Hexarelin peptide

Hexarelin peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-His-D-2-Me-Trp-Ala-Trp-D-Phe-Lys-NH2

6

98.1%

C₄₇H₅₈N₁₂O₆

887.04

Synthetic

Powder

Hexarelin is also named: Hexarelin. CAS NO.: 140703-51-1. Hexarelin (Hexarelin Acetate) is a synthetic hexapeptide in the growth factor family which stimulates the release of growth hormone (GH) and does not interfere with the body's ability to produce its own GH. Structurally, Hexarelin (Hexarelin Acetate) is similar in structure to GHRP-6 but without the appetite increase because of its inability to drastically increase Ghrelin levels which is responsible for the increased appetite and quicker gastric emptying. Hexarelin is a synthetic growth hormone secretagogue made from six amino acids. It contains powerful growth hormone releasing properties in the human body. Hexarelin in studies over a certain period has shown that it reduces visceral fat. Hexarelin (Hexarelin Acetate) like other Growth Hormone Releasing Peptides is most effective synergistically when administered with GHRH such as Sermorelin or Modified GRF 1-29. The increase of circulating GH through Hexarelin use causes levels of Insulin-Like Growth Factor (IGF-1) to rise in the liver. IGF-1 is the prime cause of muscle growth in response to GH stimulation. Users of IGF-1 typically experience increased strength and muscle mass, as well as a very pronounced fat loss.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Deghenghi R, Cananzi MM, Torsello A, Battisti C, Muller EE, Locatelli V. GH-releasing activity of Hexarelin, a new growth hormone releasing peptide, in infant and adult rats. Life Sci. 1994;54(18):1321-8.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.