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ATCC human mcf10 2a
Human Mcf10 2a, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+mcf10+2a/MCF-10-2A/pmc03746452-33-0-16
Average 93 stars, based on 9 article reviews

human mcf10 2a - by Bioz Stars, 2026-09

93/100 stars

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Multiple Displacement Amplification:

Article Title: Restoration of the methylation status of hypermethylated gene promoters by microRNA-29b in human breast cancer: A novel epigenetic therapeutic approach
Article Snippet: .. Human MCF10-2A, MCF-7, MDA-MB-361, HCC70, BT-549, Hs-578T, and MDA-MB-231 breast cell lines were obtained from the American Type Culture Collection (ATCC, Manassas, VA) and maintained according to ATCC recommendations. ..

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FIGURE 1 – Selective induction of cell death by p53 C-terminal peptide in normal and pre-malignant human colon cells. (a) DAPI staining in normal human colon cells CDD-33Co (wt p53), pre-malignant colorectal adenoma cells AA/C1 (wt p53), RG/C2 (mutant p53) and BR/C1 (mutant p53). Cells were treated with 50 M p53p alone, Ant alone, p53-AntCONT or p53p-Ant for 24 hr and nuclear morphology was analyzed by DAPI staining. Number of apoptotic cells with nuclear morphology typical of apoptosis were scored in at least 400 cells in each sample by ﬂuorescence microscopy. All microscopy experiments were carried out by a blinded reader to the actual groups. Data represent mean and SD of triplicate experiments. (b) TdT (TUNEL) assay in normal human colon cells CDD-33Co (wt p53), pre-malignant colorectal adenoma cells AA/C1 (wt p53), RG/C2 (mutant p53) and BR/C1 (mutant p53). Cells were treated with 50 M p53p-Ant for 18 hr. Apoptotic cells were determined by TdT assay and representative histograms show relative apoptotic cell numbers. (c) Effects of endogenous p53 status upon p53 C-terminal peptide induced apoptosis in H1299 cells with stably transfected human ts p53 mutant 143Ala. Cells were pre-incubated for 16 hr at 37 or 32.5°C and then treated with 50 M p53p-Ant for an additional 18 hr. Apoptotic cells were determined by TdT (TUNEL) assay and representative histograms show relative apoptotic cell numbers. (d) Morphological analysis of apoptotic cells in MCF10-2A (wt p53) and MDA-MB-468 (mutant p53) cells. Cells were treated with 10 M p53p-AntCONT or p53p-Ant for 12 hr and then nuclear morphology was analyzed by DAPI staining. The typical morphology in 400 magniﬁcation.

Journal: International journal of cancer

Article Title: Selective induction of apoptosis through the FADD/caspase-8 pathway by a p53 c-terminal peptide in human pre-malignant and malignant cells.

doi: 10.1002/ijc.20838

Figure Lengend Snippet: FIGURE 1 – Selective induction of cell death by p53 C-terminal peptide in normal and pre-malignant human colon cells. (a) DAPI staining in normal human colon cells CDD-33Co (wt p53), pre-malignant colorectal adenoma cells AA/C1 (wt p53), RG/C2 (mutant p53) and BR/C1 (mutant p53). Cells were treated with 50 M p53p alone, Ant alone, p53-AntCONT or p53p-Ant for 24 hr and nuclear morphology was analyzed by DAPI staining. Number of apoptotic cells with nuclear morphology typical of apoptosis were scored in at least 400 cells in each sample by ﬂuorescence microscopy. All microscopy experiments were carried out by a blinded reader to the actual groups. Data represent mean and SD of triplicate experiments. (b) TdT (TUNEL) assay in normal human colon cells CDD-33Co (wt p53), pre-malignant colorectal adenoma cells AA/C1 (wt p53), RG/C2 (mutant p53) and BR/C1 (mutant p53). Cells were treated with 50 M p53p-Ant for 18 hr. Apoptotic cells were determined by TdT assay and representative histograms show relative apoptotic cell numbers. (c) Effects of endogenous p53 status upon p53 C-terminal peptide induced apoptosis in H1299 cells with stably transfected human ts p53 mutant 143Ala. Cells were pre-incubated for 16 hr at 37 or 32.5°C and then treated with 50 M p53p-Ant for an additional 18 hr. Apoptotic cells were determined by TdT (TUNEL) assay and representative histograms show relative apoptotic cell numbers. (d) Morphological analysis of apoptotic cells in MCF10-2A (wt p53) and MDA-MB-468 (mutant p53) cells. Cells were treated with 10 M p53p-AntCONT or p53p-Ant for 12 hr and then nuclear morphology was analyzed by DAPI staining. The typical morphology in 400 magniﬁcation.

Article Snippet: Normal human colon cell line CCD-33Co (wild-type p53), non-malignant human breast cell line MCF10-2A (wild-type p53), malignant human breast cell lines MCF-7 (wild-type p53), MDA-MB-468 (mutant p53), MDA-MB-231 (mutant p53) and MDA-MB-157 (null p53) and human lung cancer cell line H1299 (null p53) were obtained from ATCC.

Techniques: Staining, Mutagenesis, Microscopy, TUNEL Assay, Stable Transfection, Transfection, Incubation

FIGURE 2 – Surface plasmon resonance (SPR) binding assays (BIA- CORE) of p53p-Ant exposed to H1299/p53-143#6 whole cell lysates. Measurement of binding kinetics are shown between immobilized p53p-Ant at 1 pg/mm2 and H1299/p53-143 transfectant cell lysates at 32.5°C (wt p53 form; dotted line) and 37°C (mutant p53 form; solid line). Concentration of 10 nM p53p-Ant demonstrated differences in the maximum binding capacity and association/dissociation constants at the two temperatures. SPR were determined by using a BIAcoreX biosensor system. (a) Sensogram. (b) Association slope. (c) Dissoci- ation slope.

Journal: International journal of cancer

Article Title: Selective induction of apoptosis through the FADD/caspase-8 pathway by a p53 c-terminal peptide in human pre-malignant and malignant cells.

doi: 10.1002/ijc.20838

Figure Lengend Snippet: FIGURE 2 – Surface plasmon resonance (SPR) binding assays (BIA- CORE) of p53p-Ant exposed to H1299/p53-143#6 whole cell lysates. Measurement of binding kinetics are shown between immobilized p53p-Ant at 1 pg/mm2 and H1299/p53-143 transfectant cell lysates at 32.5°C (wt p53 form; dotted line) and 37°C (mutant p53 form; solid line). Concentration of 10 nM p53p-Ant demonstrated differences in the maximum binding capacity and association/dissociation constants at the two temperatures. SPR were determined by using a BIAcoreX biosensor system. (a) Sensogram. (b) Association slope. (c) Dissoci- ation slope.

Techniques: SPR Assay, Binding Assay, Transfection, Mutagenesis, Concentration Assay

$FIGURE 3 – p53 C-terminal peptide-induced cell death: apoptosis vs. necrosis. (A) DAPI staining in human breast non-malignant cells MCF10-2A (wt p53) and malignant cells MDA-MB-468 (mutant p53). Cells were treated with 30 M p53p-Ant for the indicated times and nuclear morphology was analyzed by DAPI staining. Number of apoptotic cells with nuclear morphology typical of apoptosis were scored in at least 400 cells in each sample by ﬂuorescence microscopy. All microscopy experiments were carried out by a blinded reader to the actual groups. Data represent mean and SD of triplicate experiments. (b) LDH assay in human breast malignant cells MDA-MB-468 (mutant p53) and MCF-7 (wt p53). Cells were untreated or treated with 30 M p53p-Ant (C-terminal peptide, aa 361–382) or p53(15)Ant (N-terminal peptide, aa 12–26) for 1 hr. LDH released into the surrounding media was determined according to manufacturer’s instructions (Promega, Madison, WI). Results are expressed as a percentage of the maximum LDH re- lease, determined by cell fractionation by repeated freeze-thawing. The p53 N-terminal peptide, which only induced necrosis without apoptosis, was used as a positive control for necrosis.36,37 Data represent mean and SD of triplicate experiments.$

Journal: International journal of cancer

Article Title: Selective induction of apoptosis through the FADD/caspase-8 pathway by a p53 c-terminal peptide in human pre-malignant and malignant cells.

doi: 10.1002/ijc.20838

Figure Lengend Snippet: FIGURE 3 – p53 C-terminal peptide-induced cell death: apoptosis vs. necrosis. (A) DAPI staining in human breast non-malignant cells MCF10-2A (wt p53) and malignant cells MDA-MB-468 (mutant p53). Cells were treated with 30 M p53p-Ant for the indicated times and nuclear morphology was analyzed by DAPI staining. Number of apoptotic cells with nuclear morphology typical of apoptosis were scored in at least 400 cells in each sample by ﬂuorescence microscopy. All microscopy experiments were carried out by a blinded reader to the actual groups. Data represent mean and SD of triplicate experiments. (b) LDH assay in human breast malignant cells MDA-MB-468 (mutant p53) and MCF-7 (wt p53). Cells were untreated or treated with 30 M p53p-Ant (C-terminal peptide, aa 361–382) or p53(15)Ant (N-terminal peptide, aa 12–26) for 1 hr. LDH released into the surrounding media was determined according to manufacturer’s instructions (Promega, Madison, WI). Results are expressed as a percentage of the maximum LDH re- lease, determined by cell fractionation by repeated freeze-thawing. The p53 N-terminal peptide, which only induced necrosis without apoptosis, was used as a positive control for necrosis.36,37 Data represent mean and SD of triplicate experiments.

Techniques: Staining, Mutagenesis, Microscopy, Lactate Dehydrogenase Assay, Cell Fractionation, Positive Control

FIGURE 4 – Western blot for p21 expression in human breast malig- nant cells MDA-MB468 (mutant p53), MDA-MB231 (mutant p53) and MCF7 (wt p53). Cells were treated with 30 M p53p-Ant for 0, 3 or 6 hr. p21 expression was analyzed by Western blot using anti-p21 polyclonal antibody (clone: H-164). Expression of -tubulin was used as a control.

Journal: International journal of cancer

Article Title: Selective induction of apoptosis through the FADD/caspase-8 pathway by a p53 c-terminal peptide in human pre-malignant and malignant cells.

doi: 10.1002/ijc.20838

Figure Lengend Snippet: FIGURE 4 – Western blot for p21 expression in human breast malig- nant cells MDA-MB468 (mutant p53), MDA-MB231 (mutant p53) and MCF7 (wt p53). Cells were treated with 30 M p53p-Ant for 0, 3 or 6 hr. p21 expression was analyzed by Western blot using anti-p21 polyclonal antibody (clone: H-164). Expression of -tubulin was used as a control.

Techniques: Western Blot, Expressing, Mutagenesis, Control

FIGURE 5 – Effect of speciﬁc caspase-3 inhib- itor (Z-DEVD-FMK), caspase-8 inhibitor (Z- IETD-FMK) and caspase-9 inhibitor (Z-LEHD- FMK) on p53p-Ant-induced apoptosis in human breast malignant cells MDA-MB-468 (mutant p53). Cells were pre-treated with 4 M inhibitors for 60 min and then treated with 30 M p53p- Ant for 6 hr. Apoptotic cells were determined by TdT (TUNEL) assay and quantitated by ﬂow cytometry according to the manufacturer’s in- structions. Representative histograms show rela- tive apoptotic cell numbers.

Journal: International journal of cancer

Article Title: Selective induction of apoptosis through the FADD/caspase-8 pathway by a p53 c-terminal peptide in human pre-malignant and malignant cells.

doi: 10.1002/ijc.20838

Figure Lengend Snippet: FIGURE 5 – Effect of speciﬁc caspase-3 inhib- itor (Z-DEVD-FMK), caspase-8 inhibitor (Z- IETD-FMK) and caspase-9 inhibitor (Z-LEHD- FMK) on p53p-Ant-induced apoptosis in human breast malignant cells MDA-MB-468 (mutant p53). Cells were pre-treated with 4 M inhibitors for 60 min and then treated with 30 M p53p- Ant for 6 hr. Apoptotic cells were determined by TdT (TUNEL) assay and quantitated by ﬂow cytometry according to the manufacturer’s in- structions. Representative histograms show rela- tive apoptotic cell numbers.

Techniques: Inhibition, Mutagenesis, TUNEL Assay, Cytometry

FIGURE 7 – Effect of FADD ex- pression on p53 C-terminal peptide- induced apoptosis. (a) Expression of the dominant-negative FADD (DN- FADD, aa 80–293) in MDA-MB- 468 breast and H1299/ts p53-143#6 lung cancer cells (at 37°C-mutant p53 form). Cells were infected with 10 MOI adenovirus containing pAd/ CMV/DsRed (vector) or pAd/CMV/ DN-FADD (DN-FADD) for 24 hr. Expression of DN-FADD protein was detected by Western blot using anti-human FADD monoclonal anti- body (clone: 1F7). Expression of -tubulin was used as a control. (b) DN-FADD blocked p53p-Ant-in- duced apoptosis. Transient transfec- tants from the 2 cell lines above were treated without or with 30 M p53p-Ant for 6 hr (MDA-MB-468 cells) or 50 M p53p-Ant for 18 hr (H1299 cells). Apoptotic cells were determined by TdT (TUNEL) assay and quantitated by ﬂow cytometry according to the manufacturer’s in- structions. Representative histo- grams show relative apoptotic cell numbers.

Journal: International journal of cancer

Article Title: Selective induction of apoptosis through the FADD/caspase-8 pathway by a p53 c-terminal peptide in human pre-malignant and malignant cells.

doi: 10.1002/ijc.20838

Figure Lengend Snippet: FIGURE 7 – Effect of FADD ex- pression on p53 C-terminal peptide- induced apoptosis. (a) Expression of the dominant-negative FADD (DN- FADD, aa 80–293) in MDA-MB- 468 breast and H1299/ts p53-143#6 lung cancer cells (at 37°C-mutant p53 form). Cells were infected with 10 MOI adenovirus containing pAd/ CMV/DsRed (vector) or pAd/CMV/ DN-FADD (DN-FADD) for 24 hr. Expression of DN-FADD protein was detected by Western blot using anti-human FADD monoclonal anti- body (clone: 1F7). Expression of -tubulin was used as a control. (b) DN-FADD blocked p53p-Ant-in- duced apoptosis. Transient transfec- tants from the 2 cell lines above were treated without or with 30 M p53p-Ant for 6 hr (MDA-MB-468 cells) or 50 M p53p-Ant for 18 hr (H1299 cells). Apoptotic cells were determined by TdT (TUNEL) assay and quantitated by ﬂow cytometry according to the manufacturer’s in- structions. Representative histo- grams show relative apoptotic cell numbers.

Techniques: Expressing, Dominant Negative Mutation, Mutagenesis, Infection, Plasmid Preparation, Western Blot, Control, TUNEL Assay, Cytometry

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