TAT-ANK peptide (TFA removed)

TAT-ANK peptide (TFA removed)

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

Batch to batch variation of the purity

H-YGRKKRRQRRRQTLQAELLVVYGA-OH

H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gln-Thr-Leu-Gln-Ala-Glu-Leu-Leu-Val-Val-Tyr-Gly-Ala-OH

24

97.74%

C₁₂₈H₂₂₁N₄₇O₃₃

2946.41

Synthetic

Powder

TAT-ANK is a peptide derived from amino acid residues 179–191 (QTLQAELLVVYGA) of the G-protein coupled receptor kinase interacting protein-1 (GIT1) ankyrin domain, which are are crucial for GIT1 binding to the Notch transcription repressor RBP-J. In vitro, application of TAT-ANK significantly inhibits Delta-like 4 (Dll4) expression and Notch 1 activation in human umbilical vein endothelial cells (HUVECs) by competing with activated Notch1 binding to RBP-J, and in mouse models, TAT-ANK reduces tumour size through impairing tumour angiogenesis.Since the TAT sequence is YGRKKRRQRRR, the full peptide sequence is YGRKKRRQRRR-QTLQAELLVVYGA.

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

• Zhu et al (2022) A novel peptide inhibitor of Dll4-Notch1 signalling and its pro-angiogenic functions. Br J Pharmacol. 1-16 PMID: 34796471

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.