Gluten Exorphin C peptide

Gluten Exorphin C peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

YPISL

H-Tyr-Pro-Ile-Ser-Leu-OH

5

95.3%

C₂₉H₄₅N₅O₈

591.71

142479-62-7

Synthetic

Powder

This peptide, isolated from the pepsin-trypsin-chymo-trypsin digest of wheat gluten, was considered as a δ-opioid receptor-selective ligand. The hydrophobicity of Ile3 seems to be important for the expression of the opioid activity of gluten exorphin C. Moreover, this peptide appears to be quite different from any of the endogenous and exogenous opioid peptides ever reported as the N-terminal Tyr is the only aromatic amino acid in the structure.

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

• C.Zioudrou et al., J. Biol. Chem., 254, 2446 (1979)
• F.R.Huebner et al., Peptides, 5, 1139 (1984)
• S.Fukudome et al., Peptide Chemistry 1991, A.Suzuki, ed., Protein Research Foundation, Osaka, p. 345, (1992)
• S.Fukudome and M.Yoshikawa, FEBS Lett., 316, 17 (1993)

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.