cMyc-HA plasmid were analysed using ImageJ software.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: Expressing, Western Blot, Software, Plasmid Preparation, Transfection

Fig. 6 – The transactivation of ribosomal protein S12 (RPS12) is regulated by Akt/mTOR/c-Myc signalling. A. The pGL3-basic plasmid at 0.5 µg, or 0.5 or 1.0 µg of the pGL3-RPS12-pro plasmid was transfected into A431-P cells for 48 h, and the transactivation activities were analysed using a luciferase assay. B. The pGL3-RPS12-pro plasmid was transfected into A431-III cells for 24 h, and the cells were treated with DMSO or 10 or 20 µM luteolin for an additional 24 h. The transactivation activities were measured by a luciferase assay. C. The pGL3-RPS12-pro plasmid was transfected into A431-III cells for 24 h, and the cells were treated with 20 or 40 µM quercetin for an additional 24 h. The transactivation activity was measured by a luciferase assay. D. The pGL3-RPS12-pro plasmid was transfected into A431-III cells for 24 h, and the cells were treated with 100 or 200 µM 10058-F4 for an additional 24 h. The transactivation activity was measured by a luciferase assay.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 6 – The transactivation of ribosomal protein S12 (RPS12) is regulated by Akt/mTOR/c-Myc signalling. A. The pGL3-basic plasmid at 0.5 µg, or 0.5 or 1.0 µg of the pGL3-RPS12-pro plasmid was transfected into A431-P cells for 48 h, and the transactivation activities were analysed using a luciferase assay. B. The pGL3-RPS12-pro plasmid was transfected into A431-III cells for 24 h, and the cells were treated with DMSO or 10 or 20 µM luteolin for an additional 24 h. The transactivation activities were measured by a luciferase assay. C. The pGL3-RPS12-pro plasmid was transfected into A431-III cells for 24 h, and the cells were treated with 20 or 40 µM quercetin for an additional 24 h. The transactivation activity was measured by a luciferase assay. D. The pGL3-RPS12-pro plasmid was transfected into A431-III cells for 24 h, and the cells were treated with 100 or 200 µM 10058-F4 for an additional 24 h. The transactivation activity was measured by a luciferase assay.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: Plasmid Preparation, Transfection, Luciferase, Activity Assay

Fig. 7 – The migratory ability of A431-III cells is blocked by Akt/mTOR/c-Myc signalling. A. A wound-healing assay was conducted, and the cells were observed for migration into the wound area. A431-III cells were treated with (a) DMSO; (b) 5 nM, (c) 10 nM rapamycin; (d) 5 µM, (e) 10 µM LY294002; (f) 100 µM, (g) 200 µM 10058-F4 for 24 h. B. The migrating cells were measured and analysed using ImageJ software.

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 7 – The migratory ability of A431-III cells is blocked by Akt/mTOR/c-Myc signalling. A. A wound-healing assay was conducted, and the cells were observed for migration into the wound area. A431-III cells were treated with (a) DMSO; (b) 5 nM, (c) 10 nM rapamycin; (d) 5 µM, (e) 10 µM LY294002; (f) 100 µM, (g) 200 µM 10058-F4 for 24 h. B. The migrating cells were measured and analysed using ImageJ software.

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: Wound Healing Assay, Migration, Software

Fig. 8 – RPS12 promotes the invasion of cancer cells. (A) Two RPS12 shRNA were transfected into A431-III cells, and protein expression was analysed via western blotting. A trans-well assay was used to analyse the invasion ability of A431-III cells transfected with control shRNA (B), two RPS12 shRNA (C, D) and treated with 0.01% DMSO (E), or 200 µM 10058-F4 (F).

Journal: Journal of Functional Foods

Article Title: RPS12 increases the invasiveness in cervical cancer activated by c-Myc and inhibited by the dietary flavonoids luteolin and quercetin

doi: 10.1016/j.jff.2015.09.030

Figure Lengend Snippet: Fig. 8 – RPS12 promotes the invasion of cancer cells. (A) Two RPS12 shRNA were transfected into A431-III cells, and protein expression was analysed via western blotting. A trans-well assay was used to analyse the invasion ability of A431-III cells transfected with control shRNA (B), two RPS12 shRNA (C, D) and treated with 0.01% DMSO (E), or 200 µM 10058-F4 (F).

Article Snippet: Parental A431 cells (human epidermal carcinoma cells called A431-P in this study) were obtained from ATCC (Manassas, VA, USA).

Techniques: shRNA, Transfection, Expressing, Western Blot, Control

Cross-regulation of EGFR ligands AREG and EREG in A431 SCC cells. ( A ) Lysates from A431 parental cells and their derivatives ‘control shRNA’, ‘AREG shRNA’, ‘EREG shRNA’, and ‘DUSP6-shRNA’ were prepared and analysed by western blot for expression of AREG, EREG, and DUSP6 proteins using specific antibodies as described in the ‘Materials and Methods’ section. The Western blots were also probed with an anti- β -actin antibody to demonstrate equal protein loading. ( B ) Commercially available ELISAs were used for the quantitative determination of AREG and EREG protein expression in whole-cell lysates from A431-derived ‘control (Ct.) shRNA’, ‘AREG shRNA’, ‘EREG shRNA’, and ‘DUSP6-shRNA’ cell lines. Results are means ( columns ) and 95% confidence intervals ( bars ) of two independent experiments made in duplicate. Statistically significant differences (one-factor ANOVA analysis) between experimental condition groups (i.e., A431 cells stably expressing shRNAs against AREG, EREG, and DUSP6) and ‘control (Ct.) shRNA’ cells are shown (NS no statistically significant).

Journal: British Journal of Cancer

Article Title: Cross-suppression of EGFR ligands amphiregulin and epiregulin and de-repression of FGFR3 signalling contribute to cetuximab resistance in wild-type KRAS tumour cells

doi: 10.1038/bjc.2012.103

Figure Lengend Snippet: Cross-regulation of EGFR ligands AREG and EREG in A431 SCC cells. ( A ) Lysates from A431 parental cells and their derivatives ‘control shRNA’, ‘AREG shRNA’, ‘EREG shRNA’, and ‘DUSP6-shRNA’ were prepared and analysed by western blot for expression of AREG, EREG, and DUSP6 proteins using specific antibodies as described in the ‘Materials and Methods’ section. The Western blots were also probed with an anti- β -actin antibody to demonstrate equal protein loading. ( B ) Commercially available ELISAs were used for the quantitative determination of AREG and EREG protein expression in whole-cell lysates from A431-derived ‘control (Ct.) shRNA’, ‘AREG shRNA’, ‘EREG shRNA’, and ‘DUSP6-shRNA’ cell lines. Results are means ( columns ) and 95% confidence intervals ( bars ) of two independent experiments made in duplicate. Statistically significant differences (one-factor ANOVA analysis) between experimental condition groups (i.e., A431 cells stably expressing shRNAs against AREG, EREG, and DUSP6) and ‘control (Ct.) shRNA’ cells are shown (NS no statistically significant).

Article Snippet: Parental A431 vulvar squamous carcinoma cells (obtained from the American Type Culture Collection, Manassas, VA, USA) were routinely grown in Dulbecco’s modified Eagle’s medium (DMEM, Gibco Cell Culture Systems, Invitrogen S.A., Barcelona, Spain) containing 10% heat-inactivated foetal bovine serum (FBS, Bio-Whittaker, Inc., Walkersville, MD, USA), 1% L-glutamine, 1% sodium pyruvate, 50 U ml −1 penicillin, and 50 U ml −1 streptomycin.

Techniques: Control, shRNA, Western Blot, Expressing, Derivative Assay, Stable Transfection

Differential regulation of EGFR ligands AREG and EREG by Ctx in Ctx-responsive and Ctx-resistant SCC cells. AREG- and EREG-specific ELISAs were used to quantitatively assess the effects of Ctx treatment (48 h) in Ctx-responsive A431 parental cells ( A ) and in two independent Ctx-resistant A431 pooled populations ( B ). Results are means ( columns ) and 95% confidence intervals ( bars ) of two independent experiments made in duplicate. Statistically significant differences (one-factor ANOVA analysis) between Ctx-untreated and Ctx-treated cells and/or between A431 parental cells and their Ctx-unresponsive pooled populations are shown.

Journal: British Journal of Cancer

Article Title: Cross-suppression of EGFR ligands amphiregulin and epiregulin and de-repression of FGFR3 signalling contribute to cetuximab resistance in wild-type KRAS tumour cells

doi: 10.1038/bjc.2012.103

Figure Lengend Snippet: Differential regulation of EGFR ligands AREG and EREG by Ctx in Ctx-responsive and Ctx-resistant SCC cells. AREG- and EREG-specific ELISAs were used to quantitatively assess the effects of Ctx treatment (48 h) in Ctx-responsive A431 parental cells ( A ) and in two independent Ctx-resistant A431 pooled populations ( B ). Results are means ( columns ) and 95% confidence intervals ( bars ) of two independent experiments made in duplicate. Statistically significant differences (one-factor ANOVA analysis) between Ctx-untreated and Ctx-treated cells and/or between A431 parental cells and their Ctx-unresponsive pooled populations are shown.

Techniques:

Activation of FGFR3 replaces loss of EGFR-ligands signalling and contributes to Ctx resistance through pathway redundancy. ( A ) Phosphoproteome profiling of A431 cells during acquisition of resistance to Ctx. Total cell lysates (750 μ g) from A431 cells before (WT) and after (POOL1) adaptation to Ctx treatment were incubated with membranes of the phosphoproteomic platforms human Phospho-RTK (top panels; 42 different RTKs) and human Phospho-MAPK (bottom panels; 23 different MAPKs and other serine/threonine kinases) as per the manufacturer’s instructions (Proteome Profiler; R&D Systems). Figure shows representative phosphoproteome analyses that were developed on X-ray film following exposure to chemiluminescent reagents. Equivalent results were obtained in three independent experiments. ( B ) Synergy analyses of the interaction between Ctx and PD173074. Top : Ctx-naive A431 parental cells and Ctx-resistant POOL1 cells were incubated with graded concentrations of PD173074 in the absence or presence of 100 μ g ml −1 Ctx, as specified. Cell viability, measured using MTT uptake assays, was expressed as % of untreated control cells (=100% cell viability). Results are means and 95% confidence intervals ( bars ) of three independent experiments made in triplicate. Bottom : Quantification of apoptosis-related cell death in Ctx-naive A431 parental cells and Ctx-resistant POOL1 cells in response to 72 h treatment with Ctx, PD173074 or Ctx plus PD173074, as specified, was determined by Cell Death ELISA as described in ‘Materials and Methods’. Data are the mean (columns) and 95% confidence intervals (bars) of three independent experiments performed in duplicates.

Journal: British Journal of Cancer

Article Title: Cross-suppression of EGFR ligands amphiregulin and epiregulin and de-repression of FGFR3 signalling contribute to cetuximab resistance in wild-type KRAS tumour cells

doi: 10.1038/bjc.2012.103

Figure Lengend Snippet: Activation of FGFR3 replaces loss of EGFR-ligands signalling and contributes to Ctx resistance through pathway redundancy. ( A ) Phosphoproteome profiling of A431 cells during acquisition of resistance to Ctx. Total cell lysates (750 μ g) from A431 cells before (WT) and after (POOL1) adaptation to Ctx treatment were incubated with membranes of the phosphoproteomic platforms human Phospho-RTK (top panels; 42 different RTKs) and human Phospho-MAPK (bottom panels; 23 different MAPKs and other serine/threonine kinases) as per the manufacturer’s instructions (Proteome Profiler; R&D Systems). Figure shows representative phosphoproteome analyses that were developed on X-ray film following exposure to chemiluminescent reagents. Equivalent results were obtained in three independent experiments. ( B ) Synergy analyses of the interaction between Ctx and PD173074. Top : Ctx-naive A431 parental cells and Ctx-resistant POOL1 cells were incubated with graded concentrations of PD173074 in the absence or presence of 100 μ g ml −1 Ctx, as specified. Cell viability, measured using MTT uptake assays, was expressed as % of untreated control cells (=100% cell viability). Results are means and 95% confidence intervals ( bars ) of three independent experiments made in triplicate. Bottom : Quantification of apoptosis-related cell death in Ctx-naive A431 parental cells and Ctx-resistant POOL1 cells in response to 72 h treatment with Ctx, PD173074 or Ctx plus PD173074, as specified, was determined by Cell Death ELISA as described in ‘Materials and Methods’. Data are the mean (columns) and 95% confidence intervals (bars) of three independent experiments performed in duplicates.

Techniques: Activation Assay, Incubation, Control, Enzyme-linked Immunosorbent Assay

Review

a431 parental cells (OriGene)

Structured Review

Images

Related Articles

Plasmid Preparation:

Similar Products

Image Search Results