LL-37
LL-37 is the cationic antimicrobial peptide encoded by the CAMP gene, a member of the cathelicidin family. Also known as CAP18, FALL-39 and cathelicidin antimicrobial peptide, it contributes to innate immune defence and to the regulation of inflammation. Browse Assay Genie's current range of LL-37 research reagents below, or read on for the biology behind the target.
LL-37 belongs to the cathelicidin family of antimicrobial peptides. Its precursor is characterised by a highly conserved N-terminal signal peptide containing a cathelin domain, followed by a structurally variable cationic antimicrobial peptide that is released from the C-terminus by extracellular proteolysis. UniProt annotation records that the protein inhibits the growth of E. coli and B. megaterium and shows haemolytic activity against human red blood cells.
The protein plays an important role in innate immune defence against viruses. Beyond its antibacterial, antifungal and antiviral activities, LL-37 functions in cell chemotaxis, the induction of immune mediators and the regulation of the inflammatory response. This breadth makes it a useful subject for studies that link host defence with immune signalling. The protein is annotated as secreted and as present in vesicles.
The gene is CAMP (cathelicidin antimicrobial peptide), and HGNC places it in the receptor ligands gene group. Aliases include CAP18, FALL39 and FALL-39, and the mouse ortholog is Camp. Researchers working with the LL-37 protein or the CAMP gene often study the full-length precursor and the processed peptide side by side, because the active peptide arises through proteolytic cleavage.
LL-37 is a cathelicidin peptide with a documented role in innate immune defence, including defence against viruses.
The peptide shows antibacterial, antifungal and antiviral activities, and inhibits the growth of E. coli and B. megaterium.
LL-37 functions in cell chemotaxis, immune mediator induction and the regulation of the inflammatory response.
The active peptide is produced from the precursor by extracellular proteolysis, which makes it a model for studying cathelicidin maturation.
LL-37 is an antimicrobial peptide with antibacterial, antifungal and antiviral activities, and it contributes to innate immune defence against viruses. It also functions in cell chemotaxis, immune mediator induction and regulation of inflammation. UniProt notes haemolytic activity against human red blood cells.
LL-37 is encoded by the CAMP gene, and its full name is cathelicidin antimicrobial peptide. Aliases include CAP18, FALL39, FALL-39 and LL37. The active peptide is produced from a larger precursor by extracellular proteolysis of the C-terminal region.
Yes. The mouse ortholog is Camp, and the protein belongs to the conserved cathelicidin family. A rat ortholog is not given in the data used here, so check the datasheet of any product for its validated reactivity.
Other antimicrobial peptides, innate immunity mediators and inflammation markers with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P49913; product specifications from Assay Genie datasheets.