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$104.00
Trinity-X, also listed as GLP3-RT, is a synthetic research peptide supplied as a lyophilized powder in sealed glass vials for laboratory work only.
It acts at three metabolic receptors at once, so laboratories use it as a single-molecule tool in incretin signalling, energy-balance mechanism and glucose homeostasis research carried out in preclinical models.
Quantity
$104.00
GLP3-RT (Trinity-X) · 10mg
$104.00
Recommended with this order
Frequently paired with this compound by other researchers.
For Research Use Only. Not for human consumption or therapeutic treatment.
Compound Class and Structure
Trinity-X (GLP3-RT) is a synthetic single-chain peptide of 39 amino acids, supplied as a lyophilized solid for in vitro and preclinical laboratory research. Its sequence sits within the glucagon–secretin peptide superfamily, a family in which a conserved N-terminal segment drives receptor engagement while the central helical region and C-terminal extension govern selectivity, conformational stability and plasma residence. Engineering across all three regions, together with a fatty-acid modification that supports reversible albumin association, is intended to hold one defined tri-receptor activity profile inside a single molecule instead of requiring three separate agonist peptides in the same experimental system.
Receptor Pharmacology and Signalling
Trinity-X is characterised as a tri-agonist at three class B1 G-protein-coupled receptors: the glucagon-like peptide-1 receptor (GLP-1R), the glucose-dependent insulinotropic polypeptide receptor (GIPR) and the glucagon receptor (GCGR). All three couple predominantly to Gαs, so receptor engagement is typically read out as adenylate cyclase activation and intracellular cAMP accumulation, followed by protein kinase A activity, CREB phosphorylation and, in β-cell systems, downstream calcium flux. Secondary signalling branches examined in vitro include β-arrestin recruitment, receptor internalisation and recycling kinetics, and biased-signalling comparisons between the three receptor arms. Because relative potency differs at GLP-1R, GIPR and GCGR, investigators commonly profile the compound in receptor-transfected reporter lines to map EC50 relationships before interpreting composite readouts obtained in whole-animal studies.
Research Areas, Models and Endpoints
Published research interest clusters around three fields: incretin signalling, energy-balance mechanisms and glucose homeostasis in preclinical models. Common systems include HEK293 and CHO lines stably expressing human GLP-1R, GIPR or GCGR; isolated rodent pancreatic islets; primary hepatocyte and adipocyte cultures; and whole-animal work in diet-induced obese mice, Zucker rats and genetically modified receptor-knockout strains.
Measured endpoints vary by field. Cell-based work quantifies cAMP EC50 values, luminescence or fluorescence reporter output, receptor occupancy and arrestin recruitment. Islet and hepatocyte studies record glucose-stimulated insulin secretion by immunoassay, glucagon output, glycogen content and lipid handling markers. Whole-animal protocols track glucose excursion and area under the curve during oral or intraperitoneal glucose tolerance testing, plasma insulin and glucagon profiles, gastric emptying rate, oxygen consumption and respiratory exchange ratio by indirect calorimetry, hepatic triglyceride quantification, adipose and liver histology, and receptor or target-gene expression by qPCR and Western blot. Endpoints describe what an assay records in a model system; they are not statements about effects in people.
Storage and Laboratory Documentation
The lyophilized solid is shipped and held as a stable powder. Standard laboratory documentation for material of this class specifies storage at -20°C for long-term inventory, with short-term holding at 2°C to 8°C acceptable for active projects. Vials should be kept sealed, fully desiccated and protected from light, since peptide solids of this family are sensitive to ambient moisture and to prolonged ultraviolet exposure. Repeated warming and cooling cycles are avoided, and vials are allowed to equilibrate to ambient temperature before the seal is broken so that condensation does not form on the solid. Good practice is to log lot number, receipt date and freezer location against the certificate of analysis issued for that specific lot, keeping chain-of-custody records aligned with the analytical report. Trinity-X is sold strictly as a research material for qualified laboratory professionals. It is not a medicine, not approved for any therapeutic purpose, and not for human or veterinary use.

Trinity-X is the catalogue identity for GLP3-RT, a synthetic 39-amino-acid research peptide engineered as a tri-agonist at the GLP-1, GIP and glucagon receptors. It is manufactured by solid-phase peptide synthesis, purified by reversed-phase chromatography and supplied as a white to off-white lyophilized solid in sealed glass vials.
Structurally it belongs to the glucagon–secretin peptide superfamily, with a conserved activation region at the N-terminus and an engineered helical core and C-terminal extension that shape receptor selectivity and stability. A fatty-acid modification supports reversible albumin association, extending the window over which the molecule remains intact in a preclinical system.
The practical appeal for laboratories is consolidation: one characterised molecule covering three receptor arms, rather than three separate agonists with independent handling, lot histories and analytical records. Trinity-X is offered in 10mg, 12mg, 20mg, 10ml, 15mg and 30mg formats for research use only.

Real Peptides supplies Trinity-X on supply-chain terms that laboratories can document. Every production lot is submitted to an independent, third-party analytical laboratory, and the resulting certificate of analysis is published against that specific lot rather than presented as a generic sample report. Identity and purity data are generated by mass spectrometry and high-performance liquid chromatography.
Material is filled as a lyophilized solid into sealed glass vials with intact crimp seals and tamper-evident closures, then held in controlled cold storage until dispatch. Vials are inspected before release, and lot identifiers on the vial match the identifiers on the analytical report, so inventory records, freezer logs and paperwork stay aligned.
Orders ship from United States stock, packed with insulated materials for transit stability. Available formats are 10mg, 12mg, 20mg, 10ml, 15mg and 30mg. All material is sold for laboratory research use only, to qualified professionals, and is not for human or veterinary use.

Most metabolic research peptides fall into narrower mechanism classes. Single-receptor incretin agonists engage GLP-1R alone, producing a clean but one-dimensional signalling readout. Dual incretin agonists add GIPR, allowing comparison of two Gαs-coupled arms but leaving hepatic and energy-expenditure pathways unaddressed. Glucagon-receptor agonists probe that third arm in isolation, usually without incretin input.
Trinity-X sits in the tri-agonist class, engaging GLP-1R, GIPR and GCGR within one defined molecule. That matters experimentally because the three arms interact: GCGR engagement recruits hepatic and energy-expenditure endpoints, while incretin-arm engagement dominates islet and gastrointestinal readouts. Combining separate peptides introduces independent pharmacokinetic profiles and confounds interpretation; a single molecule holds the ratio fixed across an experiment.
Comparative pharmacology also differs. Investigators can map EC50 values arm by arm in receptor-transfected reporter lines, then re-test in knockout models to attribute a composite whole-animal readout to a specific receptor contribution.
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