LL-37 acid


  • Description

  • Application Data


Broad-spectrum anti-microbial activity. Produced in human epithelial cells.

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Application Data

Catalogue number crb1000007
Molecular Weight 4490.6
Sequence (one letter code)


Sequence (three letter code)


Aliase hCAP18
Purity >95%
Storage - 20 ° C

Singh et al., (2014). LL-37 Peptide Enhancement of Signal Transduction by Toll-like Receptor 3 Is Regulated by pH. J. Biol. Chem. 289(40) 27614 PMID: 25092290


Tripathi et al., (2014). LL-37 modulates human neutrophil responses to influenza A virus. J. Leukoc. Biol. 96(5) 931 PMID: 25082153


Roth et al., (2020). LL-37 fights SARS-CoV-2: The Vitamin D-Inducible Peptide LL-37 Inhibits Binding of SARS-CoV-2 Spike Protein to its Cellular Receptor Angiotensin Converting Enzyme 2 In Vitro. Preprint. doi: https://doi.org/10.1101/2020.12.02.408153

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

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 different forms of anti-microbial peptides. As well as its anti-microbial properties LL-37 also regulates many aspects of the innate immune system and overexpression of LL-37 has been linked to autoimmune diseases such as asthma and psoriasis, making LL-37 the most studied form of the human cathelicidin peptides.

More recently, studies have shown that LL-37 binds to SARS-CoV-2 S protein and inhibits binding to its receptor hACE2, which may inhibit viral entry into the cell. LL-37 is upregulated by vitamin D, therefore this may be one mode of action for the positive outcomes seen with vitamin D treatment for Covid-19.

LL-37 acid

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