Everything below concerns AOD-9604. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Updated 2026-01-24. Numbers and descriptions here follow the published literature rather than marketing material.
AOD9604 is commonly supplied as a white to off-white lyophilized powder. The powder is typically stored at -20 °C or below, protected from light and moisture, because peptides can degrade through oxidation, hydrolysis, or aggregation. If it is reconstituted for laboratory use, an appropriate aqueous buffer or solvent is chosen, and the solution is kept cold and handled to avoid repeated freeze-thaw cycles. These practices support stability but do not imply suitability for human use.
Identity and purity are usually assessed with reversed-phase high-performance liquid chromatography and mass spectrometry. Reversed-phase HPLC separates the peptide from related impurities and can estimate purity by ultraviolet absorbance, while mass spectrometry confirms the molecular mass and detects modifications. Peptide mapping, amino acid analysis, and disulfide mapping may be used when the sequence or disulfide arrangement must be verified. Because AOD9604 contains cysteine residues, oxidation and disulfide isomers are possible quality concerns in synthetic batches.
Quality varies among research-grade suppliers, so certificates of analysis and independent testing are important for verification. A typical certificate reports purity by HPLC, identity by mass spectrometry, appearance, and sometimes residual solvents or water content. AOD9604 is often sold as a research chemical not intended for human consumption, and labels can be inaccurate. Common misconceptions include treating the peptide as a form of growth hormone, assuming supplement status, or expecting approved-drug quality from unregulated products.
AOD-9604 is a synthetic peptide whose sequence matches the C-terminal fragment of human growth hormone, specifically residues 176 through 191. This region differs from the full hormone in its receptor interactions. The peptide is not a growth hormone secretagogue and does not bind the growth hormone receptor in the same manner. Researchers have examined it for effects on lipid metabolism, but its exact pharmacological profile remains an active area of study.
Development of AOD-9604 began in the 1990s as scientists sought to isolate metabolic effects of growth hormone without its growth-promoting actions. Early laboratory work focused on fat cells and animal models. Several human trials followed, examining changes in body composition and fat mass. Results have been mixed, and the peptide has not progressed to widespread clinical approval. Interest continues in research settings, particularly regarding its mechanism and potential metabolic targets.
Regulatory status varies by country. In the United States, AOD-9604 is not approved as a prescription drug. It is sometimes sold as a research chemical or dietary supplement, though such marketing may fall outside legal frameworks. The World Anti-Doping Agency prohibits its use in sport. Researchers must obtain it through legitimate suppliers and follow institutional rules. Its legal classification continues to evolve as authorities increasingly assess peptide products more broadly.
| Property | Value | Notes |
|---|---|---|
| Appearance | White to off-white powder | Lyophilized form; visual inspection |
| Solubility | Soluble in water and aqueous buffers | Depends on pH, purity, and counterion |
| Typical storage | -20 °C or below, desiccated | Protect from light; avoid repeated freeze-thaw after reconstitution |
| Common analytical method | Reversed-phase HPLC and mass spectrometry | Purity by HPLC; identity and mass by LC-MS or MALDI-TOF |
| Common synonyms | hGH fragment 176–191; AOD-9604 | Names vary in research and product labeling |
Analytical characterization of AOD-9604 typically employs reversed-phase high-performance liquid chromatography (RP-HPLC) to assess purity and identity. Mass spectrometry provides confirmation of molecular mass, while amino acid analysis can verify composition. These methods are standard for peptide research chemicals. Because the peptide lacks a distinct chromophore, detection often relies on ultraviolet absorbance at 214 nm or mass spectrometric response. Laboratories may also use capillary electrophoresis for separation. For example, size-exclusion chromatography can detect aggregates.
Stability of AOD-9604 depends on storage conditions. Lyophilized powder is generally more stable than reconstituted solution. Recommended storage is typically at -20°C or lower, protected from light and moisture. Repeated freeze-thaw cycles can cause aggregation or degradation. In solution, the peptide may be susceptible to hydrolysis or oxidation, so aliquoting and cold storage are common practices. Researchers often add stabilizers such as mannitol or trehalose during lyophilization to improve shelf life.
Regulatory status: AOD-9604 is not approved as a therapeutic drug in the United States, European Union, or other major markets. It is listed by the World Anti-Doping Agency as a prohibited substance in sport, specifically under growth hormone fragments. Many jurisdictions restrict its sale for human consumption. Products marketed online may not meet pharmaceutical quality standards. The legal status varies by country and often depends on whether the material is presented as a research chemical, supplement, or drug.
Detection and characterization of AOD-9604 in research and anti-doping settings typically rely on mass spectrometry coupled with liquid chromatography. These methods can identify the peptide by its mass and fragmentation pattern. Immunoassays may also be used in some screening contexts, but they can cross-react with related peptides. Because the molecule is small and may be present at low concentrations, sample preparation and method validation are important. Confirmatory analysis usually requires comparison with a certified reference standard.
dipolar bond Also coordinate covalent bond, coordinate bond, dative bond, and semipolar bond. A type of covalent bond formed by the coordination of two or more electrically neutral moieties, the combination of which results in a charge-separated molecule or coordination complex, in which two electrons deriving from the same atom are shared between the donor atom and an acceptor atom, creating an internal two-center molecular dipole moment.
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== History == Scientists in Japan began to collaborate as early as 1939 on the development of an electron microscope. Kenji Kazato and Kazuo Ito met while working at the Naval Central Institute in Tokyo during World War II. After the war, Kazato attracted Ito and a group of others to Mobara, Chiba Prefecture, Japan. This initial group developed a prototype magnetic field–type electron microscope called the DA-1, which was sold to Mitsubishi in 1947. Because of differences over the direction of this early company, Kazato and Ito chose to found a new organization. The Japan Electron Optics Laboratory Company, Limited (Nihon Denshi Kogaku Kenkyujo) was founded in 1949 by Kenji Kazato and Kazuo Ito in Mitaka, Tokyo. It produced its first commercial model transmission electron microscope, the JEM-1, a year later. Overseas sales began in 1956 with the sale of a system to France. The company's strengths were the customization of orders to fit customer requests, and the provision of strong customer support. In 1961, the company was renamed JEOL, Limited. Its first overseas subsidiary, JEOL Company (USA) Inc., was established in 1962 and headquartered in Peabody, MA. JEOL was listed on the Second Section of the Tokyo Stock Exchange by 1962, and on the First Section of the Tokyo Stock Exchange by 1966. The company expanded from electron microscopy to nuclear magnetic resonance (NMR), releasing the first NMR system in Japan, the JNM-1, in 1956. They produced their first mass spectrometer in 1963, and their first scanning electron microscope in 1966.
Sources: en.wikipedia.org
== Properties == Silica gel's high specific surface area—around 750–800 m2/g (230,000–240,000 sq ft/oz)—allows it to absorb water readily, making it useful as a desiccant (drying agent). Silica gel is often described as "absorbing" moisture, which may be appropriate when the gel's microscopic structure is ignored, as in silica gel packs or other products. However, material silica gel removes moisture by adsorption onto the surface of its numerous pores rather than by absorption into the bulk of the gel. Silica gel is able to absorb up to 37% of its own weight in moisture in high-humidity environments. This moisture can be released upon heating at about 120 °C (248 °F) for 1–2 hours. This makes it reusable multiple times with very little, if any, loss of efficiency.
Photoacoustic Tomography (PAT) is a hybrid imaging modality that utilizes the photoacoustic effect without the use of ionizing radiation. It works without contact with very fast laser pulses that generate ultrasound in the tissue under examination. The local absorption of the light leads to sudden local heating and the resulting thermal expansion. The result is broadband acoustic waves. The original distribution of absorbed energy can be reconstructed by measuring the outgoing ultrasound waves with appropriate ultrasound transducers.
SEA is an abbreviation of bis(2-sulfanylethyl)amido (Scheme 1). SEA ligation involves the reaction of a peptide featuring a C-terminal bis(2-sulfanylethyl)amido group with a Cys peptide. This reaction proceeds probably through the formation of a transient thioester intermediate, obtained by intramolecular attack of one SEA thiol on the peptide C-terminal carbonyl group as shown in Scheme 1. Then, the thioester undergoes a series of thiol-thioester exchanges, including with exogeneous thiols present in the ligation mixture such as mercaptophenyl acetic acid (MPAA). Exchange with the cysteine thiol group of the second peptide segment results in a transient thioester intermediate, which as for Native Chemical Ligation, rearranges by intramolecular S,N-acyl shift migration into a native peptide bond.
Sources: en.wikipedia.org
Lyophilized AOD9604 is generally kept at -20 °C or colder, desiccated, and protected from light. Reconstituted solutions are usually refrigerated and handled to minimize repeated freeze-thaw cycles. These are general laboratory handling practices, not instructions for human use.
Mass spectrometry, such as LC-MS or MALDI-TOF, confirms the molecular mass and can reveal sequence-related impurities. Reversed-phase HPLC is used for purity, and peptide mapping or amino acid analysis can support sequence identity. No single method establishes every quality attribute.
No. AOD9604 is a short synthetic fragment of the hGH sequence, not the full 191-amino-acid hormone. It lacks the regions that mediate hGH receptor activation and growth-promoting effects. Products labeled as AOD9604 should not be assumed to have the same properties as hGH.
AOD-9604 is a synthetic peptide fragment of human growth hormone, corresponding to amino acids 176-191. It is studied for potential effects on fat metabolism, but it is not approved as a drug in most countries. Its exact mechanism remains under investigation.