Lactoferrin acetate represents an acetylated protein-derived fragment used in iron-binding, redox, and structural studies. Its arrangement of basic and acidic residues contributes to folding behavior and metal coordination. The acetate form improves handling and supports solution-phase assessments. Researchers employ it across nutritional biochemistry, protein-fragment modeling, and oxidative-stress pathway exploration.
CAT No: R2208
CAS No:2828433-30-1
Synonyms/Alias:Lactoferrin acetate;2828433-30-1;GLXC-27250;Lactoferrin (17-41) (acetate);EX-A7136;LACTOFERRIN (17-41) ACETATE;G90160;H-Phe-Lys-Cys(1)-Arg-Arg-Trp-Gln-Trp-Arg-Met-Lys-Lys-Leu-Gly-Ala-Pro-Ser-Ile-Thr-Cys(1)-Val-Arg-Arg-Ala-Phe-OH 8 AcOH;
Lactoferrin acetate is a specialized derivative of the iron-binding glycoprotein lactoferrin, designed for enhanced solubility and stability in biochemical research applications. As a naturally occurring multifunctional protein, lactoferrin is known for its strong affinity for ferric ions and its involvement in a range of physiological processes, particularly those related to iron metabolism and innate immunity. The acetate form is commonly utilized to facilitate its incorporation into various experimental systems, supporting studies that demand precise control over protein structure and function. Its unique biochemical properties make it a valuable reagent for researchers investigating protein-ligand interactions, iron homeostasis, and the molecular mechanisms underlying host-pathogen dynamics.
Protein-ligand interaction studies: In molecular biology and biochemistry, lactoferrin acetate serves as a robust model for examining protein-ligand interactions, especially those involving iron chelation and release. Its well-characterized binding domains enable researchers to dissect the structural features responsible for high-affinity iron coordination. By employing this compound in in vitro assays, scientists can evaluate the effects of mutations, environmental conditions, or competitive ligands on the protein's binding kinetics and thermodynamics. These insights are critical for advancing the understanding of metalloprotein function and for the rational design of novel iron chelators or protein-based sensors.
Iron metabolism research: The acetate salt of lactoferrin is particularly useful for exploring the regulatory mechanisms of iron uptake, transport, and storage in cellular and subcellular systems. Its ability to reversibly bind ferric ions allows for controlled manipulation of iron availability in experimental models. Researchers utilize it to simulate physiological and pathological states of iron overload or deficiency, thereby elucidating the impact of altered iron homeostasis on cellular metabolism, oxidative stress, and gene expression. Such studies are instrumental in revealing the molecular basis of iron-related disorders and informing the development of targeted interventions.
Microbial interaction assays: Lactoferrin acetate is frequently employed in studies investigating the interactions between host defense proteins and microbial pathogens. Its iron-sequestering capability creates an environment of iron limitation, a condition that mimics aspects of innate immune defense. By incorporating this protein into microbial culture systems, researchers can monitor changes in microbial growth, gene expression, and virulence factor production under iron-restricted conditions. These experiments provide valuable data on microbial adaptation strategies and the role of iron-binding proteins in modulating host-microbe dynamics.
Cell culture supplementation: In cell biology, lactoferrin acetate is utilized as a functional supplement in defined media formulations to modulate iron bioavailability and influence cellular responses. Its addition can support studies on cell proliferation, differentiation, and oxidative stress management, particularly in models sensitive to iron flux. The acetate form enhances solubility and compatibility with various culture conditions, enabling reproducible experimental setups. By adjusting protein concentrations, researchers can systematically assess the effects of iron-binding proteins on cellular physiology and signaling pathways.
Analytical method development: Analytical chemists and biotechnologists leverage lactoferrin acetate as a standard or reference protein in the development and validation of assays targeting iron-binding proteins. Its defined structure and binding properties make it suitable for calibrating chromatographic, spectrophotometric, and immunoassay techniques. The compound is also valuable in method optimization for protein quantification, purity assessment, and functional characterization, supporting a wide range of research and quality control applications across the biochemical sciences.
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