Caveolin-1 (82-101) amide (human, mouse, rat), also known as Caveolin-1 scaffolding domain peptide, mitigates aging-related detrimental alterations in various organs and inhibits tyrosine kinases [1].

WL47 is a high-affinity ligand for caveolin-1 (CAV1) with a dissociation constant (Kd) of 23 nM, demonstrating potent disruption of CAV1 oligomers. This compound exhibits selectivity for CAV1, with minimal interaction towards BSA, casein, and HEWL. Notably, WL47's molecular structure is 80% smaller than its T20 parent sequence, rendering it a useful tool for investigating caveolin-1 function [1].

High affinity caveolin-1 (CAV1) ligand (Kd = 23 nM); disrupts caveolin-1 oligomers. Exhibits selectivity for CAV1 over BSA, casein and HEWL.

WL47 TFA, a high-affinity cavolin-1 (CAV1) ligand (Kd=23 nM), potently disrupts CAV1 oligomers and exhibits selectivity over BSA, casein, and HEWL. At 80% shorter than the original T20 parent sequence, WL47 TFA is used to investigate caveolin-1 function [1].