TAT-HuR-HNS3 peptide

TAT-HuR-HNS3 peptide

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

Batch to batch variation of the purity

H-YGRKKRRQRRRSPMGVDHMSGLSGVNVPGNASSG-OH

H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Ser-Pro-Met-Gly-Val-Asp-His-Met-Ser-Gly-Leu-Ser-Gly-Val-Asn-Val-Pro-Gly-Asn-Ala-Ser-Ser-Gly-OH

34

95.98%

C₁₅₁H₂₅₇N₅₉O₄₆S₂

3699.14

Synthetic

Powder

TAT-HuR-HNS3 is a cell penetrating peptide derived from the human antigen R - nucleocytoplasmic shuttling sequence (HuR-HNS) domain. HuR, also known as embryonic lethal abnormal vision-like 1 (ELAVL1) is a well characterized RNA-binding protein that increases the stability of short lived mRNAs which encode proinflammatory mediators. HuR employs its HNS domain to interact with poly(ADP-ribose) polymerase 1 (PARP1), and intervention by TAT-HuR-HNS3 interrupts this interaction, resulting in lower poly-ADP-ribosylation and decreased cytoplasmic distribution of HuR. TAT-HuR-HNS3 also blocks HuR dimerization and promotes argonaute 2-based miRNA induced silencing complex binding. TAT-HuR-HNS3 lowers the mRNA stability of proinflammatory mediators in TNF-α treated epithelial cells and macrophages, and decreases TNF-α induced inflammatory responses in animal lung models.

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

• Wang et al (2022) Cell-Penetrating Peptide TAT-HuR-HNS3 Suppresses Proinflammatory Gene Expression via Competitively Blocking Interaction of HuR with Its Partners. J Immunol. 208(10) 2376 PMID: 35444028

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.