Nuclear Factor NF-KB Inhibitor SN50 peptide

Nuclear Factor NF-KB Inhibitor SN50 peptide

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

AAVALLPAVLLALLAPVQRKRQKLMP

H-Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu-Ala-Pro-Val-Gln-Arg-Lys-Arg-Gln-Lys-Leu-Met-Pro-OH

26

95.8%

C₁₂₉H₂₃₀N₃₆O₂₉S

2781.54

213546-53-3

Synthetic

Powder

Nuclear Factor NF-KB Inhibitor SN50 is a cell-permeable nuclear translocation inhibitor of the transcription factor NF-KB. It consists of the hydrophobic region (h-region) of the Kaposi fibroblast growth factor (K-FGF) signal sequence which mediates the cellular import of this peptide and the nuclear localization signal (NLS) of the NF-KB p50 subunit. The peptide inhibited nuclear translocation of NF-KB in LPS- or TNF-alpha-stimulated murine endothelial LE-II and human monocytic THP-1 cells. In seve

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

• Y.-Z.Lin et al., J. Biol. Chem., 270, 14255 (1995)
• R.J.Salmond et al., Eur. J. Immunol., 32, 1737 (2002)
• M.A.Robbins et al., Endocrinology, 144, 4616 (2003)
• M.Guizzetti et al., Neuroscience, 120, 941 (2003)

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.