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)
Maurocalcine 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. Many analogues have been derived by internal cysteine replacement by 2-aminobutyric acid (Abu) and by sequence truncation. 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. Maurocalcine potently and reversibly modifies channel gating behavior of the type 1 ryanodine receptor. It binds to disialoganglioside GD3 at cell surface.
Cys-functionalized Minimaurocalcine allows covalent coupling of thiol reactive compounds e.g.
Perform calculation, complex formation and cargo transduction according to detailed protocols given in the general manual.
 Fajloun et al. (2000) Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca2+ release channel/ryanodine receptors. FEBS Letters 469:179.
 Tisseyre et al. (2013) Cell penetration proprtiesof a high efficient mini maurocalcine peptide. Pharmaceuticals 6:320.
 Poillot et al. (2012) Small efficient cell-penetrating peptides derived from scorpion toxin Maurocalcine. J. Biol. Chem. 287:17331.
 Poillot et al. (2010) D-Maurocalcine, a pharmacologically inert efficient cell-penetrating peptide analogue. J. Biol. Chem. 285 (44): 34168.
 Perret et al. (2015) Biodistribution, stability, and blood distribution of the cell penetrating peptide Maurocalcine in mice. Int. J. Molecular Sciences 16:27730.
 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.
 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.
 Badescu et al. (2014) A new reagent for stable thiol-specific conjuagtion. Bioconjugate Chem. 25:460.
 Smeenk et al. (2012) Synthesis of water-soluble scaffolds for peptide cyclization, labeling and ligation. Organic Lett. 14 (5):1194.
 Dewkar et al. (2012) Synthesis of novel peptide linkers: simultaneous cyclization and labeling. Organic Lett. 11 (20):4708.