Dermorphine 8 peptide

Dermorphine 8 peptide

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

Batch to batch variation of the purity

YaFWYPN-NH2

H-Tyr-D-Ala-Phe-Trp-Tyr-Pro-Asn-NH2

7

97.98%

C₅₀H₅₈N₁₀O₁₀

959.06

Synthetic

Powder

Dermorphin and deltorphin are naturally occurring heptapeptides purified from skin extracts of the South American frog Phyllornedusa sauvagei that show high affinity and selectivity for μ and δ opioid receptors, respectively. They share a similar N-terminal tripeptide sequence Tyr-D-Xaa-Phe, where D-Xaa is either D-Ala (dermorphin) or D-Met (deltorphin), and have an amidated COOH terminus. The two dermorphin-like peptides(Dermorphin 1 and Dermorphin 8) have a similar affinity and selectivity for the mu opioid receptor as dermorphin.

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

• Mignogna G, Severini C, Simmaco M, et al. Identification and characterization of two dermorphins from skin extracts of the Amazonian frog Phyllomedusa bicolor. FEBS Lett. 1992;302(2):151-4.

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.