LL-37 Monoclonal Antibody (Clone 3G10)

LL-37 is a cationic α-helical peptide expressed in human bone marrow, testis, granulocytes, gingival epithelium, and a variety of immune cells.¹ It is produced by proteolytic cleavage of the cathelicidin human cationic antimicrobial protein of 18 kDa (hCAP18).² LL-37 has antimicrobial and antiviral activity, and protein levels of LL-37 are increased in epithelial cells, macrophages, and neutrophils following bacterial infection in vitro.^1,3,4,5 It functions as a chemoattractant for human monocytes, neutrophils, and T cells, and induces chemokine secretion from epithelial cells in infected tissues.^6,2 LL-37 is a component of LPS-induced neutrophil extracellular traps (NETs) produced from human neutrophils isolated from patients with systemic lupus erythrematosus (SLE) or individuals without SLE.⁷ It also enhances formation of NETs induced by phorbol 12-myristate 13-acetate (PMA) or S. aureus.⁸ LL-37 can be citrullinated by protein arginine deiminase 2 (PAD2) and PAD4, a modification that reduces its antibacterial and antiviral activities.^9,5 Native, but not citrullinated, LL-37 prevents mortality in a mouse model of D-galactosamine-sensitized endotoxic shock.⁹ Cayman's LL-37 Monoclonal Antibody (Clone 3G10) can be used for ELISA and flow cytometry (FC) applications.

WARNING This product is not for human or veterinary use.

1. Weinberg, A., Krisanaprakornkit, S., and Dale, B.A. Epithelial antimicrobial peptides: Review and significance for oral applications. Crit. Rev. Oral Biol. Med. 9(4), 399-414 (1998).

2. Méndez-Samperio, P. The human cathelicidin hCAP18/LL-37: A multifunctional peptide involved in mycobacterial infections. Peptides 31(9), 1791-1798 (2010).

3. Rivas-Santiago, B., Hernandez-Pando, R., Carranza, C., et al. Expression of cathelicidin LL-37 during Mycobacterium tuberculosis infection in human alveolar macrophages, monocytes, neutrophils, and epithelial cells. Infect. Immun. 76(3), 935-941 (2008).

4. Gudmundsson, G.H., Agerberth, B., Odeberg, J., et al. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238(2), 325-332 (1996).

5. Casanova, V., Sousa, F.H., Shakamuri, P., et al. Citrullination alters the antiviral and immunomodulatory activities of the human cathelicidin LL-37 during rhinovirus infection. Front. Immunol. 11, 85 (2020).

6. Yang, B.D., Chen, Q., Schmidt, A.P., et al. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192(7), 1069-1074 (2000).

7. Kahlenberg, J.M., Carmona-Rivera, C., Smith, C.K., et al. Neutrophil extracellular trap-associated protein activation of the NLRP3 inflammasome is enhanced in lupus macrophages. J. Immunol. 190(3), 1217-1226 (2013).

8. Neumann, A.W., Berends, E.T.M., Nerlich, A., et al. The antimicrobial peptide LL-37 facilitates the formation of neutrophil extracellular traps. Biochem. J. 464(1), 3-11 (2014).

9. Koziel, J., Bryzek, D., Sroka, A., et al. Citrullination alters immunomodulatory function of LL-37 essential for prevention of endotoxin-induced spesis. J. Immunol. 192(11), 5363-5372 (2014).