Glucagon-Like Peptide (GLP) II, human is a 33-amino acid peptide derived from the C-terminal of proglucagon and mainly produced by the intestinal L cells. Glucagon-Like Peptide (GLP) II, human stimulates intestinal mucosal growth and decreased apoptosis of enterocytes .
CAT No: R1385
CAS No:89750-15-2
Synonyms/Alias:89750-15-2;Glucagon-like peptide II;DTXSID50237869;DTXCID50160360;[Ala19]Glucagon-Like Peptide II, rat;FG109356;GLP-2 (1-34) (human) trifluoroacetate salt;99120-49-7;H-His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe -Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-A sp-Arg-OH; H-HADGSFSDEMNTILDNLAARDFINWLIQTKITDR-OH;
Glucagon-Like Peptide (GLP) II, human, is a biologically active peptide belonging to the glucagon peptide family, recognized for its pivotal role in gastrointestinal physiology and metabolic regulation. Structurally derived from the proglucagon gene, GLP-II is an intestinal hormone predominantly secreted by L-cells in the distal gut. Its unique sequence and receptor specificity distinguish it from other proglucagon-derived peptides, making it a valuable tool for elucidating gut hormone signaling pathways. The compound's ability to modulate intestinal growth, nutrient absorption, and mucosal integrity has established its significance in a range of basic and translational research contexts, particularly in studies focused on gastrointestinal biology, nutrient metabolism, and peptide-receptor interactions.
Peptide receptor characterization: GLP-II is widely employed in receptor-binding assays and signal transduction studies to investigate the GLP-2 receptor (GLP2R) and its downstream signaling mechanisms. By serving as a selective agonist, the peptide enables researchers to map receptor distribution in various tissues, quantify receptor affinity, and delineate the molecular pathways activated upon ligand engagement. These insights are crucial for advancing the understanding of gut hormone receptor pharmacology and for identifying novel targets within the glucagon peptide family.
Intestinal physiology research: The peptide is instrumental in exploring the regulation of intestinal epithelial growth, mucosal repair, and barrier function. Experimental models utilizing GLP-II facilitate the analysis of its trophic effects on the intestinal mucosa, including the stimulation of crypt cell proliferation and enhancement of nutrient absorption. Such studies provide foundational knowledge for deciphering the mechanisms underlying gastrointestinal adaptation to injury, resection, or altered nutrient states.
Metabolic pathway studies: GLP-II is an important tool for dissecting the interplay between gut-derived peptides and systemic metabolism. Its administration in experimental settings allows for the assessment of nutrient-driven hormonal responses, modulation of lipid and carbohydrate absorption, and the regulation of energy homeostasis. These applications support investigations into the gut's role as an endocrine organ and contribute to a broader understanding of metabolic integration at the organismal level.
Peptide synthesis and structure-activity relationship (SAR) analysis: The human form of GLP-II is frequently utilized in peptide chemistry laboratories for the development and optimization of analogs with altered stability, receptor selectivity, or bioactivity. Through systematic modification and comparative bioassays, researchers can elucidate critical structural determinants that govern peptide-receptor interactions, inform the design of novel peptide-based tools, and expand the repertoire of research reagents targeting the GLP-2 signaling axis.
Analytical and quantification assays: GLP-II serves as a reference standard in the development and validation of immunoassays, chromatographic methods, and mass spectrometry protocols aimed at quantifying endogenous peptide levels in biological samples. Its inclusion in these analytical workflows ensures assay specificity and sensitivity, enabling accurate measurement of GLP-II concentration dynamics in studies of gastrointestinal physiology, nutrient sensing, and hormonal regulation.
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