GenScript Catalog Peptide: Indolicidin (RP11242)

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.

Full Name

Indolicidin

Alias

ILPWKWPWWPWRR-NH2

Sequence
(one-letter code)

ILPWKWPWWPWRR-NH₂

Sequence
(three-letter code)

{ILE}{LEU}{PRO}{TRP}{LYS}{TRP}{PRO}{TRP}{TRP}{PRO}
{TRP}{ARG}{ARG}-NH₂

C-Terminal

NH₂

Description

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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