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Pep-1 (uncapped)  |
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| Cat. No. |
Size |
Price |
Figures |
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RP10130-1 mg
| 1 mg | $ 142.00 | HPLC: 20060721145614 (PDF)
MS: 20060721145553 (PDF)
MSDS: 20080710034739 (PDF)
References:
- Henriques ST, et al. Re-evaluating the role of strongly charged sequences in amphipathic cell-penetrating peptides: a fluorescence study using Pep-1. FEBS. Lett. Aug 2005; 579(20): 4498-4502.
- Weller K, et al. Biophysical and biological studies of end-group-modified derivatives of Pep-1. Biochemistry. Dec 2005; 44(48):1 5799-5811.
- Eum WS, et al. In vivo protein transduction: biologically active intact pep-1-superoxide dismutase fusion protein efficiently protects against ischemic insult. Free Radic. Biol. Med. Nov 2004; 37(10): 1656-1669.
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| Full Name | |
Sequence
(one-letter code) |
KETWWETWWTEWSQPKKKRKV | Sequence
(three-letter code) | {LYS}{GLU}{THR}{TRP}{TRP}{GLU}{THR}{TRP}{TRP}{THR}
{GLU}{TRP}{SER}{GLN}{PRO}{LYS}{LYS}{LYS}{ARG}{LYS}
{VAL} |
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| Description | PEP-1 peptide, which has 21 amino acid residues, is a known carrier peptide that delivers full-length native proteins in vitro and in vivo. Pep-1 peptide, consists of three domains: (1) a hydrophobic tryptophan-rich motif containing five tryptophan residues (KETW WETWWTEW); (2) a hydrophilic lysine-rich domain (KKKRKV) derived from the nuclear localization sequence (NLS) of simian virus 40 (SV-40) large T antigen; and (3) a spacer domain (SQP), separating the two domains mentioned above, containing a proline residue, which improves the flexibility and the integrity of both the hydrophobic and the hydrophilic domains. In standard cell culture conditions, Pep-1 localizes rapidly, in <10 min, to the nucleus of human HS-68, murine NIH-3T3 fibroblasts, or Cos cells. Similar experiments, performed by incubating cells for 30 min at 4°C before transfection, yielded essentially the same result, indicating that Pep-1 internalization is independent of normal endocytosis. |
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| Formula | C136H195N35O33 |
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| M.W. | 2848.3 |
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| Purity | > 95% |
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| Storage | Store at -20°C |
| * For Non-Clinical Research Use Only *
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