H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Pro-Pro-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-NH2 is a highly cationic peptide enriched in arginine and lysine residues. The sequence mimics nuclear localization signal patterns and can strongly associate with nucleic acids or acidic proteins. Researchers investigate its cell-penetrating potential and condensation behavior. Applications include delivery-vector design, chromatin interaction models, and peptide-DNA complex studies.
CAT No: R2585
CAS No:1220985-78-3
Synonyms/Alias:H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Pro-Pro-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-NH2;DT-2;EX-A9120;1220985-78-3;
H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Pro-Pro-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-NH2 is a synthetic peptide featuring a sequence rich in basic amino acids, making it an attractive tool for a variety of biochemical and molecular research applications. The arrangement of tyrosine, glycine, multiple arginine and lysine residues, along with glutamine, proline, leucine, and histidine, imparts unique physicochemical properties, including strong cationic charge and potential for diverse molecular interactions. Researchers value this peptide for its ability to participate in protein-protein interaction studies, its potential as a substrate or modulator in enzymatic assays, and its utility in cell biology investigations. Due to its tailored sequence, it can be incorporated into experimental workflows requiring high specificity or affinity for negatively charged biomolecules, such as nucleic acids or membrane components. The peptide's terminal amidation further enhances its stability and resistance to proteolytic degradation, making it suitable for extended in vitro applications and mechanistic studies.
Protein-Protein Interaction Analysis: H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Pro-Pro-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-NH2 is frequently utilized in the analysis of protein-protein interactions, particularly those involving recognition of polybasic motifs. Its sequence enables researchers to probe the binding specificity and affinity of protein domains, such as SH3 or WW domains, that interact with positively charged peptide regions. By incorporating this peptide into pull-down assays or surface plasmon resonance experiments, scientists can dissect the molecular determinants of recognition and binding, shedding light on the structural requirements for these critical cellular interactions.
Nucleic Acid Binding Studies: The high density of arginine and lysine residues in this peptide makes it an effective model for investigating peptide-nucleic acid interactions. Its strong cationic nature facilitates electrostatic binding to negatively charged DNA or RNA molecules, allowing researchers to study the mechanisms of nucleic acid condensation, protection, or delivery. In electrophoretic mobility shift assays or fluorescence-based binding studies, this peptide serves as a probe to evaluate the influence of polybasic sequences on nucleic acid structure and function, which is valuable for understanding gene regulation and the design of nucleic acid delivery systems.
Cell Penetrating Peptide Research: Owing to its rich content of basic amino acids, this peptide is often explored as a cell-penetrating peptide (CPP) or as a component in the development of novel CPPs. Its ability to traverse cellular membranes enables its use in delivering molecular cargo into cells, including proteins, nucleic acids, or small molecules. Researchers employ this peptide in uptake assays, confocal microscopy, or flow cytometry experiments to quantify and visualize cellular internalization, providing insights into the mechanisms governing membrane translocation and intracellular trafficking.
Enzyme Substrate and Inhibitor Studies: The unique sequence of H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Pro-Pro-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-NH2 makes it a valuable substrate or competitive inhibitor in enzyme assays, particularly those involving proteases or kinases that recognize basic motifs. By monitoring the peptide's cleavage or modification in vitro, scientists can assess enzyme specificity, catalytic efficiency, and inhibition kinetics. This application is instrumental in the characterization of novel enzymes, the screening of small molecule inhibitors, or the validation of biochemical pathways implicated in cellular regulation.
Immunological and Epitope Mapping Research: The presence of multiple arginine and lysine residues within this peptide sequence provides opportunities for immunological studies, particularly in the context of epitope mapping or antibody generation. It can be used to identify antibody binding sites, assess cross-reactivity, or evaluate the immunogenic potential of polybasic motifs. In ELISA, western blotting, or peptide array assays, this peptide enables the detailed characterization of immune recognition, supporting the development of diagnostic tools or the exploration of immune signaling mechanisms.
Peptide-based Delivery System Development: Researchers investigating advanced delivery systems often turn to polybasic peptides such as this one for their ability to facilitate the transport of bioactive molecules across biological barriers. By conjugating this peptide to drugs, nanoparticles, or imaging agents, scientists can enhance cellular uptake and targeting efficiency in vitro. Its sequence serves as a platform for optimizing carrier design, evaluating delivery efficacy, and understanding the interplay between peptide structure and transport properties. Collectively, these diverse applications underscore the scientific value of H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Pro-Pro-Leu-Arg-Lys-Lys-Lys-Lys-Lys-His-NH2 in advancing research across molecular biology, biochemistry, and biotechnology disciplines.
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