Rb4 peptide

Rb4 peptide

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

Batch to batch variation of the purity

H-MADSERLSAPGCWAACTNFSRTRK-NH2

H-Met-Ala-Asp-Ser-Glu-Arg-Leu-Ser-Ala-Pro-Gly-Cys-Trp-Ala-Ala-Cys-Thr-Asn-Phe-Ser-Arg-Thr-Arg-Lys-NH2

24

95.25%

C₁₁₀H₁₇₇N₃₇O₃₄S₃

2657.99

Synthetic

Powder

Rb4 is a peptide derived from the N-terminal of proteolipid protein 2 (PLP2), a transmembrane lipoprotein first identified in human colonic epithelial cells. Rb4 triggers necrotic cell death in murine melanoma mainly through ER stress caused by inhibition of SERCA transporter activity, which leads to alteration of actin dynamics and RIP1 inhibition. Rb4 acts directly on tumour cells to induce the expression of two damage associated molecular pattern (DAMP) molecules, HMGB1 and calreticulin, which triggers an immunoprotective response against melanoma cells. In vivo Rb4 reduces lung metastasis of tumour cells and delays subcutaneous melanoma 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

• Maia et al (2022) PLP2-derived peptide Rb4 triggers PARP-1-mediated necrotic death in murine melanoma cells. Sci Rep. 12(1) 2890 PMID: 35190586

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.