ERG inhibitory peptide 2(EIP2)

ERG inhibitory peptide 2(EIP2)

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

Batch to batch variation of the purity

H-LSFGSLP-NH2

H-Leu-Ser-Phe-Gly-Ser-Leu-Pro-NH2

7

97.2%

C₃₄H₅₄N₈O₉

718.8

Synthetic

Powder

ERG inhibitory peptide 2, also known as EIP2 peptide was first reported in 'Development of Peptidomimetic Inhibitors of the ERG Gene Fusion Product in Prostate Cancer, Cancer Cell (2017)' by Wang et al. EIP2 peptide comprising the amino acid sequence: LSFGSLP. The EIP2 (LSFGSLP) was found to be homologous to the SR domain of DLC1 protein, which is encoded by a tumor suppressor gene often deleted in liver, prostate, lung, colorectal, and breast cancers. EIP1 & EIP2 peptide could bind ERG with high affinity and specificity, leading to proteolytic degradation of the ERG protein. The EIPs attenuated ERG-mediated transcription, chromatin recruitment, protein-protein interactions, cell invasion and proliferation, and tumor growth.

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., Development of Peptidomimetic Inhibitors of the ERG Gene Fusion Product in Prostate Cancer, Cancer Cell (2017), http://dx.doi.org/10.1016/j.ccell.2017.02.017

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.