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LL-37 is a cationic α-helical peptide expressed in human bone marrow, testis, granulocytes, and gingival epithelium and a variety of immune cells.1 It has antimicrobial and antiviral activity, and protein levels of LL-37 are increased in epithelial cells, macrophages, and neutrophils following bacterial infection in vitro.1,2,3,4 LL-37 can be citrullinated by protein arginine deiminase 2 (PAD2) and PAD4, a modification that reduces its antibacterial and antiviral activities.5 Citrullinated, unlike native, LL-37 does not prevent mortality in a mouse model of D-galactosamine-sensitized endotoxic shock.6 Citrullinated LL-37 has been found in neutrophil extracellular traps (NETs), as well as the serum of patients with rheumatoid arthritis (RA) and individuals without RA.7 Cayman's Citrullinated LL-37 Monoclonal Antibody (Clone 6A8) can be used for ELISA and Western blot (WB) applications. The antibody recognizes citrullinated LL-37 at approximately 9 kDa from human samples.
WARNING This product is not for human or veterinary use.
1. Epithelial antimicrobial peptides: Review and significance for oral applications. Crit. Rev. Oral Biol. Med. 9(4), 399-414 (1998).
2. Expression of cathelicidin LL-
3. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-
4. A new sulfonated tetrazolium salt that produces a highly water-
5. Citrullination alters the antiviral and immunomodulatory activities of the human cathelicidin LL-
6. Citrullination alters immunomodulatory function of LL-
7. A novel biological role for peptidyl-