IFN-alpha Receptor Recognition Peptide 1 (IRRP1)

IFN-alpha Receptor Recognition Peptide 1 (IRRP1)

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

CLKDRHD

H-Cys-Leu-Lys-Asp-Arg-His-Asp-OH

7

96.5%

C₃₅H₅₉N₁₃O₁₂S

886.00

Synthetic

Powder

This peptide is derived from a consensus IFN-alpha sequence and corresponds to a putative receptor recognition domain of IFN-alpha. The binding capacity of cells for IFN-alphas was increased in the presence of IRRP1. Increased receptor occupancy resulted in increased phosphorylation-activation of the transcription factor ISGF3 and enhanced antiviral activity.

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

• E.N.Fish, FEBS Lett., 365, 87 (1995)

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.