Cagrilintide is a long-acting acylated analog of amylin — the pancreatic hormone co-secreted with insulin from beta cells — engineered for stability and non-selective activity across the amylin and calcitonin receptor family. It matters to metabolic researchers because it works through a pathway entirely separate from the incretin receptors, which makes it the standard tool for asking what the amylin axis contributes on top of GLP-1 signalling. We supply research-grade cagrilintide as lyophilized powder in sealed vials, for laboratory use only.
Cagrilintide is investigational. It has no marketing approval anywhere as of 2026, and research-grade material is a reference chemical rather than a medicine.
What is cagrilintide, precisely
Native human amylin (islet amyloid polypeptide, IAPP) is a 37-residue peptide released with insulin after nutrient intake. It has two properties that make it useless as a research tool in its native form: a plasma half-life of minutes, and a strong tendency to self-aggregate into amyloid fibrils — the same fibrils found in the islets of people with type 2 diabetes. Any usable amylin analog has to solve both problems at once. Pramlintide, the earlier analog, solved aggregation by borrowing proline substitutions from rat amylin, which does not fibrillate, but remained short-acting. Cagrilintide, cited as AM833 in the literature, solves both: it is a non-aggregating analog carrying a fatty-acid side chain for albumin binding, giving it a duration measured in days.
Origin and structure
- Amylin-derived backbone with substitutions that suppress the beta-sheet stacking responsible for amyloid formation.
- Intramolecular disulfide bridge between the two N-terminal cysteines, forming the small ring that native amylin and calcitonin both require for receptor activity — reflected in the two sulfur atoms in the formula.
- C-terminal amidation, as in native amylin, which is necessary for receptor engagement.
- Fatty-acid acylation at a lysine side chain, conferring reversible albumin binding and the long circulating persistence reported in pharmacokinetic work.
- Non-selective receptor profile, with reported activity across AMY1, AMY2 and AMY3 receptors and at the calcitonin receptor itself.
Catalog identifiers: CAS 1415456-99-3, molecular formula C194H309N55O59S2, molecular weight 4409.07 Da.
How cagrilintide is thought to work
Amylin receptors are not conventional standalone GPCRs. They are heterodimers: the calcitonin receptor (CTR) complexed with one of three receptor activity-modifying proteins, RAMP1, RAMP2 or RAMP3, producing AMY1, AMY2 and AMY3 respectively. The RAMP partner reshapes the ligand-binding pocket so that the same core receptor prefers amylin over calcitonin. This architecture has a direct consequence for experimental design: expressing CTR alone in a cell line does not give you an amylin receptor, and the RAMP subtype present determines the pharmacology you measure.
Reported downstream signalling is Gs-coupled cAMP accumulation, with receptor populations concentrated in the area postrema and nucleus tractus solitarius — hindbrain regions outside the tight blood-brain barrier. Preclinical work has described reduced food intake and slowed gastric emptying following amylin receptor agonism, and the effect has generally been attributed to these hindbrain populations. Because that circuitry is anatomically and pharmacologically distinct from the hypothalamic and vagal GLP-1 receptor populations, amylin and GLP-1 agonists are reported to produce additive rather than redundant effects in animal models — the rationale behind co-administration studies pairing cagrilintide with semaglutide.
Selectivity is a live design question in this family, not a solved one. A non-selective agonist that engages AMY1, AMY2, AMY3 and the calcitonin receptor produces a composite response, and calcitonin receptor activation carries its own biology in bone and elsewhere. Selective amylin analogs are being developed precisely to separate those contributions, so a laboratory choosing cagrilintide should recognise that it answers the question what does broad amylin-family agonism do, not what does AMY3 specifically do. Where subtype attribution is the goal, RAMP-defined recombinant lines and subtype-selective comparators are the appropriate tools.
What research has examined
- Receptor pharmacology. cAMP and binding assays in cells co-expressing CTR with RAMP1, 2 or 3, used to establish the non-selective profile that distinguishes cagrilintide from selective amylin analogs.
- Aggregation and biophysical studies. Thioflavin T fibrillation assays, circular dichroism and stability work — a core research area for any amylin analog, because aggregation propensity is the defining liability of this peptide family.
- Rodent studies. Food intake, gastric emptying and body composition in diet-induced obesity models, plus combination experiments testing additivity with GLP-1 receptor agonists.
- Human clinical trials. Phase 1 and 2 data have been published for cagrilintide alone and in fixed combination with semaglutide, and phase 3 programmes have reported results. These describe an investigational pharmaceutical under clinical supervision and do not transfer to research-grade material. Our note on why researchers pair cagrilintide with semaglutide covers the combination logic.
A further methodological point applies to any amylin work. Peptide adsorption to glass and polypropylene is significant at the low nanomolar concentrations used in receptor assays, and adsorptive loss is indistinguishable from low potency in the resulting curve. Carrier protein in the assay buffer, low-binding plasticware and freshly prepared dilutions are standard mitigations, and their absence is a common reason published potency values for amylin analogs disagree between laboratories by an order of magnitude or more, even when the same nominal compound and receptor construct were used.
Forms and sizes we supply
| Attribute | Specification |
|---|---|
| Form | Lyophilized powder, sealed glass vial |
| Sizes | 5 mg, 10 mg |
| Purity | Greater than or equal to 99% by HPLC, lot-matched COA |
| CAS | 1415456-99-3 |
| Molecular weight | 4409.07 Da |
| Formula | C194H309N55O59S2 |
| Class | Long-acting acylated amylin analog |
| Also cited as | AM833 |
| Intended use | Laboratory research only |
Sizes and pricing are on the cagrilintide product page, listed within the GLP-1 and incretin peptides collection because most laboratories buying it are running incretin comparisons.
Reconstitution and storage in a lab context
Standard concentration arithmetic applies: a 5 mg vial reconstituted with 2 mL of bacteriostatic water gives 2.5 mg/mL, equal to 2,500 mcg/mL, so 0.1 mL of that solution contains 250 mcg of peptide. Handling deserves more care than for a typical acylated peptide. Amylin-family sequences retain some aggregation propensity even when engineered against it, and mechanical agitation, low concentrations on untreated plastic surfaces and pH near the isoelectric point all promote it. Add diluent gently down the vial wall, swirl rather than shake, and inspect the solution for haze or fibres before use — a cloudy amylin analog solution is a failed preparation, not a cosmetic issue.
Sealed lyophilized powder keeps at minus 20 degrees Celsius, protected from light and moisture. Reconstituted solution is stored at 2 to 8 degrees Celsius and used within the study window; because aggregation is time and temperature dependent, shortening the interval between reconstitution and use matters more here than for incretin peptides. See our reconstitution guide, storage guide.
Purity, COA and how to read it
A cagrilintide certificate should include an HPLC chromatogram with main-peak area percentage, a mass spectrometry identity result checked against the theoretical 4409.07 Da, net peptide content, lot number and analysis date. One extra check is specific to this molecule: the disulfide bridge must be correctly formed, and a reduced or scrambled variant differs from the intended structure by only two mass units, which a low-resolution spectrum can miss. Where disulfide integrity is critical to your assay, ask what the analysis actually resolved. Our guide to reading a COA explains the rest.
Storage of prepared working solutions warrants one final comment. Amylin-family peptides are the class where the interval between preparation and use most reliably shows up in the data, because aggregation proceeds slowly enough to be invisible at preparation and advanced enough to matter hours later. Laboratories that record preparation time alongside experimental time, and that treat a solution older than the validated window as a new preparation rather than the same one, remove a source of drift that is otherwise easy to attribute to biological variability. The same discipline explains much of the disagreement between amylin studies conducted in different laboratories.
Regulatory status
Cagrilintide is investigational, with no marketing approval in any jurisdiction as of 2026. Research-grade cagrilintide is supplied as a reference chemical for laboratory investigation, labelled research use only, and is not approved, formulated or permitted for administration to humans or animals. Published clinical data describe a trial product and create no human-use pathway for laboratory material — see research use only, explained.
Related peptides and comparisons
The most common pairing is with a GLP-1 receptor agonist, examined in cagrilintide vs semaglutide. Researchers comparing amylin analogs will also want pramlintide, the short-acting predecessor. For multi-receptor incretin work see retatrutide.