GLP-2(1-33) (human) is an enteroendocrine hormone which can bind to the GLP-2 receptor and stimulate the growth of intestinal epithelium.
CAT No: R1865
CAS No:223460-79-5
Synonyms/Alias:GLP-2 (human);223460-79-5;Glucagon-like peptide 2;GLP-2 [MI];UNII-0825W549JC;1-33-Glucagon-like peptide II;GLP-2;GLP-2 (1-33);0825W549JC;GLP-2 (1-33) (human) ammonium acetate salt;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-asp;GLP-2(1-33)(human);GLP-2-ARG;AKOS024457012;DA-73760;G12301;
GLP-2 (1-33) (human) is a synthetic peptide corresponding to the full-length, biologically active form of human glucagon-like peptide-2. As a member of the proglucagon-derived peptide family, it plays a pivotal role in intestinal physiology, particularly in the regulation of nutrient absorption and mucosal growth. Its sequence and structure make it a valuable tool for probing the mechanisms underlying gut hormone signaling, epithelial cell proliferation, and nutrient homeostasis. Researchers frequently utilize this peptide to investigate enteric functions, gastrointestinal adaptation, and the molecular pathways that mediate intestinal health and disease. The availability of the human-specific sequence ensures relevance in translational studies and comparative analyses involving peptide-receptor interactions.
Peptide receptor characterization: GLP-2 (1-33) serves as a reference ligand for studies of the GLP-2 receptor (GLP2R), a G protein-coupled receptor expressed predominantly in the gastrointestinal tract. By employing this peptide in receptor binding assays, signaling pathway elucidation, and structure-activity relationship investigations, scientists can delineate receptor specificity, affinity, and downstream effector mechanisms. Such studies are essential for understanding the receptor's physiological roles and for the identification of novel modulators or antagonists that may influence GLP-2-mediated signaling.
Intestinal epithelial biology research: In vitro and ex vivo models frequently utilize GLP-2 (1-33) to assess its effects on intestinal epithelial cell proliferation, differentiation, and barrier function. The peptide's ability to stimulate crypt cell growth and enhance mucosal integrity provides a mechanistic basis for studying gut adaptation, epithelial restitution, and responses to various forms of injury or stress. These investigations contribute to a deeper understanding of the molecular events governing tissue homeostasis and regeneration within the gastrointestinal tract.
Nutrient absorption and metabolism studies: The role of GLP-2 in modulating nutrient transport and metabolic regulation is of significant interest in biochemical research. Experimental models employing this peptide enable the assessment of changes in carbohydrate, lipid, and mineral absorption, as well as the regulation of intestinal blood flow and digestive enzyme activity. Such applications support the exploration of the endocrine and paracrine actions of gut peptides in nutrient assimilation and energy balance.
Peptide stability and degradation analysis: GLP-2 (1-33) is instrumental in studies examining peptide stability, enzymatic degradation, and inactivation pathways in biological systems. Researchers use the peptide to evaluate the kinetics of cleavage by dipeptidyl peptidase IV (DPP-IV) and other proteases, providing insight into the factors that influence peptide half-life and bioavailability. These findings inform the design of analogues with improved stability and functional properties for research purposes.
Peptide synthesis and analytical validation: As a well-characterized reference peptide, GLP-2 (1-33) is commonly employed in peptide synthesis optimization, chromatographic method development, and mass spectrometric analysis. Its defined sequence and physicochemical properties make it suitable for calibrating analytical platforms, validating detection methodologies, and benchmarking synthetic protocols. These activities are crucial for ensuring reproducibility and accuracy in peptide research and development workflows.
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