LL-37 (Human) Biotinylated, Pegylated combines the full-length human cathelicidin with PEG and biotin tags for enhanced solubility and affinity capture. The PEG segment modulates aggregation and diffusion, while biotin enables streptavidin-based immobilization. Researchers track its interactions with membranes, proteins, or nucleic acids. Applications include antimicrobial-peptide mechanism studies, binding assays, and surface-functionalization work.
CAT No: R2746
LL 37 (human) biotinylated, pegylated is a chemically modified peptide derived from the human cathelicidin antimicrobial peptide LL-37, engineered for enhanced biochemical utility through both biotinylation and pegylation. As a member of the host defense peptide family, LL-37 is recognized for its broad-spectrum antimicrobial activity and its role in modulating immune responses. The addition of a biotin tag enables precise affinity-based detection and capture, while pegylation confers improved solubility, stability, and reduced aggregation, making this conjugated peptide particularly valuable for advanced biochemical and cellular assays. These modifications expand the peptide's applicability across a range of research contexts, facilitating detailed studies of peptide function, interactions, and mechanisms in human biology.
Affinity-based detection: Biotinylated LL-37 allows for robust and specific immobilization or capture using streptavidin- or avidin-based systems, enabling sensitive detection and quantification in various assay formats. In applications such as ELISA, pull-down assays, or surface plasmon resonance, the biotin tag ensures oriented and high-affinity binding to sensor surfaces or beads, supporting precise measurement of peptide-protein interactions, ligand binding affinities, or the identification of novel binding partners relevant to innate immunity and inflammation research.
Protein-protein interaction studies: The dual modification of LL-37 with both biotin and polyethylene glycol (PEG) enables its use as a versatile probe for investigating molecular interactions in complex biological samples. Pegylation enhances the peptide's solubility and reduces nonspecific binding, which is crucial for minimizing background noise in co-immunoprecipitation or protein microarray experiments. Researchers can employ this conjugate to dissect the interactome of LL-37 in cellular extracts, elucidating its role in modulating signaling pathways, membrane-associated processes, or immune cell recruitment.
Cellular uptake and trafficking assays: Pegylated LL-37 exhibits improved resistance to proteolytic degradation and increased half-life in biological environments, making it an ideal candidate for cellular uptake studies. By leveraging the biotin tag for subsequent detection, scientists can monitor the internalization, subcellular localization, and trafficking of the peptide in various cell types. These studies yield valuable insights into the mechanisms governing peptide-mediated signaling, antimicrobial action, or modulation of host cell responses.
Peptide structure-function analysis: The availability of a biotinylated, pegylated form of LL-37 supports detailed structure-activity relationship investigations. Researchers can systematically evaluate how modifications such as pegylation influence the peptide's biological activity, membrane binding properties, or interaction with specific targets. Such studies are instrumental in understanding the determinants of LL-37's function and in guiding the rational design of next-generation antimicrobial peptides with improved pharmacological profiles.
Biosensor and diagnostic tool development: The unique combination of biotinylation and pegylation in this LL-37 derivative enables its integration into biosensor platforms and diagnostic assays. The biotin moiety facilitates stable and oriented immobilization on sensor surfaces, while pegylation enhances signal reproducibility by minimizing nonspecific adsorption. This makes the modified peptide a valuable component in the development of sensitive detection systems for biomarkers of infection, inflammation, or immune activation, supporting translational research and assay development in the field of immunology and host-pathogen interactions.
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