L-Tyrosinamide,N-acetyl-L-leucylglycyl-L-arginyl-L-leucyl-L-seryl-L-glutaminyl-L-a-glutamyl-L-leucyl-L-histidyl-L-arginyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparaginyl-L-threonylglycyl-L-seryl-L-asparaginyl-L-threonyl- forms a complex peptide chain reflecting coordinated hydrophobic, charged, and polar influences. Its extended length provides a model for protein-like folding and multivalent interactions. Researchers use it to examine hydrogen-bond networks and domain-level conformational shifts. The sequence offers broad value in structural biology, binding studies, and peptide-based material design.
CAT No: R2432
CAS No:151804-79-4
Synonyms/Alias:L-Tyrosinamide,N-acetyl-L-leucylglycyl-L-arginyl-L-leucyl-L-seryl-L-glutaminyl-L-a-glutamyl-L-leucyl-L-histidyl-L-arginyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparaginyl-L-threonylglycyl-L-seryl-L-asparaginyl-L-threonyl-;151804-79-4;L-Tyrosinamide,N-acetyl-L-leucylglycyl-L-arginyl-L-leucyl-L-seryl-L-glutaminyl-L-a-glutamyl-L-leucyl-L-histidyl-L-arginyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparaginyl-L-threonylglycyl-L-seryl-L-asparaginyl-L-threonyl-;AKOS034834088;PD080399;
L-Tyrosinamide,N-acetyl-L-leucylglycyl-L-arginyl-L-leucyl-L-seryl-L-glutaminyl-L-a-glutamyl-L-leucyl-L-histidyl-L-arginyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparaginyl-L-threonylglycyl-L-seryl-L-asparaginyl-L-threonyl- is a complex carbohydrate-based peptide compound that embodies a sophisticated sequence of amino acids and carbohydrate moieties. This unique molecular architecture offers a versatile platform for research and development in a variety of scientific fields, owing to its intricate structure and functional groups that facilitate diverse molecular interactions. The peptide's design is tailored to enable specific binding, signaling, or structural roles in biochemical assays, making it a valuable tool for laboratories focused on investigating protein-carbohydrate interactions, enzymatic mechanisms, and cellular signaling pathways. Its solubility and stability characteristics further enhance its applicability in experimental protocols, allowing researchers to explore its properties in different assay conditions and biological environments. The presence of both hydrophilic and hydrophobic residues within the sequence provides an excellent model for studying amphipathic interactions and conformational dynamics in synthetic and biological systems.
Biochemical Assay Development: L-Tyrosinamide,N-acetyl-L-leucylglycyl-L-arginyl-L-leucyl-L-seryl-L-glutaminyl-L-a-glutamyl-L-leucyl-L-histidyl-L-arginyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparaginyl-L-threonylglycyl-L-seryl-L-asparaginyl-L-threonyl- serves as an ideal substrate or probe in the development of biochemical assays aimed at characterizing enzyme specificity, substrate affinity, and reaction kinetics. By incorporating this peptide into in vitro systems, researchers can monitor enzymatic cleavage, modification, or binding events with high sensitivity, facilitating the discovery of new enzymatic activities or the optimization of assay conditions for high-throughput screening. Its well-defined sequence enables precise mapping of enzyme-substrate interactions, which is critical for advancing our understanding of catalytic mechanisms and for the design of selective inhibitors or activators.
Cell Signaling Research: The compound's multifaceted structure makes it an effective tool for dissecting signal transduction pathways in cellular models. Scientists leverage its ability to mimic natural ligands or interact with cell-surface receptors to investigate downstream effects on cellular metabolism, gene expression, or cytoskeletal organization. By introducing this synthetic peptide into cultured cells, it is possible to delineate the roles of specific residues or motifs in receptor recognition, internalization, and signaling cascade activation, thereby contributing to the elucidation of complex regulatory networks that govern cell behavior.
Protein-Protein Interaction Studies: As a mimic of naturally occurring peptide sequences, this carbohydrate-peptide conjugate is instrumental in exploring the principles of protein-protein recognition and binding. Its sequence diversity and functional group presentation allow for systematic analysis of binding affinities, specificity, and conformational changes upon complex formation. Researchers utilize it in pull-down assays, surface plasmon resonance experiments, and co-immunoprecipitation studies to unravel the molecular determinants of protein association, which is fundamental for understanding cellular machinery and for guiding the design of novel molecular probes or therapeutics.
Structural Biology Investigations: The unique conformation adopted by L-Tyrosinamide,N-acetyl-L-leucylglycyl-L-arginyl-L-leucyl-L-seryl-L-glutaminyl-L-a-glutamyl-L-leucyl-L-histidyl-L-arginyl-L-leucyl-L-glutaminyl-L-threonyl-L-tyrosyl-L-prolyl-L-arginyl-L-threonyl-L-asparaginyl-L-threonylglycyl-L-seryl-L-asparaginyl-L-threonyl- provides an excellent model for structural biology studies, including NMR spectroscopy, X-ray crystallography, and computational modeling. By analyzing its three-dimensional structure in different environments, researchers gain insights into the folding, stability, and dynamics of complex peptide-carbohydrate assemblies. These findings inform the rational design of biomimetic materials and the engineering of peptides with tailored structural and functional properties.
Immunological Research: The compound's sequence and carbohydrate content render it valuable in immunological investigations, particularly for studying antigen recognition, epitope mapping, and immune response modulation. Scientists employ this peptide in assays designed to probe antibody specificity, T-cell activation, or immune complex formation, thereby advancing our understanding of immune surveillance and molecular recognition processes. Its use in these contexts supports the development of novel diagnostic reagents and the identification of immune-regulatory motifs relevant to basic and applied immunology.
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