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) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.