Bioactive region of the LL-37 peptide, also known as FK-13
Catalogue number crb1000035 Molecular Weight 1719.09 Sequence (one letter code) FKRIVQRIKDFLR-acid Sequence (three letter code) H-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-OH Molecular Weight 1719.09 Purity >95% Storage - 20 ° C References
Sol et al (2015) Interaction of the core fragments of the LL-37 host defense peptide with actin. RSC Adv. 5(13) 9361 PMID: 26726303
Li et al (2006) Solution Structures of Human LL-37 Fragments and NMR-Based Identification of a Minimal Membrane-Targeting Antimicrobial and Anticancer Region. JACS 128(17) 5776 PMID: 16637646
esidues 17-29 of the LL-37 peptide, also known as FK-13. FK-13 has near-similar anti-microbial and anti-cancer properties to LL-37. This core fragment also contains part of the LL-37 actin binding domain and can associate weakly with actin, actin binding protects this fragment from protease degradation.
LL-37 is a member of the large cationic family of anti-microbial peptides called cathelicidins which have broad-spectrum anti-microbial activity and are expressed in many species. The only cathelicidin found in humans is LL-37; this is produced in epithelial cells, by proteolytic cleavage from the C‑terminal of the hCAP-18 protein. LL-37 can be processed into several different forms of anti-microbial peptides. As well as its anti-microbial properties LL-37 also has anti-cancer properties and regulates many aspects of the innate immune system; overexpression of LL-37 has been linked to autoimmune diseases such as asthma and psoriasis