H1 DNA-binding region of c-Myc containing Ser to Ala, and Phe to Ala substitutions (underlined) to confer an increase in its potency to inhibit c-Myc. The N-terminus of this peptide is the Int peptide sequence derived from the third Antennapedia homeodomain, to confer cell permeability. Control for this peptide is H1-S6A,F8A c-Myc inhibibitor peptide (Prod. No. BML-P606). Inhibited cloning efficiency of MCF-7 human breast cancer cells by 90% at 10 µM (IC
50=5.9 µM). In MCF-7 cells, it inhibited cell growth and induced apoptosis.
In addition, at 10 µM it strongly inhibited transcription of the c-Myc regulated genes ODC and p53. The non-cell-permeable control for this peptide is H1-S6A, F8A c-Myc inhibitor peptide which lacks the N-terminal internalization sequence.
Product Specification
| MW: | 3873.6 |
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| Purity: | ≥95% (HPLC) |
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| Sequence: | Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-Asn-Glu-Leu-Lys-Arg-Ala-Phe-Ala-Ala-Leu-Arg-Asp-Gln-Ile |
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| Formulation: | Lyophilized solid |
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| Solubility: | Soluble in water |
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| Long Term Storage: | -20°C |
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| Background / Technical Information: | Please click here for the comprehensive product datasheet. |
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Product Literature References
Inhibition of cancer cell growth and c-Myc transcriptional activity by a c-Myc helix 1-type peptide fused to an internalization sequence: L. Giorello et al.; Cancer. Res.
58, 3654 (1998),
Abstract;
The third helix of the Antennapedia homeodomain translocates through biological membranes: D Derossi et al.; J. Biol. Chem.
270, 14255 (1995),
Abstract;
Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR: L. J. Draeger et al.;
269, 1785 (1994),
Abstract;