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Products
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- Technical support
- Resources
Caveolin-1 scaffolding domain peptide
Cat. No. PP-170
Structure:
H-Asp-Gly-Ile-Trp-Lys-Ala-Ser-Phe-Thr-Thr-Phe-Thr-Val-Thr-Lys-Tyr-Trp-Phe-Tyr-Arg-NH2
Other Names:
CSD
Activity:
The binding domain of caveolin-1
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.
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
Related areas
All peptides >
All protein-protein interaction modulators >
All kinase modulators >
All cardiovascular research categories >
Technical Data
| Structure | H-Asp-Gly-Ile-Trp-Lys-Ala-Ser-Phe-Thr-Thr-Phe-Thr-Val-Thr-Lys-Tyr-Trp-Phe-Tyr-Arg-NH2 |
| Molecular Weight | 2516.88 |
| Formula | C124H170N28O29 |
| Sequence | DGIWKASFTTFTVTKYWFYR-NH2 |
| Modifications | C terminal amide |
Solubility and Storage
| Solubility | Soluble in DMSO |
| Appearance | Freeze dried solid |
| Storage | Store dry, frozen and in the dark |
Batch Specific Data
| Purity | >95% by hplc |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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