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Melittin

*This product has been discontinued!*
This 26-residue polypeptide isolated from bee venom binds calmodulin in a Ca2+-dependent manner, activates phospholipase A2, and inhibits protein kinase C (IC50=5-7 mM) by binding to the catalytic domain in a Mg-ATP-sensitive manner.
RP10290
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Overview
Description This 26-residue polypeptide isolated from bee venom binds calmodulin in a Ca2+-dependent manner, activates phospholipase A2, and inhibits protein kinase C (IC50=5-7 mM) by binding to the catalytic domain in a Mg-ATP-sensitive manner.
Cas No 20449-79-0
Sequence
{GLY}{ILE}{GLY}{ALA}{VAL}{LEU}{LYS}{VAL}{LEU}{THR}{THR}{GLY}{LEU}{PRO}{ALA}{LEU}{ILE}{SER}{TRP}{ILE}{LYS}{ARG}{LYS}{ARG}{GLN}{GLN}-NH2
Sequence Shortening GIGAVLKVLTTGLPALISWIKRKRQQ-NH2
Molecular Formula C131H229N39O31
C Terminal NH2
Molecular Weight 2846.46
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Properties
Purity > 95%
Form Lyophilized
Storage Store at -20°C
Note Polypeptide from honey bee venom
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Citations
El Shazely B, et al. Resistance Evolution Against Antimicrobial Peptides in Staphylococcus aureus Alters Pharmacodynamics Beyond the MIC. Front Microbiol. (2020)
EbbensgaardAnna, et al. The Role of Outer Membrane Proteins and Lipopolysaccharides for the Sensitivity of to Antimicrobial Peptides. Front Microbiol. (2018)
EbbensgaardAnna, et al. Comparative Evaluation of the Antimicrobial Activity of Different Antimicrobial Peptides against a Range of Pathogenic Bacteria. PLoS ONE. (2015)