Research Use Only — documentation confirmed by inquiry
AOD9604
| Units | Discount |
|---|---|
| 1–2 | 0% |
| 3–4 | 10% |
| 5–6 | 15% |
| 7–9 | 20% |
| 10–+ | 30% |
AOD9604 (modified human growth hormone fragment 176-191) · ≥98% (HPLC)
AOD9604 is a synthetic 16-residue fragment of human growth hormone (residues 176-191) supplied as a characterized reference material for in-vitro lipid-metabolism research, independent of the GH/IGF-1 axis. Research Use Only.
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Research context and documentation
- Why researchers study it
- Studied in vitro as a fragment-based probe for isolating the lipid-metabolism-associated region of human growth hormone from its growth-promoting (GH-receptor-mediated) activity.
- Mechanism themes in research
- Lipolytic signaling independent of GH-receptor/IGF-1 activationDisulfide-constrained (Cys7–Cys14) fragment stability chemistryStructure-activity mapping of the HGH C-terminal regionAnalytical reference standardization for fragment-peptide identity
- What the evidence does not establish
- Published references describe research context only. They do not establish safety, efficacy, biological activity, or any outcome in humans or animals, and HELIX BioScience makes no such claims.
- Quality markers
- ≥98% (HPLC)MS contextCOA statusStorage stated where verified
- Documentation status
- Product specifications and COA status are shown on this page. Current lot documentation is provided when issued and matched to the offered lot.
AOD9604 is a synthetic 16-residue fragment related to the C-terminal region of human growth hormone. It is supplied as a characterized reference material for in-vitro peptide chemistry, fragment structure–activity work, and lipid-metabolism research. The page is intentionally framed around laboratory evidence and does not provide human-use or dosing guidance.
Identity and fragment design
AOD9604 is commonly described as a modified human growth-hormone fragment corresponding to residues 176–191, with a disulfide-constrained sequence and a reported molecular weight near 1815.1 g/mol. Public records list CAS 221231-10-3 and a molecular formula of C₇₈H₁₂₃N₂₃O₂₃S₂. Researchers should reconcile catalog data with the lot-specific COA, especially when comparing salts, sequence conventions, or analytical reporting formats.
Why fragments are useful
Peptide fragments can help investigators study one structural region without attributing every observation to the full parent protein. AOD9604 is therefore relevant to experiments that separate C-terminal fragment behavior from growth-hormone-receptor and IGF-axis signaling. This is a research design question: the value of a fragment depends on the assay, controls, purity, and whether the experiment can distinguish direct activity from degradation or matrix effects.
| Full name | AOD9604 (modified human growth hormone fragment 176-191) |
| Research theme | Metabolic signaling |
| CAS number | 221231-10-3 |
| Molecular formula | C₇₈H₁₂₃N₂₃O₂₃S₂ |
| Molecular weight | 1815.1 g/mol |
| Purity | ≥98% (HPLC) |
| Physical form | Lyophilized powder |
| Storage | −20 °C, desiccated, protected from light |
Sequence
Reported research areas
- Lipid-metabolism signaling independent of GH-receptor activation
- Structure-activity studies of HGH C-terminal fragments
- Disulfide-constrained peptide stability chemistry
- Analytical reference standard for peptide identity and purity (HPLC/MS)
Credible sources
- PubChem — AOD9604
- PubMed — AOD9604 and human growth-hormone fragment research
- PubMed — growth hormone residues 176–191
COA status shown
Request the current documentation packet for the offered material. When available, it identifies the reported HPLC result and any identity method; public product specifications are not current lot results.
- HPLC result, when reported
- Identity method, when reported
- Appearance, molecular weight, and storage where documented
- Lot number and testing status
Specimen Certificate of Analysis
| Product | AOD9604 (reference) |
| Status | Format preview — not a current lot |
| Purity (RP-HPLC) | 98%+ |
| Identity (MS) | Confirmed · 1815.1 g/mol |
| Appearance | Lyophilized powder |
| Storage | −20 °C, desiccated |
Format preview only. Current lot records and measured results are not published here until supplied and verified.
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