Caveolin-1 scaffolding domain peptide

Caveolin-1 scaffolding domain peptide

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

Batch to batch variation of the purity

H-DGIWKASFTTFTVTKYWFYR-NH2

H-Asp-Gly-Ile-Trp-Lys-Ala-Ser-Phe-Thr-Thr-Phe-Thr-Val-Thr-Lys-Tyr-Trp-Phe-Tyr-Arg-NH2

20

95.27%

C₁₂₄H₁₇₀N₂₈O₂₉

2516.84

Synthetic

Powder

Caveolin-1 scaffolding domain peptide is amino acids 82–101 of caveolin-1, a structural cytoplasmic membrane protein involved in the formation and function of caveolae. Caveolin-1 scaffolding domain peptide can reverse aging associated fibrosis, microvascular leakage, and organ dysfunction in the heart, kidneys, and brain of mice through a mechanism that involves the suppression of the activity of multiple tyrosine kinases, reducing age related microvascular leakage and interstitial fibrosis to the levels of healthy, young mice.

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

• Kuppuswamy et al (2021) The Caveolin-1 Scaffolding Domain Peptide Reverses Aging-Associated Deleterious Changes in Multiple Organs. J Pharmacol Exp Ther. 378(1) 1 PMID: 33879542

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.