ARF(1-22) peptide

ARF(1-22) peptide

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

Batch to batch variation of the purity

H-MVRRFLVTLRIRRACGPPRVRV-OH

H-Met-Val-Arg-Arg-Phe-Leu-Val-Thr-Leu-Arg-Ile-Arg-Arg-Ala-Cys-Gly-Pro-Pro-Arg-Val-Arg-Val-OH

22

95.2%

C₁₁₆H₂₀₇N₄₃O₂₄S₂

2652.28

Synthetic

Powder

The tumor suppressor p14ARF is widely deregulated in many types of cancers and is believed to function as a failsafe mechanism, inhibiting proliferation and inducing apoptosis as cellular response to a high oncogene load. A 22-amino-acid-long peptide derived from the N-terminal part of p14ARF, denoted ARF(1–22), which has been shown to mimic the function of p14ARF, has cell-penetrating properties. This peptide is internalized to the same extent as the cell-penetrating peptide (CPP) TP10 and dose-dependently decreases proliferation in MCF-7 and MDA MB 231 cells. Uptake of the ARF(1–22) peptide is associated with low membrane disturbance, measured by deoxyglucose and lactate dehydrogenase (LDH) leakage, as compared to its scrambled peptide. Also, flow cytometric analysis of annexin V/propidium iodide (PI) binding and Hoechst staining of nuclei suggest that ARF(1–22) induces apoptosis, whereas scrambled or inverted peptide sequences have no effect. The ARF(1–22) peptide mainly translocates cells through endocytosis, and is found intact inside cells for at least 3 hours.

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

• Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, et al. Characterization of a novel cytotoxic cell-penetrating peptide derived from p14ARF protein. <em>Mol Ther</em>. 2008;16(1):115-23

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.