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AOD-9604 (5mg)

$45.00

* The information on this page is a summary and is not intended to cover all available information about this medication. It does not cover all possible uses, directions, precautions, drug interactions or adverse effects and is not a substitute for the expertise and judgement of your healthcare professional.

Key Specifications

Category Parameter Specification / Details
Identification & Nomenclature Primary Compound Name AOD-9604 (HGH Fragment 177-191)
CAS Registry Number 221231-10-3
Sequence / IUPAC Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe
Chemical & Physical Properties Molecular Formula C78H123N23O23S2
Molar Mass / Weight 1815.1 g/mol
Physical Appearance White lyophilized (freeze-dried) solid/powder
Solubility Profile Highly soluble in Bacteriostatic Water and sterile water.
Product Specifications Tested Purity ≥98% via HPLC
Active Ingredient (Total) 5mg per vial
Dry / Powder Formulations Lyophilized powder
Handling & Logistics Storage Guidelines Lyophilized: Store at -20°C for long-term stability. Protect from light.Reconstituted: Must be refrigerated at 2°C to 8°C.
Estimated Shelf Life 24 months from manufacture date (lyophilized).
Terms of Application For laboratory research purposes only. Not for human or veterinary use. Investigated as a C-terminal peptide fragment of hGH to evaluate beta-3 adrenergic receptor modulation and targeted lipolysis in in-vitro adipocyte assays, specifically without inducing IGF-1 or altering glucose homeostasis.

Foundational Scientific Overview

AOD-9604 (5mg) is a highly specialized subject within the field of localized lipolysis and beta-adrenergic receptor modulation. Synthesized as a modified C-terminal fragment of human Growth Hormone (tyrosine-hGH 177-191), it has become a staple for researchers examining fat catabolism without the associated anabolism, IGF-1 elevation, or insulin resistance typical of full-length GH.

At 4 Amino Labs, we provide this highly purified peptide fragment to ensure experimental reproducibility across varied lipid metabolic assays.

Scientific Literature Reference: The biochemical isolation of the lipolytic domain of human growth hormone, proving its capacity to upregulate fat oxidation independently of the growth hormone receptor, is a cornerstone of lipolytic research. See: Heffernan, M. A., et al. (2001). “The effects of human GH and its lipolytic fragment (AOD9604) on lipid metabolism following chronic treatment in obese mice and beta(3)-AR knock-out mice.” Endocrinology, 142(12), 5182-5189.

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