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    Thermo Fisher superscript iii first strand synthesis system
    Suppression of Akt by PTEN E307K mutant . (A) <t>MDA-MB-453</t> cells were solubilized in 0.01% saponin-containing buffer. The membrane ( Mem ) and cytosolic ( Cyt ) fractions were resolved on SDS-PAGE gel and probed with an anti-PTEN monoclonal antibody (A2B1). The purity of the cytosolic and membrane fractions was confirmed with antibodies against tubulin and EGFR, respectively. (B) Pten -/- MEFS were transduced with the indicated retroviral expression plasmids. Cell lysates were prepared from cell lines and subjected to Western blotting analysis using the indicated antibodies. (C) MCF7 cells were electroporated with the indicated expression plasmids and total cell extracts were prepared for Western blotting analysis. Results from <t>three</t> independent experiments were quantified ( right panel ). Bars , SE. *, p
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    Suppression of Akt by PTEN E307K mutant . (A) <t>MDA-MB-453</t> cells were solubilized in 0.01% saponin-containing buffer. The membrane ( Mem ) and cytosolic ( Cyt ) fractions were resolved on SDS-PAGE gel and probed with an anti-PTEN monoclonal antibody (A2B1). The purity of the cytosolic and membrane fractions was confirmed with antibodies against tubulin and EGFR, respectively. (B) Pten -/- MEFS were transduced with the indicated retroviral expression plasmids. Cell lysates were prepared from cell lines and subjected to Western blotting analysis using the indicated antibodies. (C) MCF7 cells were electroporated with the indicated expression plasmids and total cell extracts were prepared for Western blotting analysis. Results from <t>three</t> independent experiments were quantified ( right panel ). Bars , SE. *, p
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    Suppression of Akt by PTEN E307K mutant . (A) <t>MDA-MB-453</t> cells were solubilized in 0.01% saponin-containing buffer. The membrane ( Mem ) and cytosolic ( Cyt ) fractions were resolved on SDS-PAGE gel and probed with an anti-PTEN monoclonal antibody (A2B1). The purity of the cytosolic and membrane fractions was confirmed with antibodies against tubulin and EGFR, respectively. (B) Pten -/- MEFS were transduced with the indicated retroviral expression plasmids. Cell lysates were prepared from cell lines and subjected to Western blotting analysis using the indicated antibodies. (C) MCF7 cells were electroporated with the indicated expression plasmids and total cell extracts were prepared for Western blotting analysis. Results from <t>three</t> independent experiments were quantified ( right panel ). Bars , SE. *, p
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    Qiagen gel extraction kit
    Suppression of Akt by PTEN E307K mutant . (A) <t>MDA-MB-453</t> cells were solubilized in 0.01% saponin-containing buffer. The membrane ( Mem ) and cytosolic ( Cyt ) fractions were resolved on SDS-PAGE gel and probed with an anti-PTEN monoclonal antibody (A2B1). The purity of the cytosolic and membrane fractions was confirmed with antibodies against tubulin and EGFR, respectively. (B) Pten -/- MEFS were transduced with the indicated retroviral expression plasmids. Cell lysates were prepared from cell lines and subjected to Western blotting analysis using the indicated antibodies. (C) MCF7 cells were electroporated with the indicated expression plasmids and total cell extracts were prepared for Western blotting analysis. Results from <t>three</t> independent experiments were quantified ( right panel ). Bars , SE. *, p
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    Suppression of Akt by PTEN E307K mutant . (A) MDA-MB-453 cells were solubilized in 0.01% saponin-containing buffer. The membrane ( Mem ) and cytosolic ( Cyt ) fractions were resolved on SDS-PAGE gel and probed with an anti-PTEN monoclonal antibody (A2B1). The purity of the cytosolic and membrane fractions was confirmed with antibodies against tubulin and EGFR, respectively. (B) Pten -/- MEFS were transduced with the indicated retroviral expression plasmids. Cell lysates were prepared from cell lines and subjected to Western blotting analysis using the indicated antibodies. (C) MCF7 cells were electroporated with the indicated expression plasmids and total cell extracts were prepared for Western blotting analysis. Results from three independent experiments were quantified ( right panel ). Bars , SE. *, p

    Journal: BMC Cancer

    Article Title: Characterization of a novel PTEN mutation in MDA-MB-453 breast carcinoma cell line

    doi: 10.1186/1471-2407-11-490

    Figure Lengend Snippet: Suppression of Akt by PTEN E307K mutant . (A) MDA-MB-453 cells were solubilized in 0.01% saponin-containing buffer. The membrane ( Mem ) and cytosolic ( Cyt ) fractions were resolved on SDS-PAGE gel and probed with an anti-PTEN monoclonal antibody (A2B1). The purity of the cytosolic and membrane fractions was confirmed with antibodies against tubulin and EGFR, respectively. (B) Pten -/- MEFS were transduced with the indicated retroviral expression plasmids. Cell lysates were prepared from cell lines and subjected to Western blotting analysis using the indicated antibodies. (C) MCF7 cells were electroporated with the indicated expression plasmids and total cell extracts were prepared for Western blotting analysis. Results from three independent experiments were quantified ( right panel ). Bars , SE. *, p

    Article Snippet: Sequencing analysis cDNAs were generated from total RNA of MDA-MB-453 using SuperScript® III First-Strand Synthesis System (Invitrogen).

    Techniques: Mutagenesis, Multiple Displacement Amplification, SDS Page, Transduction, Expressing, Western Blot