(1 reference)-
- Antigène
- Pep-1 (Uncapped)
- Pureté
- > 95 %
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- Restrictions
- For Research Use only
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- Stock
- -20 °C
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: "The cell-penetrating peptide, Pep-1, has activity against intracellular chlamydial growth but not extracellular forms of Chlamydia trachomatis." dans: The Journal of antimicrobial chemotherapy, Vol. 63, Issue 1, pp. 115-23, (2008) (PubMed).
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: "The cell-penetrating peptide, Pep-1, has activity against intracellular chlamydial growth but not extracellular forms of Chlamydia trachomatis." dans: The Journal of antimicrobial chemotherapy, Vol. 63, Issue 1, pp. 115-23, (2008) (PubMed).
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- Antigène
- Pep-1 (Uncapped)
- Sujet
- 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- before transfection, yielded essentially the same result, indicating that Pep-1 internalization is independent of normal endocytosis.
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