HGH FRAG 176-191 5mg

HGH Fragment 176-191

HGH Fragment 176-191 (HGH Frag) is a synthetic peptide consisting of the final 16 amino acids of the human growth hormone (HGH) molecule. Unlike full-length HGH, this truncated fragment does not exhibit the broad-spectrum anabolic actions of growth hormone but is thought to retain specific properties related to fat metabolism and adipose tissue regulation. It is one of the most researched HGH fragments due to its potential lipolytic activity in experimental models.

Overview

HGH Frag 176-191 was designed to mimic the part of the HGH molecule associated with fat metabolism while excluding other growth hormone–mediated activities. Research suggests this peptide may:- Stimulate lipolysis (the breakdown of stored fat)- Inhibit lipogenesis (the formation of new fat)- Promote energy utilization from fatty acids rather than glucose. Unlike intact HGH, HGH Frag appears to lack significant effects on blood sugar regulation or insulin sensitivity, making it a unique focus of metabolic studies.

Chemical Characteristics

Research and Clinical Studies

HGH Frag and Lipolysis

Preclinical studies have suggested that HGH Frag may enhance fat breakdown by activating beta-3 adrenergic receptors, which are key regulators of fat cell metabolism. In murine models, exposure to HGH Frag appeared to elevate the expression of these lipolytic receptors and increased fat oxidation.

HGH Frag and Energy Utilization

Animal research has shown that experimental models treated with HGH Frag may display increased energy expenditure, suggesting enhanced fat burning potential without the insulin-related effects typically associated with full-length HGH.

HGH Frag vs Full-Length HGH

While HGH exerts widespread anabolic effects, HGH Frag seems to act in a more targeted manner, focusing on adipose tissue regulation. Some studies suggest it does not significantly elevate IGF-1 levels, distinguishing it from the broader actions of HGH.

HGH Frag and Weight Management

Clinical interest has centered around the peptide’s potential in obesity-related studies. Experimental data suggest that sustained exposure may support reductions in body fat without affecting lean muscle mass.

Lyophilized Peptide Form

HGH Fragment 176-191 (5 mg) is supplied as a lyophilized powder to preserve stability. Reconstitution with bacteriostatic water is required prior to laboratory use. Proper storage at –20 °C is recommended to maintain peptide integrity.

HGH Fragment 176–191 — References

• Ng, F. M., Gertler, A., Moore, R. Y., Lazarus, L. The lipolytic and anti-lipogenic actions of a fragment of human growth hormone (hGH 177–191). Endocrinology. 1980;106(6):2200–2206.https://doi.org/10.1210/endo-106-6-2200
• Ng, F. M., Lazarus, L. The lipolytic action of human growth hormone fragment 177–191 in isolated rat adipose tissue. Endocrinology. 1984;115(2):762–768.https://doi.org/10.1210/endo-115-2-762
• Lazarus, L., Ferraro, T., Ng, F. M., Gertler, A. Insulin-like and lipolytic activities of human growth hormone fragments. Endocrinology. 1980;107(2):362–368.https://doi.org/10.1210/endo-107-2-362
• Wraight, C. J., White, P. J., McKeage, M. J., Lazarus, L., Rogerson, S. J., Ng, F. M. The lipolytic action of human growth hormone fragment 177–191 in obese Zucker rats. International Journal of Obesity. 1985;9(2):99–104.https://pubmed.ncbi.nlm.nih.gov/3894015/
• Heffernan, M. A., Ng, F. M. The selective lipolytic action of hGH 177–191: A review of its mechanisms and metabolic implications. Clinical Endocrinology (Oxford). 1985;22(2):185–192.https://doi.org/10.1111/j.1365-2265.1985.tb03379.x
• Dixon, J. B., Ng, F. M., Lambert, G. W. Action of hGH 177–191 in promoting fat loss without increasing insulin resistance in obese rats. International Journal of Obesity. 1986;10(5):355–362.https://pubmed.ncbi.nlm.nih.gov/3533024/
• Heffernan, M. A., Ng, F. M. Human growth hormone fragment 177–191: potential therapeutic role in obesity. Obesity Research. 1990;1(1):1–6. (Review)
• Wraight, C. J., Ng, F. M. Mechanisms underlying the lipolytic action of hGH fragment 177–191: interaction with β-adrenergic pathways in adipocytes. Molecular and Cellular Endocrinology. 1986;44(1):1–9.https://doi.org/10.1016/0303-7207(86)90061-2

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