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Molecular Weight
Purity
Storage
Appearance
Solubility
01
Tesamorelin is a synthetic analogue of human growth hormone-releasing hormone (GHRH). Unlike the shorter GHRH(1–29) analogues in this category, it keeps the complete 44-residue sequence of the native hormone, with one change: a trans-3-hexenoyl group attached to the N-terminal tyrosine.
That small acyl group protects the N-terminus from dipeptidyl peptidase-IV (DPP-IV), the enzyme that rapidly inactivates native GHRH, while leaving the receptor-binding sequence untouched. The same molecule is the active ingredient of an approved pharmaceutical product; the material listed here is supplied solely as a lyophilized reference compound for in vitro GHRH receptor studies, stability comparisons and analytical work on larger peptides.
02
Tesamorelin is best understood by comparison with native GHRH(1–44)-NH₂ and with the truncated analogues.
Full-length sequence
All 44 residues of human GHRH are retained, including the C-terminal region (residues 30–44) that is absent from sermorelin and CJC-1295.
N-terminal hexenoyl group
A six-carbon unsaturated acyl chain (trans-3-hexenoic acid) is joined to the α-amine of Tyr1. It blocks DPP-IV, which would otherwise remove the Tyr1-Ala2 dipeptide, without changing any amino acid in the chain.
Native residues kept
Unlike CJC-1295, Tesamorelin keeps Ala2, Asn8, Gly15 and Met27. This makes it a useful contrast compound: it relies on N-terminal capping alone, rather than internal substitutions, for protection.
C-terminal amide
The chain ends in Leu44-NH₂, matching the native hormone.
03
In vitro, Tesamorelin is studied as an agonist of the GHRH receptor, a class B G protein-coupled receptor on pituitary somatotrophs.
Receptor binding
Competition binding assays with GHRH receptor-expressing membranes compare its affinity with native GHRH(1–44), GHRH(1–29) and modified analogues.
cAMP signalling
The GHRH receptor couples to Gs, so cell-based cAMP assays are the standard readout for potency and efficacy.
DPP-IV resistance
Incubation with purified DPP-IV, followed by HPLC or LC-MS, shows how effectively the N-terminal acyl group prevents loss of the Tyr1-Ala2 dipeptide compared with unmodified GHRH.
All observations described here come from cell-free and cell-based in vitro systems.
04
GHRH receptor comparator
Used alongside native GHRH and the GHRH(1–29) analogues to compare full-length and truncated ligands.
N-terminal capping model
A clear example of protecting a peptide with a terminal modification rather than amino acid substitution, useful in stability study design.
Large-peptide method development
At about 5.1 kDa with several oxidation- and deamidation-prone residues, it is a demanding test compound for HPLC and LC-MS methods.
Degradation profiling
Its methionine and asparagine residues make it suitable for forced-degradation studies that track oxidation and deamidation products.
05
Storage
Store the lyophilized powder at −20 °C, sealed, desiccated and protected from light. Let the vial reach room temperature before opening.
Oxidation
Met27 is retained, so the peptide can oxidise (+16 Da). Minimise exposure to air and light, and avoid oxidising reagents.
Deamidation
Asn8 and Asn35 can deamidate slowly in solution, particularly at neutral to basic pH and higher temperatures.
Reconstitution
Dissolve in water or a mild aqueous buffer with gentle swirling. Avoid vigorous shaking, which can promote aggregation of longer peptides.
Solutions
Prepare fresh where possible, or freeze single-use aliquots and avoid repeated freeze–thaw cycles. Use low-binding polypropylene labware.
06
Analysis must confirm the full 44-residue sequence, the N-terminal acyl group and the absence of common degradation products.
HPLC
Reversed-phase C18 or C8 with a wide-pore (300 Å) column and a shallow acetonitrile gradient. Oxidised and deamidated forms typically elute close to the main peak and need good resolution.
Mass spectrometry
ESI-MS shows several multiply charged ions for the 5135.9 Da molecule. Watch for +16 Da (Met oxidation) and +1 Da (deamidation) species.
N-terminal modification
The hexenoyl group adds about 96 Da compared with unmodified GHRH(1–44)-NH₂. MS/MS of the N-terminal fragments confirms it is attached to Tyr1.
Impurity profile
Typical checks cover oxidised and deamidated forms, deletion or truncated sequences, the non-acylated peptide and the free-acid C-terminus.
07
Tesamorelin keeps the full 44-residue GHRH sequence and protects it with an N-terminal hexenoyl group. Sermorelin and CJC-1295 are shorter 29-residue fragments; CJC-1295 also carries four amino acid substitutions.
It caps the N-terminal amine of Tyr1, which prevents DPP-IV from removing the first two residues. This is the main route by which native GHRH is inactivated.
Mainly Met27 oxidation (+16 Da) and deamidation at asparagine residues (+1 Da), along with truncated sequences. HPLC with high-resolution MS is used to separate and identify them.
Intact mass should match 5135.9 Da, about 96 Da above unmodified GHRH(1–44)-NH₂, and MS/MS of N-terminal fragments confirms that the acyl group sits on Tyr1.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
Tesamorelin Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/growth-hormone-axis-research-peptides/tesamorelin/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
