lyophilized powder is one of those subjects where the details matter more than the headlines. This page pulls together the background, the mechanisms, and the practical points readers ask about most.
Last reviewed on 2026-03-19. Where a claim depends on a specific study, the study is described rather than over-claimed.
AOD-9604 is a synthetic peptide modeled on the C-terminal region of human growth hormone. It corresponds to residues 176-191 of the 191-amino-acid hGH sequence. The fragment is not the full hormone and lacks the receptor-binding region associated with growth and metabolic effects of hGH. Researchers developed it to isolate a specific portion of hGH for study. Its exact sequence and length are often stated in peptide catalogs and patents.
The peptide is frequently described as a growth hormone fragment, although it is chemically distinct from full-length hGH. AOD-9604 contains 16 amino acids and includes two cysteine residues that can form an intramolecular disulfide bond. In solution, this structural feature can influence folding, aggregation, and stability. Published descriptions sometimes call it hGH 176-191 or AOD9604, with spacing and capitalization varying. Such naming differences can complicate literature searches, database entries, and product verification.
Researchers have studied the fragment in cell and animal models to understand its metabolic actions. Some experiments report effects on fat breakdown and fat storage pathways, but the underlying mechanism remains incompletely defined. AOD-9604 does not appear to stimulate the same broad growth hormone receptor signaling as full-length hGH. Whether its observed activities arise from direct receptor interactions or downstream metabolic changes is an open question. Results from different assays are not always consistent.
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.
Quality control for AOD-9604 involves verifying identity, purity, and concentration. Suppliers may provide a certificate of analysis listing HPLC purity and mass spectrometry data. Independent verification is advised because peptide products can vary in quality. Researchers should check for counterions, residual solvents, and microbial contamination. Proper documentation supports reproducibility and safety in laboratory studies. When sourcing, institutions often require third-party testing and detailed chain-of-custody records. These steps help ensure that experimental results are attributable to the peptide rather than impurities.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic peptide | Derived from a fragment of human growth hormone |
| Sequence basis | hGH residues 176-191 | Commonly described as a 16-amino-acid fragment |
| Appearance | White to off-white powder | Typical for lyophilized research peptides |
| Solubility | Soluble in water or aqueous buffer | Exact solubility depends on pH and purity |
| Common synonyms | AOD9604; hGH 176-191 | Spelling and punctuation vary across sources |
AOD-9604 is a synthetic peptide whose sequence is modeled on the C-terminal region of human growth hormone. Published descriptions commonly place it as a modified fragment corresponding to hGH amino acids 176–191, with a tyrosine residue added or retained at the N-terminus to support detection and handling. It is not intact growth hormone and lacks the full receptor-binding architecture of the parent protein. The molecule was developed as a research candidate for metabolic studies rather than as a replacement for growth hormone therapy. Its identity is defined by its amino acid sequence rather than by any single commercial preparation.
AOD-9604 drew attention in the 1990s and 2000s as a potential anti-obesity agent. Early work explored both injectable and oral routes, which is unusual for a peptide of this size. Animal studies reported changes in fat metabolism without the growth-promoting or insulin-like effects associated with full-length growth hormone. Subsequent human trials produced mixed or modest results, and the compound did not obtain regulatory approval for weight management in major markets. It remains known mainly through research literature, sports anti-doping listings, and non-approved supplement advertising.
AOD-9604 is prohibited in sport by the World Anti-Doping Agency under the peptide hormone class. Its presence in a sample can be detected through mass spectrometry-based methods, although the exact assay depends on the laboratory. In research settings, material is often supplied as a lyophilized powder for reconstitution. Buyers and researchers should note that products labeled AOD-9604 may vary in purity and actual peptide content. Analytical certificates and independent testing are common ways to verify identity, but no global harmonized standard exists for all commercial lots.
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.
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.
== Filme == Klitoris – Die schöne Unbekannte. Komplett-Media (September 2007), ISBN 978-3-8312-9488-6, © ARTE Frankreich 2002. Ein Film von Stefan Firmin und Michele Dominici im Auftrag von ARTE. Klitoris – Die schöne Unbekannte. Arte-Dokumentation auf YouTube: Teil 1, Teil 2, Teil 3, Teil 4, Teil 5, Teil 6, Teil 7, abgerufen am 28. Dezember 2011 Die Klitoris - Animated Documentary. Ein animierter Kurzfilm von Lori-Malépart Traversy.
Sicht auf den Damm, „Perineum“ mit Gefäßversorgung. Abbildung eines anatomischen Präparats auf: ect.downstate.edu; abgerufen am 9. Juli 2015. Anatomie der Klitoris. Abbildung eines anatomischen Präparats Auf: ect.downstate.edu; abgerufen am 9. Juli 2015. Barbara Maier, Luci Wohlfart: Klitoris, die unbekannte Schöne. Unbekannte – unbenannte weibliche Anatomie und weibliches Lusterleben. Landeskrankenhaus Salzburg, Volltext online. Elia Bragagna: Die Physiologie der weiblichen sexuellen Erregung. (Volltext online Auf: studylibde.com). Sharon Mascall: Time for rethink on the clitoris. über Helen O’Connells Entdeckung (englisch) Auf: news.bbc.co.uk, letztes Update vom 11. Juni 2006; abgerufen am 9. Juli 2015. Anne Fawcett: Anatomy of a revolution – Helen O’Connell has changed the way students learn about the female body. Auf: smh.com.au, 8. September 2005 (englisch), abgerufen am 9. Juli 2015. Petra Stute – Universitätsspital Bern: Der weibliche Orgasmus. Physiologie und Pathophysiologie, hormonelle Einflüsse und weibliche Orgasmusstörung. (Volltext als PDF; 14 MB) Auf: klinikschuetzen.ch, abgerufen am 31. Juli 2018. Daniel Haag-Wackernagel: Das weibliche Erregungssystem aus Sicht der Evolutionsbiologie. Departement Biomedizin der Universität Basel, 2017 (Volltext als PDF; 1,2 MB).
Die extrazelluläre Matrix (Extrazellularmatrix, Interzellularsubstanz, EZM; englisch extracellular matrix, ECM) ist der Gewebeanteil (vor allem im Bindegewebe), der zwischen den Zellen im sogenannten Interzellularraum liegt. Die extrazelluläre Matrix setzt sich aus diversen Komponenten zusammen, die in zwei große Gruppen eingeteilt werden: Grundsubstanz und Fasern. Das Verhältnis der Grundsubstanz zum Faseranteil schwankt je nach Lokalisation ebenso wie der Anteil der extrazellulären Matrix am Gewebe insgesamt, bedingt durch dessen jeweilige Funktion. Bei Pflanzenzellen spricht man nicht von einer extrazellulären Matrix, auch wenn bei diesen ebenfalls ein substanzerfüllter Interzellularraum vorliegt.
== Grundsätzliches == Zunächst schrieb man – vereinfacht gesehen – den Hauptkomponenten der extrazellulären Matrix lediglich eine Funktion als „Leim“ (daraus Kollagen) oder als gewebeinterner Wasserspeicher (Mucopolysaccharide, Proteoglykane) zu. Die EZM umfasst nach heutiger Sicht die Gesamtheit der Makromoleküle, die sich außerhalb der Plasmamembran von Zellen in Geweben und Organen befinden. So dient die EZM – oberflächlich betrachtet – primär als eine Fixierungsmöglichkeit für die in ihr eingebetteten Zellen aller Gewebetiere. Zwischen Zellen und EZM herrscht aber stets eine wechselseitige Interaktion. Die EZM ist nicht statisch, sondern muss auf molekularer Ebene als im Fließgleichgewicht verstanden werden. Die Komponenten der EZM werden von Zellen synthetisiert und sezerniert, teilweise erst extrazellulär über weitere Bindungen fixiert und schließlich extrazellulär oder nach Endozytose intrazellulär abgebaut. Darüber hinaus wird durch die Bindung an bestimmte Komponenten der EZM durch Zellrezeptoren die Expression von Genen in den Zellen reguliert. Zelladhäsion, Zellmigration, Zellproliferation sowie der Aufbau, Umbau und Abbau von Gewebe resultieren damit ebenso aus der wechselseitigen Beeinflussung, die EZM und Zellen widerfährt. So können z. B. Moleküle, die als strukturgebende Proteine vorliegen, unter anderen Bedingungen Botenstoffe darstellen. Im Rahmen der Gordon-Konferenz für Proteoglykane von 1998 wurde eine treffende Charakterisierung dieser Eigenschaften von EZM-Komponenten geprägt.
Sources: de.wikipedia.org
No, it is a synthetic peptide fragment corresponding to a small portion of hGH. It is not the full 191-amino-acid hormone and does not reproduce all of hGH's effects.
It is commonly described as a 16-amino-acid peptide based on residues 176-191 of human growth hormone. Some sources vary in notation, so checking the stated sequence is useful.
It is not typically described as a standalone natural hormone. The sequence is derived from the C-terminal region of human growth hormone, but the synthetic peptide is a laboratory-made construct.
Reversed-phase HPLC is used to assess purity, and mass spectrometry confirms molecular mass. Amino acid analysis can verify composition. These methods are standard for peptide characterization.