TRAP-14 amide peptide

TRAP-14 amide peptide

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

SFLLRNPNDKYEPF

H-Ser-Phe-Leu-Leu-Arg-Asn-Pro-Asn-Asp-Lys-Tyr-Glu-Pro-Phe-NH2

14

98.1%

C₈₁H₁₁₉N₂₁O₂₂

1738.96 net

Synthetic

Powder

TRAP-14 amide has been shown to inhibit monocyte spreading on fibronectin-coated slides. The rapidly induced withdrawal of pseudopodial processes and rounding of the cells is accompanied by nitric oxide and endothelin-1release. Spreading might be inhibited by autocrine endothelin-1 release and subsequent endothelin B receptor-dependent nitric oxide production.

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

• K.D.Srivastava et al., J. Immunol., 161, 5039 (1998)

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.