H-Gly-Ser-Ser(Ac)(Ac)-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH presents a long peptide enriched with acetylated serine units that influence polarity and hydrogen-bonding patterns. Hydrophobic, aromatic, and charged residues create a multiphasic folding environment. Researchers analyze domain-level flexibility and interaction specificity. Applications span structural biology, peptide-material design, and sequence-function evaluation.
CAT No: R2642
CAS No:321974-76-9
Synonyms/Alias:H-Gly-Ser-Ser(Ac)(Ac)-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH;321974-76-9;FS110191;(Ser(Ac)3)-Ghrelin (mouse, rat) trifluoroacetate salt;H-Gly-Ser-Ser(Ac)-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser- Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH; H-GSS(Ac) FLSPEHQKAQQRKESKKPPAKLQPR-OH;
H-Gly-Ser-Ser(Ac)(Ac)-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH is a synthetic peptide featuring a unique sequence of amino acids, including acetylated serine residues, which can impart distinctive biochemical properties. Designed for advanced research purposes, this peptide offers a versatile platform for studying protein-protein interactions, signaling pathways, and post-translational modifications. The presence of multiple lysine and glutamine residues, alongside proline-rich motifs, enhances its potential for mimicking specific protein regions or modulating biological processes in vitro. Researchers value its well-defined structure for exploring molecular mechanisms in cellular models, while its sequence complexity allows for investigations into peptide stability, folding, and binding affinities. As a high-quality research compound, it is suitable for a range of biochemical and molecular biology applications, particularly those requiring precise control over peptide composition and modification.
Signal Transduction Pathway Analysis: H-Gly-Ser-Ser(Ac)(Ac)-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH serves as an effective tool for dissecting intracellular signaling pathways. Its sequence, which includes acetylated serine residues and multiple charged amino acids, can be used to probe the role of post-translational modifications in modulating kinase or phosphatase activities. By introducing the peptide into cell lysates or in vitro systems, researchers can monitor downstream signaling events, protein complex formation, or the impact of acetylation on signal propagation, thereby gaining insights into regulatory mechanisms that govern cellular responses.
Protein-Protein Interaction Studies: The synthetic peptide is highly valuable in mapping protein-protein interaction domains due to its proline-rich and lysine-enriched regions. Scientists utilize it as a bait in pulldown assays or as a competitor in binding studies to identify and characterize interacting partners. Its defined structure allows for systematic analysis of binding affinities, specificity, and competitive inhibition, supporting the elucidation of molecular recognition motifs that underlie complex biological networks.
Enzyme Substrate Characterization: As a substrate analog, this peptide is employed in enzymatic assays to investigate the specificity and catalytic efficiency of proteases, acetyltransferases, or deacetylases. The acetylated serine residues serve as recognition elements for enzymes involved in acetylation and deacetylation processes, enabling the study of enzyme kinetics, substrate preferences, and the impact of sequence context on catalysis. Such assays contribute to the development of enzyme inhibitors or modulators for research applications.
Peptide Structure and Folding Research: H-Gly-Ser-Ser(Ac)(Ac)-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH is frequently used in structural biology to analyze peptide folding, stability, and conformational dynamics. The interplay between acetylated and non-acetylated residues, along with the distribution of hydrophobic and charged amino acids, offers a model system for studying secondary structure formation, aggregation propensity, and the effects of sequence modifications on peptide behavior under various environmental conditions.
Antibody Production and Epitope Mapping: Researchers employ this synthetic peptide as an immunogen or as a tool for mapping antibody binding sites. Its unique sequence and post-translational modifications facilitate the generation of specific antibodies or the identification of linear and conformational epitopes. These applications are crucial for developing research antibodies, optimizing detection assays, or characterizing immune recognition in experimental systems.
Peptide-based Assay Development: In addition to its roles in mechanistic studies, the peptide is incorporated into assay platforms for high-throughput screening or detection purposes. Its defined sequence and modifiable residues enable the design of sensitive and specific assays for monitoring enzymatic activities, protein interactions, or post-translational modifications. By leveraging its biochemical properties, researchers can create robust and reproducible assays that advance the study of molecular and cellular processes.
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