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Molecular Weight
Purity
Storage
Appearance
Solubility
01
AOD-9604 is a synthetic 16-residue peptide derived from the C-terminal end of human growth hormone (hGH). It corresponds to hGH residues 177–191, with an extra tyrosine added at the N-terminus, and is cyclised by a disulfide bond between its two cysteines (Cys7 and Cys14 in the peptide’s own numbering).
Unlike the other materials in this category, it is not a releasing factor, secretagogue or receptor-binding hormone analogue; it is a small fragment of growth hormone itself, studied in metabolic models and as a well-defined disulfide-containing peptide. It is supplied as a lyophilized reference material for in vitro research on GH-derived fragments, disulfide chemistry and analytical method development.
02
AOD-9604’s structure is defined by its relationship to hGH and by a single intramolecular disulfide.
Origin in hGH
Residues 2–16 reproduce hGH 177–191, part of the C-terminal region of the hormone.
Added Tyr1
The N-terminal tyrosine is not part of the native hGH segment. It adds a UV-absorbing residue and a convenient site for radio-iodination in binding studies.
Disulfide ring
The Cys7–Cys14 bond closes a ring made up of Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys. This constrains the backbone and gives the peptide a more defined shape than its linear, reduced form.
Free-acid C-terminus
The chain ends in Phe16 with a free carboxylic acid, unlike the amidated peptides elsewhere in this category.
Because the cysteines can exist either as a disulfide or as two free thiols, the peptide has two distinct forms, and analytical methods need to distinguish them.
03
Research on AOD-9604 falls into two broad areas.
Metabolic models
The C-terminal region of hGH has long been investigated for effects on fat metabolism separate from growth-promoting activity. AOD-9604 has been studied in adipocyte and animal models of lipolysis and lipogenesis, and published work describes it as not acting through the classical growth hormone receptor pathway in those systems.
Conformation
Circular dichroism and NMR compare the cyclic (disulfide) and reduced (linear) forms to show how the disulfide shapes the peptide.
Disulfide reactivity
Reduction studies with agents such as TCEP or DTT measure how accessible and reactive the Cys7–Cys14 bond is under different conditions.
All research context described here refers to controlled in vitro and preclinical experimental systems.
04
Disulfide method development
A simple, single-disulfide model for HPLC methods that separate oxidised (cyclic) from reduced (linear) forms.
Disulfide mapping
Used as a test case for non-reducing digestion and LC-MS workflows that confirm which cysteines are linked.
Thiol–disulfide exchange
A model substrate for studying reduction and re-oxidation kinetics and for spotting scrambled or dimerised by-products.
GH-fragment research
A reference compound in studies comparing growth hormone fragments with intact hGH in metabolic models.
05
Storage
Store the lyophilized powder at −20 °C, sealed and desiccated. The disulfide is stable in the dry state.
Reducing agents
Avoid DTT, TCEP, β-mercaptoethanol and other thiols unless reduction is intended. The reduced form can re-oxidise incorrectly or form intermolecular dimers.
pH
Mildly acidic conditions (around pH 3–5) slow thiol–disulfide exchange. Basic conditions above about pH 8 promote disulfide shuffling and should be avoided.
Reconstitution
Dissolve in water or a mildly acidic buffer with gentle swirling.
Solutions
Use promptly or freeze single-use aliquots. Use low-binding polypropylene tubes and keep away from thiol-containing reagents.
06
Analysis needs to confirm the sequence and the oxidation state of the cysteines.
HPLC
Reversed-phase C18 under non-reducing conditions. The cyclic and reduced forms usually separate, so a second peak can signal partial reduction or a mixed sample.
Mass spectrometry
Intact mass should match about 1815.1 Da. Forming the disulfide removes two hydrogens, so the reduced form is about 2 Da heavier.
Disulfide confirmation
Reducing with TCEP and then alkylating with iodoacetamide adds about 57 Da per cysteine, confirming that two cysteines were involved in the bond.
Free thiol content
Ellman’s reagent (DTNB) gives a simple spectrophotometric measure of any free thiol present.
Impurity profile
Typical checks cover the reduced form, disulfide-linked dimers, truncated sequences and oxidation of Tyr1.
07
From the C-terminal end of human growth hormone: it reproduces hGH residues 177–191 with an extra tyrosine at the N-terminus, giving 16 residues in total.
The bond between Cys7 and Cys14 makes the peptide cyclic and gives it a defined shape. The reduced, linear form behaves differently and is about 2 Da heavier, so the two forms must be distinguished analytically.
By intact mass, by comparing HPLC profiles before and after reduction, and by reducing with TCEP and alkylating with iodoacetamide, which adds about 57 Da per cysteine.
Mildly acidic pH (around 3–5), no reducing agents or thiol-containing reagents, and prompt use or frozen single-use aliquots. Basic pH promotes disulfide shuffling.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
AOD-9604 Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/growth-hormone-axis-research-peptides/aod-9604/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
