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Tesamorelin
Tesamorelin

Tesamorelin

Tesamorelin is a synthetic research peptide modeled after growth hormone–releasing hormone (GHRH).

It is widely studied in preclinical environments for its interaction with growth hormone pathways, IGF-1 signaling, and hypothalamic–pituitary axis regulation.

Research investigates how Tesamorelin may influence cellular markers associated with growth hormone secretion dynamics, peptide-receptor interaction, and downstream metabolic signaling. All existing mechanistic data arise from laboratory and animal studies unless otherwise noted.

Tesamorelin offered here is intended strictly for laboratory research purposes and is not approved for human use, therapeutic applications, or clinical administration.

Clinical References

  1. Wierman, M.E., et al. (2013). Regulation of GHRH receptor signaling. Molecular Endocrinology.
  2. MacGillivray, M.H., et al. (2015). Pituitary responses to GHRH analogs in preclinical systems. Endocrine Research.
  3. Sun, Y., et al. (2019). Molecular mechanisms of peptide-induced GH secretion. Journal of Peptide Science.
  4. Huang, Z., et al. (2021). Stability and pharmacologic properties of modified GHRH peptides. Biochemical Pharmacology.
  • GHRH Receptor Interaction: Preclinical models show Tesamorelin binds to and activates GHRH receptors in pituitary tissues.
  • Pulsatile GH Signaling: Laboratory studies observe GH secretion patterns that follow physiologic pulsatility under GHRH analog exposure.
  • IGF-1 Pathway Modulation: Cellular and animal research indicates changes in IGF-1–related biochemical markers downstream of GH signaling.
  • Neuroendocrine Regulation: Some studies examine hypothalamic involvement in the regulation of GH-related hormone cascades.
  • Metabolic Signaling Markers: Preclinical environments have reported shifts in markers associated with lipid metabolism, glucose signaling, and energy-regulatory pathways.
  • Peptide Stability: Research explores modifications that enhance peptide half-life, receptor binding, and molecular stability.
  • Receptor Specificity: Studies highlight selective action on GHRH receptors without significant binding to unrelated peptide receptors.

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