LL 37 CAS NO.154947-66-7

LL-37 Basic information
Structure
Product Name:    LL-37
Synonyms:    Antibacterial Protein LL-37 (huMan), LL37, CAMP;H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH;Antibacterial Protein LL-37 (human);LL-37 (trifluoroacetate salt);LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES;Cathelicidin LL 37 (human);LL-37, LL37, CAMP;LL-37 human acetate
CAS:    154947-66-7
MF:    C205H340N60O53
MW:    0
EINECS:    211-519-9
Product Categories:    
Mol File:    Mol File

LL-37 Chemical Properties
solubility     Water: 1 mg/ml
form     A lyophilized powder
Water Solubility     Soluble to 1 mg/ml in water
InChIKey    POIUWJQBRNEFGX-XAMSXPGMSA-N
Safety Information
MSDS Information
LL-37 Usage And Synthesis
Structure    The structure of LL-37 in SDS micelles is composed of a curved amphipathic helix-bend-helix motif spanning residues 2–31 followed by a disordered C-terminal tail. The helical bend is located between residues Gly-14 and Glu-16. Similar chemical shifts and 15N nuclear Overhauser effect (NOE) patterns of the peptide in complex with di octanoyl phosphatidylglycerol (D8PG) micelles indicate a similar structure. The aromatic rings of Phe-5, Phe-6, Phe-17, and Phe-27 of LL-37, as well as arginines, showed intermolecular NOE cross-peaks with D8PG, providing direct evidence for the association of the entire amphipathic helix with anionic lipid micelles. The structure of LL-37 serves as a model for understanding the structure and function relationship of homologous primate cathelicidins[5].
Description    LL-37, Human acetate is a 37-residue, amphipathic, cathelicidin-derived antimicrobial peptide, which exhibits a broad spectrum of antimicrobial activity.
Uses    L 37 (human) is a 37 amino acid host defense peptide originating from the C-terminal of the human cathelicidin antimicrobial peptide (CAMP, hCAP18). This peptide possesses antimicrobial, antitumor, antiviral, and immunomodulatory properties, along with physiological functions in chemotaxis, wound healing, and angiogenesis. Beyond its antimicrobial capabilities, LL 37 (human) influences various pathways in autoimmune and inflammatory diseases, playing a role in the development of lupus, rheumatoid arthritis, and atherosclerosis. As a binding partner to Aβ42, the expression of LL 37 (human) affects the onset and progression of Alzheimer's disease. Additionally, LL 37 has a notable role in human cancer, promoting tumorigenic effects in ovarian, lung, breast, prostate, pancreatic cancers, and malignant melanoma.
Origin    Mammalian AMPs belong to the defensin and cathelicidin families. So far, there is a unique cathelicidin peptide found in 1995 and called human cationic antimicrobial peptide (hCAP18). Its active part starts with double leucine and consists of 37-amino acids at the C-terminus, so which is called LL-37.
benefits    LL-37 is an important part of the human immune system, which can resist various pathogens. A plethora of experiments have demonstrated that it has the multifunctional effects of immune regulation, in addition to antimicrobial activity.  Significantly boosts immune function; Fights inflammation; Prevents cancer progression; Accelerates wound healing; Lowers the risk of heart disease; Prevents lung injury; Promotes bone repair.