HAEGTFT is the first N-terminal 1-7 residues of GLP-1 peptide.
CAT No: R1407
CAS No:926018-95-3
Synonyms/Alias:HAEGTFT;926018-95-3;BMB01895;HY-P1228;CS-8038;DA-64004;MS-31360;G16252;L-Histidyl-L-alanyl-L-?-glutamylglycyl-L-threonyl-L-phenylalanyl-L-threonine;(4S)-4-[[(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]propanoyl]amino]-5-[[2-[[(2S,3R)-1-[[(2S)-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-5-oxopentanoic acid;
HAEGTFT is a synthetic peptide corresponding to the N-terminal sequence of human glucagon-like peptide-1 (GLP-1), a key incretin hormone involved in glucose metabolism and insulin secretion. As a well-defined peptide fragment, HAEGTFT serves as a valuable molecular tool in the study of peptide-receptor interactions, structure-activity relationships, and peptide-based signaling pathways. Its precise amino acid sequence and structural fidelity make it particularly relevant for researchers investigating the physiological and biochemical mechanisms of GLP-1 and related peptide hormones. The availability of HAEGTFT enables controlled experimental investigations into the roles of short peptide motifs in modulating cellular responses, supporting a wide spectrum of peptide research and development efforts.
Peptide structure-function analysis: HAEGTFT is frequently used in structure-function studies to elucidate the essential structural features required for GLP-1 receptor binding and activation. By comparing the biological activity of this peptide fragment to that of full-length GLP-1 or other analogs, researchers can identify critical residues and motifs responsible for receptor specificity and downstream signaling. Such investigations contribute to a deeper understanding of peptide hormone-receptor interactions and can inform the rational design of novel peptide analogs with improved pharmacological profiles for research purposes.
Receptor binding assays: In vitro receptor binding assays utilize HAEGTFT to characterize the affinity and selectivity of GLP-1 receptor interactions. The peptide serves as a reference ligand or competitive inhibitor in binding studies, allowing researchers to quantify receptor-ligand kinetics, map binding sites, and screen for small molecule or peptide-based modulators of GLP-1 receptor function. These assays are fundamental in pharmacological research, enabling the development of new research tools and the validation of receptor-targeted compounds.
Peptide synthesis and analytical method development: The defined sequence of HAEGTFT makes it an ideal standard for calibrating peptide synthesis protocols and validating analytical methods such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its use as a reference compound ensures accuracy in peptide quantification and purity assessment, supporting quality control in peptide production and facilitating the development of robust analytical workflows in peptide chemistry laboratories.
Cell signaling studies: Researchers employ HAEGTFT to probe the intracellular signaling pathways triggered by GLP-1 receptor activation in various cell types. By administering this peptide to cultured cells expressing the GLP-1 receptor, investigators can monitor changes in second messenger levels, kinase activation, or gene expression profiles. Such studies provide mechanistic insights into the molecular events downstream of peptide hormone engagement, advancing the understanding of cell signaling dynamics in metabolic research.
Peptide-based assay development: HAEGTFT serves as a functional component in the design and optimization of peptide-based biochemical assays, including enzyme-linked immunosorbent assays (ELISAs) and biosensor platforms. Its well-characterized sequence and predictable behavior enable reliable assay calibration, sensitivity testing, and specificity assessments. Incorporating this peptide into assay development pipelines supports the creation of robust, reproducible tools for the quantitative detection of GLP-1-related peptides and the evaluation of peptide-receptor interactions in basic and applied research settings.
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