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Int-H1-S6A F8 c-myc inhibitor

c-Myc inhibitor
 
BML-P605-0500 0.5 mg 173.00 USD
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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 (IC50=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

Identity:Determined by MS.
 
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
 
MW:3873.6
 
Source:Synthetic.
 
Formulation:Lyophilized.
 
Purity:≥95% (HPLC)
 
Appearance:White to off-white powder.
 
Solubility:Soluble in water.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 

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.; J. Biol. Chem. 269, 1785 (1994), Abstract;

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