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Cell penetrating peptide for transduction of peptides and proteins into live cells

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CPP-P01L 2,5 mg 360,00 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on blue ice

Storage Conditions: store at -20 °C

Shelf Life: 12 months

Molecular Weight: 2247 Da confirmed by MALDI-MS.

Purity: > 95 % (HPLC)

Form: Synthetic peptide, water soluble powder, contains CF3COO- (trifluoro acetate) as counter ion.

Activity: 1 μl of stock solution is able to form a non-covalent complex with 1 μg of a protein of MW of 100 kDa. 10 to 20 μl of stock solution are necessary for complexation of 1 μg of a nucleoside triphosphate (MW approx. 0.5 kDa carrying 4 negative charges). For different MWs and/or different charges adjust amount of stock solution accordingly.

Availability Restriction: Exclusively distributed in Japan by Greiner BioOne

Penetratin is a cell penetrating peptide from the first generation, which is derived from Drosophila Antennapedia Homeodomain. It contains a nuclear localization sequence and facilitates internalization of cargo into living cells. Transport of the cargo requires in most cases the formation of a conjugate or fusion protein. Addition of a 10- to 20-fold excess of free penetratin to these constructs increases rate and efficiency of internalization. In some cases penetratin is able to form non-covalent complexes with the cargo. Penetratin shows only small cytotoxic effects on a number of cell lines (including HeLa, Jurkat, Swiss 3T3, NIH 3T3, NB-4, HT-1080, COS-7 and Leishmania tarentolae) and can used for internalization of proteins, nucleic acids as well as single nucleotides and nucleotide analogs. For cell survival the critical concentration of Penetratin in serum-free transduction medium is in the range of 20 μg/ml at which cell viability and cell membrane integrity are only marginally reduced (approx. 10-30 %).


Positive Charges:
Peptide provides 8 positive charges for complex formation. Due to ε-amino and guanido groups up to 11 trifluoro acetate residues may be present resulting in an apparent MW of about 3.1 kDa.

Stock solution:
Dissolve 0.5 mg in 1.5 ml sterile and oxygen-free water according to the general manual. Use the solution immediately or aliquot and store at -20 °C. Avoid freeze / thaw cycles. Please note that the peptide may form S-oxide (Met) when stored in solution.

Perform calculation, complex formation and cargo transduction according to detailed protocols given in the general manual.

Jena Bioscience Publications using Penetratin:
Formation of non-covalent complexes with different cargos, transport into different cell lines, uptake efficiencies and cytotoxicity's are described in four publications:
Mussbach et al. (2011). Internalization of nucleoside phosphates into live cells by complex formation with different cell penetrating peptides and JBS-Nucleoducin. In: Langel U., Editor. Cell penetrating peptides Methods and Protocols. Methods in Molecular Biology, vol. 683, Humana Press, Springer, New York, Dordrecht, Heidelberg, London. pp. 375-389.
Mussbach et al. (2011). Transduction of peptides and proteins into live cells by cell penetrating peptides. J. Cell. Biochem. 112: 3824.
Keller et al. (2013). Relationships between cargo, cell penetrating peptides and cell type for uptake of non-covalent complexes into live cells. Pharmaceuticals 6: 184.
Keller et al. (2014). Transduction of proteins into Leishmania tarentolae by formation of non-covalent complexes with cell-penetrating peptides. J. Cell. Biochem. 115: 243.

Selected References:
Handbook of Cell-Penetrating Peptides, Second Edition, Ed. by Ü. Langel, CRC Taylor and Francis, Boca Raton, London, New York (2007).
Cell-Penetrating Peptides, Methods and Protocolls, Edited by Ülo Langel, Methods in Molecular Biology 683, Springer New York, Dodrecht, Heidelberg, London (2011).
Pharmaceuticals, Special Issue 'Cell penetrating Peptides' (2010-2013).
Morris et al. (2008) Cell penetrating peptides: from molecular mechanisms to therapeutics Bio.Cell 100:201.
Gros et al. (2006) A non-covalent peptide-based strategy for protein and peptide nucleic acid transduction. Biochim. Biophys. Acta 1758:384.
Lundberg et al. (2002) Positively charged DNA-binding proteins cause apparent cell membrane translocation. Biochem. Biophys. Res. Comm. 291:367.
Balayssac et al. (2006) Comparison of Penetratin and other homeodomain-derived cell-penetrating peptides: interaction in a membrane-mimicking environment and cellular uptake efficiency. Biochemistry 45:1408.
Albrizio et al. (2006) Driving force in the delivery of Penetratin conjugated G Protein fragment. J. Med. Chem. 50:1458.
Yesylevsky et al. (2009). Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers. Biophysical J. 97: 40.
Ghibaudi et al. (2005). The interaction of the cell-penetrating peptide penetratin with heparin, heparansulfates and phospholipid vesicles investigated by ESR spectroscopy. J. Peptide Sci. 11: 401.
Ryves and Harwood (2006). Use of a penetratin-linked peptide in Dictostelium. Mol. Biotech-nology 33: 123.