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Pep-1 (uncapped)

Cat. No. Size Price Figures
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.
Full Name
Pep-1 (uncapped)
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}
DescriptionPEP-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.
FormulaC136H195N35O33
M.W.2848.3
Purity> 95%
StorageStore at -20°C
* For Non-Clinical Research Use Only *
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