S1H peptide

S1H peptide

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

Batch to batch variation of the purity

Ac-YIPKEQKYSFLQNPQT-NH2

Ac-Tyr-Ile-Pro-Lys-Glu-Gln-Lys-Tyr-Ser-Phe-Leu-Gln-Asn-Pro-Gln-Thr-NH2

16

95.19%

C₉₄H₁₄₁N₂₃O₂₇

2025.25

Synthetic

Powder

S1H is a 16-residue peptide designed as a direct sequence mimetic of the site 1 mini-helix (residues 36-51) of wild-type human growth hormone (hGH). S1H acts as an inhibitor by blocking the interaction of hGH with the human growth hormone receptor (hGHR). S1H mitigates phosphorylation of STAT5 in cells co-treated with hGH, reducing intracellular STAT5 phosphorylation levels to those of untreated controls. S1H can be used as a chemical tool to study the molecular nature of hGH–hGHR interactions.

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

• Basu et al (2021) A novel peptide antagonist of the human growth hormone receptor. J Biol Chem. 296 100588 PMID: 33774052

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.