HGH Fragment 176-191 is a 16-amino-acid GH C-terminal peptide studied in preclinical adipose models for lipolysis promotion without IGF-1 stimulation, anabolic effects, or insulin resistance.
Product definition
What is HGH Fragment 176-191?
HGH Fragment 176-191 is a 16-amino-acid GH C-terminal peptide studied in preclinical adipose models for lipolysis promotion without IGF-1 stimulation, anabolic effects, or insulin resistance.
HGH Fragment 176-191 is a peptide fragment of the C-terminal helical region of human growth hormone, developed by researchers at Monash University (Melbourne) to isolate the lipolytic activity of GH from its growth-promoting and diabetogenic effects. The fragment spans residues 176 to 191 of the 191-amino-acid GH sequence.
The critical mechanistic discovery was that this C-terminal region — a helical structure — activates lipolysis in fat cells through a receptor pathway distinct from the GH receptor. The proposed mechanism involves β3-adrenoreceptor-like interaction, producing adenylyl cyclase activation and downstream lipolysis (triglyceride hydrolysis) and inhibition of lipogenesis (triglyceride synthesis from glucose).
In the Monash research series and subsequent published studies, fragment 176-191 produced statistically significant body fat reduction in obese rodent models versus vehicle controls, with the fat loss concentrated in visceral adipose depots. Critically, these effects were achieved without IGF-1 elevation (confirming lack of GH receptor engagement), without insulin resistance (confirming no GH-like diabetogenic effect), and without growth plate stimulation (confirming no growth-promoting activity).
Research context
How is HGH Fragment 176-191 described in the research literature?
HGH Fragment 176-191 activates lipolytic pathways in adipocytes through proposed β3-adrenoreceptor interaction, stimulating fat breakdown and inhibiting lipogenesis independently of GH receptor activation. In rodent models, it produces body fat reduction without the anabolic, growth-promoting, or diabetogenic effects of full-length GH — mechanistically dissecting GH's lipolytic dimension from its other biological activities.
Compound profile
Key facts about HGH Fragment 176-191
- Class
- GH C-terminal fragment peptide
- Sequence origin
- hGH residues 176–191 (16 amino acids)
- Molecular weight
- ~1,817 Da
- Mechanism
- Lipolysis promotion via β3-adrenoreceptor pathway; not GH receptor-mediated
- IGF-1 effect
- No IGF-1 elevation in animal studies
- Research category
- Adipose biology, lipolysis, GH pharmacology, metabolic research
- Storage
- Lyophilized: −20°C. Reconstituted: 2–8°C, use within 30 days
Research areas
What research areas is HGH Fragment 176-191 associated with?
- Studied for lipolysis promotion and lipogenesis inhibition in adipocyte models — without GH receptor engagement
- No IGF-1 elevation documented in animal studies — confirms isolated lipolytic mechanism vs anabolic GH effects
- No insulin resistance induction — distinguishes from full-length GH's diabetogenic properties
- Visceral fat reduction documented in obese rodent models with vehicle comparison
- Reference compound for mechanistic dissection of GH's adipose effects from its growth-promoting effects
- High research community awareness — most searched GH-derived lipolytic research peptide
Research audience
Who researches HGH Fragment 176-191?
HGH Fragment 176-191 is used by researchers in adipose tissue biology, GH pharmacology, lipolysis mechanisms, fat cell metabolism, and metabolic disease. It is specifically valuable for investigators who need to study GH-associated lipolytic mechanisms without the confounding effects of GH's anabolic and diabetogenic receptor activities.
Preclinical research overview
What does the preclinical literature say about HGH Fragment 176-191?
The Monash University research program on HGH Fragment 176-191 was motivated by the observation that full-length GH's clinical utility in treating obesity was limited by insulin resistance induction — essentially trading metabolic benefit (fat loss) for metabolic harm (glucose dysregulation). The hypothesis was that the lipolytic and anabolic/diabetogenic activities of GH were separable at the molecular level.
The fragment 176-191 work confirmed this hypothesis: the C-terminal helical region activates fat cell metabolism through a distinct pathway from the growth hormone receptor that mediates anabolic and diabetogenic effects. The Monash group published body composition studies in genetically obese (ob/ob) mice and diet-induced obesity models showing visceral fat reduction without metabolic liabilities.
The compound was also investigated briefly in early human research (Phase I/II metabolic studies in Australia) before development was discontinued for commercial reasons. The published preclinical and early clinical data remain in the literature as the mechanistic foundation for fragment 176-191 research.
AOD-9604 is a related compound — a modified version of fragment 176-191 with a disulfide bridge — that was developed in parallel from the same Monash research program and achieved FDA GRAS designation.
Common questions
Frequently asked about HGH Fragment 176-191
How does HGH Fragment 176-191 differ from full-length GH?
Full-length GH engages the GH receptor to produce anabolic effects (IGF-1 stimulation, protein synthesis, linear growth) and diabetogenic effects (insulin resistance, glucose dysregulation) alongside lipolysis. Fragment 176-191 does not bind the GH receptor — it activates lipolysis through a separate pathway (proposed β3-adrenoreceptor interaction). The result is lipolytic activity without the anabolic or diabetogenic receptor effects of full GH, enabling mechanistic dissection of GH's adipose biology.
What is the difference between HGH Fragment 176-191 and AOD-9604?
HGH Fragment 176-191 is the parent peptide — the native GH residues 176–191 without further modification. AOD-9604 is a modified version developed at Monash University that incorporates a disulfide bridge to modify the peptide's structural properties and receptor interaction. Both were developed from the same research program and studied for similar lipolytic endpoints; AOD-9604 additionally achieved FDA GRAS designation. They are structurally related but distinct research compounds.
Is there human research on HGH Fragment 176-191?
Early Phase I/II human metabolic studies were conducted in Australia as part of the Monash development program. These studies are in the published literature but the compound was not advanced through Phase III trials. The primary research base is preclinical rodent data. Early human data provides some translational context but should not be interpreted as clinical outcome evidence.
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Research Use Only
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