LC-LL-37, biotinylated

Product Name: LC-LL-37, biotinylated

Sequence One Letter Code: Biotin-LC-LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES

Sequence Three Letter Code: Biotin-LC-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

Molecular Weight: 4833

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Inflammation and Immunology Research

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: LC-LL-37 is a biotinylated form of the human antimicrobial peptide LL-37, a member of the cathelicidin family involved in innate immunity. LL-37 exhibits broad-spectrum antimicrobial and immunomodulatory activities and participates in wound healing processes. Biotinylation enables affinity-based detection, pull-down assays, and interaction profiling without significantly altering core peptide properties. This reagent supports research on host defense mechanisms, antimicrobial peptide biology, immune modulation, and protein–ligand interaction studies.

Current Research: LL-37 is the only human cathelicidin-derived antimicrobial peptide and a central effector of innate immunity. Generated by proteolytic processing of the precursor protein hCAP-18, LL-37 is a 37-residue, amphipathic α-helical peptide with broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria, fungi, and certain enveloped viruses. Beyond its direct microbicidal properties, LL-37 modulates immune signaling, chemotaxis, cytokine production, and wound repair processes. LC-LL-37 is a biotinylated derivative of LL-37 incorporating a long-chain (LC) spacer to enable affinity-based applications while preserving functional characteristics. The long-chain biotin modification is designed to minimize steric interference with the peptide’s membrane-binding and receptor-interacting surfaces. LL-37 exerts its antimicrobial activity through electrostatic interaction with negatively charged microbial membranes, followed by membrane insertion and disruption. It also engages host receptors such as formyl peptide receptor 2 (FPR2/ALX), P2X7, and toll-like receptor-associated pathways, influencing chemotaxis, inflammatory responses, and immune cell activation. The LC spacer spatially separates the biotin moiety from the active peptide core, reducing the likelihood of disrupting these biologically relevant interactions. LC-LL-37 is widely used in affinity capture and interaction profiling studies. The high-affinity interaction between biotin and streptavidin enables immobilization of the peptide on solid supports, facilitating pull-down assays to identify binding partners. These partners may include microbial surface components, host cell receptors, nucleic acids, or extracellular matrix proteins. Subsequent detection via immunoblotting or mass spectrometry supports mapping of LL-37–associated signaling complexes and elucidation of its diverse functional roles. In antimicrobial research, LC-LL-37 enables visualization and quantification of peptide binding to microbial cells. Streptavidin-conjugated fluorescent probes allow microscopy-based tracking of peptide–bacteria interactions, providing insight into membrane targeting and permeabilization mechanisms. Such studies clarify how LL-37 discriminates between microbial and host membranes and how modifications influence antimicrobial potency. The peptide also supports investigation of LL-37’s immunomodulatory activities. LL-37 enhances chemotaxis of neutrophils, monocytes, and T cells and modulates cytokine production in epithelial and immune cells. Using LC-LL-37 in receptor-binding assays or cell-based stimulation experiments enables identification of signaling pathways activated upon peptide engagement. Affinity purification strategies can further reveal intracellular interactors following peptide internalization. LL-37 is implicated in wound healing through promotion of angiogenesis, epithelial migration, and re-epithelialization. Biotinylated LC-LL-37 facilitates studies examining interactions with growth factors, matrix components, and cell surface integrins involved in tissue repair. By enabling precise detection and quantification, the reagent supports mechanistic analysis of how LL-37 integrates antimicrobial defense with regenerative signaling. In studies of host–pathogen interactions, LC-LL-37 is employed to assess binding to bacterial lipopolysaccharide (LPS), lipoteichoic acid, and viral envelopes. Its biotin label allows competitive binding experiments to determine how microbial factors or inhibitors affect peptide association. These approaches are valuable in developing peptide-based therapeutics or understanding resistance mechanisms. Importantly, biotinylation does not significantly alter the peptide’s core physicochemical properties when appropriately designed with a long-chain spacer. This preserves its amphipathic structure and biological activity while adding versatility for detection and capture. In summary, LC-LL-37 is a biotinylated form of the human antimicrobial peptide LL-37 engineered for affinity-based applications. By enabling sensitive detection, pull-down assays, and interaction profiling, it serves as a powerful tool for studying innate immune defense, antimicrobial mechanisms, immunomodulatory signaling, and host–pathogen interactions.