Pep-1 (Uncapped) Peptide

Catalog No. ABIN399720

Product Details

Target: Pep-1 (Uncapped)

Purity: > 95 %

Application Details

Restrictions: For Research Use only

Handling

Storage: -20 °C

References

Park, Yamanaka, Tran, Chandrangsu, Akers, de Leon, Morrissette, Selsted, Tan: "The cell-penetrating peptide, Pep-1, has activity against intracellular chlamydial growth but not extracellular forms of Chlamydia trachomatis." in: The Journal of antimicrobial chemotherapy, Vol. 63, Issue 1, pp. 115-23, (2008) (PubMed).

Target Details

Target: Pep-1 (Uncapped)

Background: 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.