Shaw JE, et al. Mechanisms of antimicrobial peptide action: Studies of indolicidin assembly at model membrane interfaces by in situ atomic force microscopy. J. Struct. Biol. Apr 2006; 154(1):42-58.
Xing H, et al. Increased pathogen resistance and yield in transgenic plants expressing combinations of the modified antimicrobial peptides based on indolicidin and magainin. Planta. Apr 2006; 223(5): 1024-1032.
Hsu CH, et al. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Res. Jul 2005; 33(13): 4053-4064.
Indolicidin is a 13-residue peptide amide which was isolated and characterized from the cytoplasmic granules of bovine neutrophils, having potent antibacterial activity in vitro against bacteria and fungi. The primary structure of indolicidin is characterized by 5 tryptophan residues, which is the highest mole percentage of any known protein sequence and is unique among known endogenous antibacterial peptides.
Formula
C100H132N26O13
M.W.
1906.28
Cas
140896-21-5
Purity
> 95%
Storage
Stored at -20°C. Keep tightly closed.
* For Non-Clinical Research Use Only *
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