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CPP-P14 50 μg 152,25 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on blue ice

Storage Conditions: store at -20 °C
protect from light

Shelf Life: 12 months after date of delivery

Molecular Weight: 1079 Da confirmed by MALDI-MS, peptide provides 2 positive and one negative charge for complex formation. 3 trifluoroacetate residues may be present resulting in an apparent MW of 1.6 kDa.

Purity: ≥ 95 % (HPLC)

Form: powder

Solubility: water

Cys-[3-Abu-minimaurocalcine(1-9)] is a highly potent CPP isolated from Tunesian scorpion Scorpio Maurus palmatus. The full-length maurocalcine is a 33-mer basic peptide cross-linked by three disulfide bridges[1]. Many analogues have been derived by internal cysteine replacement by 2-aminobutyric acid (Abu) and by sequence truncation[2]. The fragment 1-9 matches the hydrophobic face of maurocalcine. Protonation of histidine residue renders the cell-penetration pH-sensitive. The fragment can thus be used to specifically target cancer cells because they grow in more acidic environment[2]. Maurocalcine potently and reversibly modifies channel gating behavior of the type 1 ryanodine receptor[1]. It binds to disialoganglioside GD3 at cell surface.
Cys-functionalized Minimaurocalcine allows covalent coupling of thiol reactive compounds e.g.

  • Maleimide-functionalized label (without addition of glutathione and Tris-(2-carboxy ethyl)phosphine within the labeling reaction[6]). Improved coupling with maleimide derivatives are described[7,8].
  • bromomethyl-phenyl-functionalized label[9,10]


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

Selected References:
[1] Fajloun et al. (2000) Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca2+ release channel/ryanodine receptors. FEBS Letters 469:179.
[2] Tisseyre et al. (2013) Cell penetration proprtiesof a high efficient mini maurocalcine peptide. Pharmaceuticals 6:320.
[3] Poillot et al. (2012) Small efficient cell-penetrating peptides derived from scorpion toxin Maurocalcine. J. Biol. Chem. 287:17331.
[4] Poillot et al. (2010) D-Maurocalcine, a pharmacologically inert efficient cell-penetrating peptide analogue. J. Biol. Chem. 285 (44): 34168.
[5] Perret et al. (2015) Biodistribution, stability, and blood distribution of the cell penetrating peptide Maurocalcine in mice. Int. J. Molecular Sciences 16:27730.
[6] Tansi et al. (2015) Internalization of near-infrared fluorescently labeled activatable cell-penetrating peptide and of proteins into human fibrosarcoma cell line HT-1080. J. Cell. Biochem. 116:1222.
[7] Ryan et al. (2011) Tunable reagents for multi-functional bioconjugation: reversible or permanent chemical modification of proteins and peptides by control of maleimide hydrolysis. Chem. Commun. 47:5452.
[8] Badescu et al. (2014) A new reagent for stable thiol-specific conjuagtion. Bioconjugate Chem. 25:460.
[9] Smeenk et al. (2012) Synthesis of water-soluble scaffolds for peptide cyclization, labeling and ligation. Organic Lett. 14 (5):1194.
[10] Dewkar et al. (2012) Synthesis of novel peptide linkers: simultaneous cyclization and labeling. Organic Lett. 11 (20):4708.
Tansi et al. (2019) New generation CPPs show distinct selectivity for cancer and noncancer cells J. Cell. Biochem. 120 (4):6528.