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Molecular Weight
Purity
Storage
Appearance
Solubility
01
Sermorelin, GHRH(1–29)-NH₂, is a synthetic peptide matching the first 29 residues of human growth hormone-releasing hormone (GHRH), with an amidated C-terminus. This N-terminal fragment is the shortest part of the 44-residue hormone that retains full activity at the GHRH receptor.
Because its sequence is completely unmodified, Sermorelin is the natural baseline for the engineered analogues in this category. CJC-1295 changes four of its residues, CJC-1295 with DAC adds an albumin-binding linker, and Tesamorelin returns to the full 44-residue chain with an N-terminal cap. Sermorelin keeps all the native weak points, notably Asn8 and Met27, which makes it valuable for receptor comparisons, degradation studies and analytical method development. It is supplied as a lyophilized reference material for in vitro research only.
02
Sermorelin reproduces native GHRH(1–29) exactly, including every residue that later analogues were designed to replace.
N-terminal binding region
The first residues, including Tyr1, Ala2, Asp3 and Phe6, are central to receptor recognition. The Tyr1-Ala2 bond is also where DPP-IV cuts, the main route of rapid inactivation.
Helical region
In membrane-like environments, much of the sequence beyond the first few residues folds into an amphipathic α-helix, with hydrophobic and charged residues on opposite faces.
Asn8-Ser9
An asparagine followed by serine is one of the faster-deamidating sequence motifs, forming aspartate and isoaspartate products. CJC-1295 replaces Asn8 with Gln.
Gly15
A helix-weakening glycine in the middle of the chain. CJC-1295 replaces it with Ala.
Met27
The only sulfur-containing residue and the main oxidation site (+16 Da). CJC-1295 replaces it with Leu.
Arg29-NH₂
The amidated C-terminus mirrors processing of the native hormone and protects against carboxypeptidases.
03
In vitro, Sermorelin is used as the reference agonist for the unmodified GHRH(1–29) sequence.
Receptor binding
Competition binding assays with GHRH receptor-expressing membranes establish the baseline affinity that modified analogues are compared against.
cAMP signalling
The GHRH receptor couples to Gs, so cAMP accumulation in receptor-expressing cells is the standard functional readout for potency and efficacy.
Truncation and substitution studies
Starting from Sermorelin, shortened and substituted versions map which residues are essential for binding and signalling.
Degradation versus activity
Tracking how oxidation at Met27 or deamidation at Asn8 changes receptor activity links specific chemical changes to their functional effects.
All observations described here come from cell-free and cell-based in vitro systems.
04
Stability baseline
Run side by side with CJC-1295 and Tesamorelin under the same thermal, oxidative and enzymatic stress to measure how much protection each modification provides.
Degradation model
Its well-characterised Met27 and Asn8 sites make it a model substrate for developing stability-indicating HPLC and MS methods.
Receptor reference
Provides the reference dose–response curve when assessing the potency of GHRH analogues.
Mass spectrometry reference
At about 3.4 kDa it forms several multiply charged ions (commonly +3 to +5), useful for setting up methods for mid-sized peptides.
05
Storage
Store the lyophilized powder at −20 °C, sealed, desiccated and protected from light. As an unmodified sequence, it is less stable than the engineered analogues.
Oxidation
Met27 oxidises readily in the presence of oxygen, trace metals and light. Minimise air exposure and use degassed buffers for sensitive work.
Deamidation
The Asn8-Ser9 motif deamidates fastest at neutral to basic pH and higher temperatures. Use solutions promptly.
Reconstitution
Dissolve in water or a mildly acidic buffer (around pH 5–6), which slows deamidation. Swirl gently.
Solutions
Aliquot into single-use portions straight after reconstitution and freeze; avoid repeated freeze–thaw cycles. Use low-binding polypropylene labware.
06
Sermorelin’s known degradation routes define what its analytical methods need to detect.
HPLC
Reversed-phase C18 on a wide-pore (300 Å) column with an acetonitrile/TFA gradient. The Met27-oxidised form is more polar and elutes slightly earlier; deamidated forms elute close to the main peak and may need method optimisation to resolve.
Mass spectrometry
ESI-MS shows charge states around +3 to +5, matching 3357.9 Da. Oxidation appears at +16 Da and deamidation at +1 Da; high-resolution MS is needed to separate the deamidation shift from the natural isotope pattern.
Forced degradation
Heat, peroxide and acidic/basic pH stress produce predictable degradation products, which are used to show that a method is stability-indicating.
C-terminal amide
The free-acid form differs by about 1 Da and is confirmed by high-resolution MS and C-terminal fragment ions.
07
They share the same 29-residue GHRH backbone. Sermorelin is the unmodified sequence; CJC-1295 replaces four residues (Ala2, Asn8, Gly15 and Met27) to make it more resistant to enzymes and chemical degradation.
Because it keeps every native weak point, including the DPP-IV cleavage site, the Asn8 deamidation site and the Met27 oxidation site, it shows how much protection each modification in the analogues provides.
Mainly Met27 oxidation (+16 Da) and Asn8 deamidation (+1 Da, giving aspartate and isoaspartate forms), plus truncated sequences such as the DPP-IV product missing the first two residues.
A mildly acidic solution, around pH 5–6, slows deamidation at Asn8. Neutral to basic pH and warm temperatures speed it up.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
Sermorelin Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/growth-hormone-axis-research-peptides/sermorelin/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
