Research Spotlight

AOD-9604: Research Overview

PūrTONIX Analytical TeamMarch 25, 20253 min read

Research Use Only — Regulatory Notice

All information contained in this article is derived exclusively from publicly available scientific literature, peer-reviewed academic publications, and publicly accessible research databases. This content is provided strictly for educational and informational purposes in the context of laboratory research.

PūrTONIX does not make any medical, therapeutic, or clinical claims. None of the compounds discussed have been approved by the U.S. Food and Drug Administration (FDA) for human use, diagnosis, treatment, or prevention of any disease or condition, except where explicitly noted for approved pharmaceutical forms.

This article does not constitute medical advice. These compounds are sold by PūrTONIX strictly as laboratory research reagents for in vitro use only. They are not intended for human or veterinary administration, dietary supplementation, or any therapeutic application.

All citations reference publicly available research. PūrTONIX makes no representations regarding the replication, accuracy, or applicability of any referenced study.

Compound Overview

Full name: Tyrosyl-human growth hormone (177-191) fragment with two cysteine disulfide-bridged residues
Molecular formula: C78H123N23O23S2
Molecular weight: 1815.10 g/mol
Sequence / class: Synthetic 16-residue C-terminal fragment of human growth hormone (residues 177-191) with an N-terminal tyrosine addition and an internal disulfide bridge between two cysteine residues
Receptor targets: Published in vitro literature describes the parent hGH C-terminal region in the context of lipid-handling biochemistry research; receptor-engagement studies remain limited in the publicly available literature
Research classification: Synthetic hGH C-terminal fragment research reagent for in vitro biochemical investigation
PubChem CID: 16132326

AOD-9604 is a synthetic 16-residue peptide derived from the C-terminal region of human growth hormone (residues 177-191) with an N-terminal tyrosine addition and an internal disulfide bridge between the two cysteine residues. The molecular formula is C78H123N23O23S2 with a calculated mass near 1815 daltons. The disulfide bridge is essential to the analytical identity of the molecule and requires care during reconstitution and handling.

Published literature classifies AOD-9604 as a synthetic hGH C-terminal fragment research reagent. The compound was developed initially as an analytical probe for studying the biochemistry of the C-terminal region of growth hormone independent of the receptor-engaging domains that define the full-length parent protein. Receptor-binding studies in publicly available literature remain limited, and the in vitro research on the fragment focuses primarily on biochemical-pathway-level observations rather than on a defined receptor target.

Research published in the peer-reviewed literature has used AOD-9604 in cellular biochemistry studies that examine lipid-handling pathway readouts in adipocyte-derived cell lines and in primary cell preparations. The compound is supplied as a lyophilized analytical reagent for reconstitution in aqueous buffer for in vitro biochemistry use.

Published research suggests that the AOD-9604 fragment does not reproduce the full receptor-engagement profile of intact human growth hormone, which has positioned the compound in the published literature as an analytical tool for dissecting the contribution of the C-terminal region rather than as a growth-hormone-receptor agonist.

Molecular Structure

AOD-9604

C78H123N23O23S2

Molecular weight 1815.10 g/mol

Structure reference: Public domain chemical databases (PubChem CID 16132326).

In Vitro Research Applications

The following applications reflect published in vitro and preclinical research only. None of these applications constitute approved medical use.

Published in vitro applications of AOD-9604 include its use in adipocyte-derived cell line lipid-handling assays, in vitro lipase-activity assays, and biochemical fractionation studies that read out the response of cellular lipid metabolism enzymes under defined buffer conditions. Investigators have used the fragment as a comparator against the full-length hGH protein to isolate the contribution of the C-terminal sequence.

Comparative in vitro literature has paired AOD-9604 with the intact human growth hormone protein in matched cellular models, allowing investigators to characterize how the truncated C-terminal fragment behaves independently of the receptor-engaging N-terminal domains of the parent protein.

Additional published research has used AOD-9604 in cellular signaling studies that examine MAPK and lipase activation kinetics under controlled in vitro conditions, with the disulfide-bridged structure maintained throughout the assay timecourse.

Published Research Highlights

[1]A study published in Biochemical Pharmacology (2001) examined the biochemistry of the human growth hormone C-terminal fragment in cellular adipocyte model systems.
[2]A study published in International Journal of Obesity (2004) investigated lipid-handling pathway biochemistry using a synthetic hGH C-terminal fragment in publicly available in vitro studies.
[3]A study published in Hormone Research (2007) reviewed publicly available literature on synthetic growth-hormone-fragment research reagents and their in vitro behavior.

The above represents a non-exhaustive summary of publicly available research. PūrTONIX does not endorse, validate, or make claims based on any referenced study.

Analytical Considerations for Laboratory Use

Published chemical property data indicate that AOD-9604 is soluble in water and in aqueous assay buffers under conditions that preserve the internal disulfide bridge. The lyophilized peptide is stored at -20°C under inert atmosphere with care to avoid reducing conditions during reconstitution and storage. Reconstituted stocks are held in single-use aliquots at 2-8°C for short-term in vitro use.

Reconstitution in bacteriostatic water or in assay-matched buffer is standard. Analytical characterization commonly includes reverse-phase HPLC purity analysis, electrospray mass spectrometry confirming the disulfide-bridged 16-residue sequence, and residual solvent screening per ICH Q3C.

Handling recommendations are based on published chemical property data and are intended for qualified laboratory personnel only.

Research-Grade Sourcing Standards

Disulfide-bridge integrity is the critical analytical attribute for AOD-9604. Material characterized for high chromatographic purity with mass-spectral data confirming intact disulfide-bonded structure are the analytical baseline for reproducible in vitro biochemistry research.

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