AOD-9604

AOD-9604 is a modified 16-residue fragment corresponding to the C-terminal region (residues 176–191) of human growth hormone, extended with an N-terminal tyrosine. Investigators developed it as a structurally defined research material for studies of lipid-metabolism signaling, where the literature describes a fragment that engages fat-metabolism pathways documented for the parent hormone’s C-terminus without the growth-promoting signaling of full-length human growth hormone. The peer-reviewed literature catalogs AOD-9604 in lipolysis and adipocyte-metabolism research and in comparative structure-activity studies of hGH-fragment peptides. Its molecular identity is fixed by structural confirmation against PubChem CID 71300630, empirical formula C78H123N23O23S2. Supplied for laboratory characterization and in-vitro metabolic-signaling studies only. For research use only; not for human consumption, medical use, or veterinary application.

AOD-9604 is a disulfide-containing peptide whose sequence reproduces the C-terminal lipolytic region of human growth hormone with an added N-terminal tyrosine residue. The published literature documents that this fragment engages adipocyte lipid-metabolism pathways associated with the parent hormone’s C-terminus while, in the studied models, not measurably influencing the IGF-1 axis or glucose-handling pathways engaged by full-length growth hormone — a selectivity profile that distinguishes the fragment from the intact hormone. The molecule’s two cysteine residues form the intramolecular disulfide bridge characteristic of the region. Pharmacokinetic descriptors documented in published animal-model investigations include rapid plasma clearance typical of a small peptide fragment. All activity descriptors here are framed as documented in published research rather than as effects of the supplied product. Structural confirmation is established by mass spectrometry and HPLC-validated purity on each Certificate of Analysis.

Experimental domains documented in the published literature include adipocyte lipolysis assays, lipid-metabolism signaling investigations, comparative structure-activity work across hGH-fragment peptides, and animal-model research into fat-metabolism pathways associated with the growth-hormone C-terminus. Investigators use AOD-9604 as a fragment reference to distinguish the lipid-metabolism signaling of the C-terminal region from the somatotropic signaling of full-length growth hormone. Use in laboratory research extends to mechanism-elucidation paradigms where the fragment serves as a defined hGH-C-terminus research standard. The reference standard is supplied for these and equivalent in-vitro and animal-model experimental contexts only, with no associated guidance for human, clinical, or veterinary use.

Each lot is characterized by reverse-phase HPLC for chromatographic purity and by mass spectrometry for molecular-ion confirmation against the C78H123N23O23S2 empirical formula. Disulfide-bond integrity is confirmed by reduction-and-alkylation mass spectrometry methods when included in the lot release specification, given the intramolecular disulfide bridge. Purity is reported as an HPLC-area percentage on the Certificate of Analysis distributed with every lot, alongside the molecular-weight match within instrument tolerance. Peptide content where applicable is determined by amino-acid analysis or nitrogen-content assay following the analytical method specified on the COA. Residual solvent and water content are reported categorically when these parameters are part of the release specification. The COA records the lot identifier, manufacturing date, and analytical method versions used. Researchers requiring batch-level analytical detail should reference the COA distributed with the supplied material.

For laboratory storage, the lyophilized reference standard should be held at −20°C in its sealed, light-protected container until ready for analytical use. Allow vials to equilibrate to ambient temperature before opening to avoid moisture condensation on the lyophile. Reconstitution for in-vitro experimental use is typically performed in bacteriostatic water or a researcher-selected buffer compatible with the downstream assay; once reconstituted, store the working solution at 2–8°C and characterize stability in the relevant buffer prior to extended storage. The intramolecular disulfide bridge is sensitive to reducing conditions — avoid reductant-containing buffers unless specifically required by the assay. Avoid repeated freeze-thaw cycles of reconstituted material — single-use aliquots are preferred where peptide integrity is assay-critical. These handling parameters reflect general best-practice for lyophilized peptide reference standards and do not constitute preparation guidance for human or veterinary use.