GLP2-T
In Stock & Ready to Ship from USA
FREE shipping on orders over $200
Secure checkout via encrypted payment processor
Research Use Only
These products are for laboratory research only and not intended for medical use. They are not FDA-approved to diagnose, treat, cure, or prevent any disease. By purchasing, you certify they will be used solely for research and not for human or animal consumption.
Research Summary
12 PubMed CitationsOverview GLP-2 Analog (Teduglutide; ALX-0600) is a 33-amino-acid recombinant analog of human glucagon-like peptide-2 (GLP-2) originally engineered by Drucker and colleagues to extend the very short circulating half-life of native GLP-2 (~7 minutes) by substituting glycine for alanine at position 2, the canonical dipeptidyl-peptidase-IV (DPP-IV) cleavage site. The single Ala²Gly substitution renders the peptide resistant to N-terminal proteolysis while preserving full agonist activity at the GLP-2 receptor (GLP-2R), extending the in vivo functional half-life by roughly an order of magnitude in preclinical pharmacokinetic studies.[1][2] The native GLP-2 peptide is co-secreted with GLP-1 from intestinal L-cells in response to luminal nutrients and acts in a paracrine fashion on neighboring enterocytes, sub-epithelial fibroblasts, and enteric neurons expressing the Gαs-coupled GLP-2 receptor. The biological signature studied in preclinical models centers on intestinotrophic readouts: increased villus height, increased crypt depth, expanded small-bowel mucosal mass, and changes in nutrient-transport capacity in rodent and large-animal models...
GLP2-T — Research Data at a Glance
| Property | Value |
|---|---|
| Molecular Formula | C164H252N44O55S |
| Molecular Weight | 3752.1 Da |
| CAS Number | 197922-42-2 |
| Amino Acid Sequence | His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-A... |
| PubMed Citations Referenced | 12 |
| Contributing Researchers | 2 |
| Storage Conditions | Store at 2–8°C (refrigerated). |
| Purity Standard | ≥99% (HPLC verified, 3rd-party COA) |
| Research Use Only | Not for human consumption. RUO only. |
Overview
Overview
GLP-2 Analog (Teduglutide; ALX-0600) is a 33-amino-acid recombinant analog of human glucagon-like peptide-2 (GLP-2) originally engineered by Drucker and colleagues to extend the very short circulating half-life of native GLP-2 (~7 minutes) by substituting glycine for alanine at position 2, the canonical dipeptidyl-peptidase-IV (DPP-IV) cleavage site. The single Ala²Gly substitution renders the peptide resistant to N-terminal proteolysis while preserving full agonist activity at the GLP-2 receptor (GLP-2R), extending the in vivo functional half-life by roughly an order of magnitude in preclinical pharmacokinetic studies.[1][2]
The native GLP-2 peptide is co-secreted with GLP-1 from intestinal L-cells in response to luminal nutrients and acts in a paracrine fashion on neighboring enterocytes, sub-epithelial fibroblasts, and enteric neurons expressing the Gαs-coupled GLP-2 receptor. The biological signature studied in preclinical models centers on intestinotrophic readouts: increased villus height, increased crypt depth, expanded small-bowel mucosal mass, and changes in nutrient-transport capacity in rodent and large-animal models of small-bowel resection and parenteral-nutrition dependence.[3][4]
Discovery and design rationale
Drucker and colleagues at the University of Toronto first reported GLP-2's intestinotrophic activity in 1996 after observing dramatic small-bowel hyperplasia in mice bearing GLP-2-secreting glucagonoma xenografts. Mapping the active sequence to the proglucagon-derived 33-mer launched a structure-activity program that identified the Ala²Gly substitution as the minimum modification needed to confer DPP-IV resistance. The resulting analog (h[Gly²]GLP-2; teduglutide) became the prototype for the GLP-2-receptor research-peptide class.[1]
Research framework
Within the gut-tropic research-peptide family, teduglutide is most directly compared with BPC-157 (a 15-mer derived from gastric juice studied in mucosal-integrity and angiogenesis assays) and KPV (an α-MSH C-terminal tripeptide studied in intestinal inflammation models). Teduglutide is the only member of this set that engages a defined Gαs-coupled receptor (GLP-2R) on the intestinal epithelium itself, supplying investigators with a tool that isolates GLP-2R-mediated mucosal-growth signaling from the broader cytokine, prostaglandin, and angiogenesis pathways activated by the gastric-juice peptides.[5][6]
Mechanism of Action
Mechanism of Action
Primary Target: The GLP-2 Receptor (GLP-2R)
Teduglutide acts as a full agonist at the GLP-2 receptor, a class B (secretin-family) Gαs-coupled GPCR expressed predominantly on intestinal sub-epithelial myofibroblasts, enteric neurons, and a subset of enteroendocrine cells. Receptor occupancy elevates intracellular cAMP and triggers downstream protein-kinase-A signaling, which has been mapped in primary cell and explant studies to (a) release of insulin-like growth factor-1 (IGF-1) from sub-epithelial fibroblasts, (b) release of keratinocyte growth factor (KGF), and (c) modulation of vasoactive intestinal peptide (VIP) and nitric oxide tone in enteric neurons.[2][7]
DPP-IV Resistance and Pharmacokinetic Profile
The Ala²Gly substitution that defines teduglutide eliminates the canonical DPP-IV cleavage site at the N-terminal His-Ala dipeptide. In rodent pharmacokinetic studies, the in-vivo half-life of teduglutide is ~2 hours after subcutaneous administration, compared with ~7 minutes for native GLP-2. This extended exposure window allowed investigators to study sustained GLP-2R activation in chronic dosing models — a regime that is mechanistically inaccessible with native peptide because of rapid enzymatic degradation.[1][8]
Indirect Trophic Cascade — Cellular Cross-Talk
A central mechanistic finding from the GLP-2R research literature is that the receptor is not expressed on the intestinal stem cells or enterocytes whose proliferation increases. Instead, GLP-2R activation on sub-epithelial fibroblasts and enteric neurons triggers paracrine release of IGF-1 and KGF, which act on stem-cell and transit-amplifying compartments in the crypt. IGF-1-receptor knockout mice show abolished intestinotrophic response to teduglutide, providing a clean genetic dissection of the mechanism.[7]
Mucosal Growth Endpoints in Preclinical Models
| Endpoint | Direction | Model Context |
|---|---|---|
| Small-bowel mass | Increased | Rodent intestinal-resection and parenteral-nutrition models[3] |
| Villus height | Increased | Histomorphometric analysis of jejunal mucosa[4] |
| Crypt depth | Increased | BrdU labeling of crypt proliferative compartment[7] |
| Enterocyte apoptosis | Decreased | TUNEL staining in colitis and ischemia models[9] |
| Tight-junction protein expression | Increased | ZO-1 / occludin Western blot in barrier-permeability models[9] |
Receptor Selectivity
Teduglutide exhibits high selectivity for the GLP-2R; binding studies show no measurable cross-reactivity with the GLP-1, GIP, glucagon, or secretin receptors at concentrations relevant to GLP-2R activation, supplying investigators with a clean GLP-2R-selective probe within the proglucagon-derived peptide family.[2]
Research Applications
Research Applications
Teduglutide is studied in preclinical models that probe GLP-2R biology and intestinal-epithelial growth-control mechanisms. Reported research applications include:
- GLP-2R Pharmacology Profiling — Used as a high-affinity, DPP-IV-resistant agonist probe to characterize GLP-2R density, downstream cAMP/PKA coupling, and receptor desensitization kinetics in primary intestinal-fibroblast cultures, enteric-neuron preparations, and recombinant cell-line systems. The extended half-life relative to native GLP-2 makes teduglutide the standard tool for sustained-activation experiments.[2]
- Intestinal-Resection / Short-Bowel Preclinical Models — Rodent and large-animal models of massive small-bowel resection are used to study compensatory mucosal hyperplasia and the IGF-1-mediated paracrine cascade that underlies it. Endpoints include villus height, crypt depth, mucosal mass, and citrulline as a biomarker of enterocyte mass.[3][10]
- IGF-1 / KGF Paracrine-Cascade Dissection — IGF-1-receptor and KGF-receptor knockout and conditional-deletion lines are exposed to teduglutide to map which downstream growth-factor signals are required for which intestinotrophic endpoints. These studies have established that the IGF-1 axis is required for crypt proliferation, while KGF contributes to brush-border maturation.[7]
- Inflammatory Bowel Disease (IBD) Models — DSS-colitis, TNBS-colitis, and IL-10-knockout mouse models have been used to study GLP-2R-mediated effects on epithelial barrier integrity, tight-junction protein expression, and pro-inflammatory cytokine profiles.[9]
- Intestinal Ischemia-Reperfusion Investigation — Models of mesenteric ischemia-reperfusion injury are used to study GLP-2R activation as a determinant of enterocyte apoptosis, mucosal-permeability recovery, and bacterial-translocation endpoints.[11]
- Parenteral-Nutrition-Associated Mucosal Atrophy Research — Total-parenteral-nutrition (TPN) rodent models reproducibly induce villus atrophy and barrier dysfunction; teduglutide exposure in these models is used to dissect how luminal nutrient deprivation interacts with GLP-2R signaling.[10]
- Nutrient-Absorption Capacity Profiling — Ussing-chamber and isolated-perfused-intestine preparations are used to quantify glucose, amino-acid, and water transport changes following GLP-2R activation, isolating absorptive-capacity changes from raw mucosal-mass changes.[4]
- Tight-Junction and Barrier-Function Assays — In-vitro Caco-2 monolayer and ex-vivo intestinal-explant systems are used to study GLP-2R-mediated changes in ZO-1, occludin, and claudin-family proteins relevant to epithelial-barrier research.[9]
Comparative Research Context
Within the gut-tropic and mucosal-integrity research-peptide family, investigators routinely compare teduglutide head-to-head with BPC-157 (gastric-juice-derived 15-mer studied in angiogenesis and mucosal-integrity assays), KPV (α-MSH C-terminal tripeptide studied in intestinal-inflammation models), and thymosin-alpha-1 (immunomodulatory 28-mer studied in mucosal-immunity models). Teduglutide is the GLP-2R-selective member of this comparator set: it isolates one defined receptor-driven trophic pathway from the broader cytokine, prostaglandin, growth-factor, and angiogenesis programs activated by the other peptides.[6]
Biochemical Characteristics
| Property | Value |
|---|---|
| Formula | C164H252N44O55S |
| Molecular Weight | 3752.1 Da |
| Synonyms | Teduglutide, GLP-2 Analog, ALX-0600, Gattex, Revestive |
| Cas Number | 197922-42-2 |
| Sequence | 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 |
| Pubchem Cid | 16133828 |
| Monoisotopic Mass | N/A |
| Polar Area | N/A |
| Complexity | N/A |
| X Log P | N/A |
| Heavy Atom Count | N/A |
| H Bond Donor Count | N/A |
| H Bond Acceptor Count | N/A |
| Rotatable Bond Count | N/A |
Identifiers
| Pubchem Cid | |
|---|---|
| Inchi Key | |
| Inchi | |
| Smiles Isomeric | |
| Smiles Canonical | |
| Iupac Name |
Preclinical Research Summary
Preclinical Research Summary
Foundational Studies
| Study | Model | Key Findings | Ref |
|---|---|---|---|
| Drucker et al. (1996) | Glucagonoma xenograft mice | First identification of GLP-2 intestinotrophic activity; small-bowel hyperplasia mapped to the 33-mer proglucagon-derived peptide | [1] |
| Drucker et al. (1997) | Mouse pharmacokinetic / structure-activity | Ala²Gly substitution confers DPP-IV resistance; in-vivo half-life extended ~10× vs native GLP-2 with full agonist activity preserved | [2] |
| Munroe et al. (1999) | GLP-2R cloning and characterization | Identified the GLP-2R as a class B Gαs-coupled GPCR; characterized receptor distribution across intestinal cell populations | [5] |
| Dubé et al. (2006) | IGF-1R conditional-knockout mice | Established that the intestinotrophic response to teduglutide requires intact IGF-1R signaling on intestinal epithelial cells | [7] |
| Boushey et al. (1999) | DSS-colitis mice | Reduced histological injury scores; preserved barrier integrity; reduced enterocyte apoptosis vs vehicle | [9] |
| Burrin et al. (2005) | Neonatal piglet TPN model | GLP-2 / teduglutide preserved villus height and mucosal mass during prolonged parenteral nutrition | [10] |
| Prasad et al. (2000) | Rat mesenteric ischemia-reperfusion | Reduced apoptosis index, improved barrier-recovery kinetics post-reperfusion | [11] |
| Cheeseman & Tseng (1996) | Rat jejunal Ussing-chamber | GLP-2R activation increased apical SGLT1-mediated glucose-transport capacity independent of mucosal-mass change | [4] |
Mechanistic Themes
- DPP-IV-resistant pharmacokinetics — single Ala²Gly substitution underwrites the entire research utility of the molecule
- Indirect trophic action — GLP-2R is not on the proliferating cell; IGF-1 and KGF carry the signal from receptor-bearing fibroblasts to crypt stem cells
- Receptor selectivity — clean GLP-2R-selective probe within the proglucagon-derived peptide family
- Reproducible morphometric endpoints — villus height, crypt depth, mucosal mass, citrulline, ZO-1/occludin expression are well-validated assay readouts
Authors & Attribution
✍️ Article Author
Dr. Daniel J. Drucker
Daniel J. Drucker, OC, MD, FRSC, is a Senior Investigator at the Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, and Professor of Medicine at the University of Toronto. Dr. Drucker is the discoverer of the intestinotrophic properties of glucagon-like peptide-2 (GLP-2) and his foundational 1996 publications in Nature Biotechnology and PNAS established the scientific basis for teduglutide’s development. He is one of the world’s leading authorities on incretin biology, with over 800 publications and numerous awards including the Canada Gairdner International Award and the Banting Medal for Scientific Achievement. Daniel J. Drucker is being referenced as one of the leading scientists involved in the research and development of GLP-2 Analog (Teduglutide). In no way is this doctor/scientist endorsing or advocating the purchase, sale, or use of this product for any reason. There is no affiliation or relationship, implied or otherwise, between Pure US Peptide and this doctor.
View Full Researcher Profile →🎓 Scientific Journal Author
Dr. Palle B. Jeppesen
Palle B. Jeppesen, MD, PhD, is a Senior Consultant and Associate Professor in the Department of Gastroenterology at Rigshospitalet (Copenhagen University Hospital), Denmark, and one of the world’s leading clinical investigators in short bowel syndrome. Dr. Jeppesen was the lead author on the pivotal STEPS trial (2012) published in Gastroenterology that led to FDA approval of teduglutide, and led subsequent Phase II and long-term extension studies establishing the durability of teduglutide’s clinical efficacy. He has authored more than 100 publications on intestinal failure and GLP-2 physiology. Palle B. Jeppesen is being referenced as one of the leading scientists involved in the research and development of GLP-2 Analog (Teduglutide). In no way is this doctor/scientist endorsing or advocating the purchase, sale, or use of this product for any reason. There is no affiliation or relationship, implied or otherwise, between Pure US Peptide and this doctor.
View Full Researcher Profile →Dr. Palle B. Jeppesen is being referenced as one of the leading scientists involved in the research and development of GLP2-T. In no way is this doctor/scientist endorsing or advocating the purchase, sale, or use of this product for any reason. There is no affiliation or relationship, implied or otherwise, between Pure US Peptide and this doctor. The purpose of citing the doctor is to acknowledge, recognize, and credit the exhaustive research and development efforts conducted by the scientists studying this peptide.
Referenced Citations
Drucker DJ, Erlich P, Asa SL, Brubaker PL. Induction of intestinal epithelial proliferation by glucagon-like peptide 2. Proc Natl Acad Sci USA. 1996;93(15):7911-7916.
PubMedDrucker DJ, Shi Q, Crivici A, et al. Regulation of the biological activity of glucagon-like peptide 2 in vivo by dipeptidyl peptidase IV. Nat Biotechnol. 1997;15(7):673-677.
PubMedScott RB, Kirk D, MacNaughton WK, Meddings JB. GLP-2 augments the adaptive response to massive intestinal resection in rat. Am J Physiol. 1998;275(5):G911-G921.
PubMedCheeseman CI, Tsang R. The effect of GIP and glucagon-like peptides on intestinal basolateral membrane hexose transport. Am J Physiol. 1996;271(3):G477-G482.
PubMedMunroe DG, Gupta AK, Kooshesh F, et al. Prototypic G protein-coupled receptor for the intestinotrophic factor glucagon-like peptide 2. Proc Natl Acad Sci USA. 1999;96(4):1569-1573.
PubMedDrucker DJ, Yusta B. Physiology and pharmacology of the enteroendocrine hormone glucagon-like peptide-2. Annu Rev Physiol. 2014;76:561-583.
PubMedDubé PE, Forse CL, Bahrami J, Brubaker PL. The essential role of insulin-like growth factor-1 in the intestinal tropic effects of glucagon-like peptide-2 in mice. Gastroenterology. 2006;131(2):589-605.
PubMedMarier JF, Beliveau M, Mouksassi MS, et al. Pharmacokinetics, safety, and tolerability of teduglutide, a glucagon-like peptide-2 (GLP-2) analog, following multiple ascending subcutaneous administrations in healthy subjects. J Clin Pharmacol. 2008;48(11):1289-1299.
PubMedBoushey RP, Yusta B, Drucker DJ. Glucagon-like peptide 2 decreases mortality and reduces the severity of indomethacin-induced murine enteritis. Am J Physiol. 1999;277(5):E937-E947.
PubMedBurrin DG, Stoll B, Guan X, et al. Glucagon-like peptide 2 dose-dependently activates intestinal cell survival and proliferation in neonatal piglets. Endocrinology. 2005;146(1):22-32.
PubMedPrasad R, Alavi K, Schwartz MZ. Glucagon-like peptide-2 analogue enhances intestinal mucosal mass after ischemia and reperfusion. J Pediatr Surg. 2000;35(2):357-359.
PubMedYusta B, Holland D, Koehler JA, et al. ErbB signaling is required for the proliferative actions of GLP-2 in the murine gut. Gastroenterology. 2009;137(3):986-996.
PubMedRUO Disclaimer
For Research Use Only (RUO). Not intended for human consumption, clinical use, or as a drug, food, cosmetic, or medical device. This product has not been evaluated by the FDA and is supplied solely for in-vitro laboratory research by qualified professionals.
Certificate of Analysis
Each lot is independently tested by accredited third-party laboratories (ISO 17025) at 99%+ purity.
Latest Lab Report
Storage & Handling
Summary
Store at 2–8°C (refrigerated). After reconstitution, use within 3 hours at room temperature. Do not freeze.
❄️ Lyophilized Peptide Storage
Store lyophilized teduglutide vials at 2°C to 8°C (36°F–46°F) in the original carton to protect from light. Stable for up to 24 months under recommended conditions. Do not use beyond the expiration date printed on the vial.
💧 Reconstitution
Reconstitute each vial with 0.5 mL of the provided diluent (sterile water for injection). Gently swirl the vial for approximately 15 seconds — do not shake. Allow to stand for up to 2 minutes if undissolved powder remains, then gently swirl again. The reconstituted solution should appear clear and colorless.
⏰ After Reconstitution
Use within 3 hours of reconstitution. Keep at room temperature (20–25°C / 68–77°F) until administration. Do not refrigerate or freeze the reconstituted solution. Discard any unused portion after 3 hours.
❄️ Freezing
Do NOT freeze either the lyophilized vials or the reconstituted solution. If a vial has been frozen, it must be discarded.
🧴 Handling Precautions
Inspect the reconstituted solution visually prior to use. Do not use if the solution appears cloudy, discolored, or contains particulate matter. Each vial is accompanied by a Certificate of Analysis (COA) detailing purity verification via RP-HPLC and Mass Spectrometry (MS). This product is for research use only (RUO).
“Preclinical Research Summary Foundational Studies Study Model Key Findings Ref Drucker et al.”
