• Stimulate Aap2/3 complex activity
• Study in vitro regulation of actin dynamics

The WASP VCA domain is a modular protein region that regulates actin cytoskeleton remodeling by activating the Arp2/3 complex through its Verprolin, Central, and Acidic (VCA) motifs. Its precise control over actin nucleation makes it a critical driver in cell motility, endocytosis, and intracellular trafficking.

The WASP VCA domain has been produced in a bacterial expression system.

• Protein tag: N-terminal GST tag for purification
• Amino acids: aa 392-505
• Molecular weight: ~43 kDa
• Formulation: supplied as a lyophilized powder
• Composition: when resuspended to 1 mg/ml, the buffer composition is: 20 mM Tris pH 7.5, 25 mM KCl, 1 mM MgCl2, 0.5 mM EDTA, 0.2% dextran, and 2% sucrose

Protein purity is determined by scanning densitometry of Coomassie Blue-stained protein on a 4-20% polyacrylamide gel. Purity is ≥90%

The biological activity of VCG03 is determined by its ability to stimulate Arp2/3 to induce the branched polymerization of actin filaments in vitro. Under the experimental conditions (see datasheet for details), the VCG03 plus Arp2/3 complex can enhance actin polymerization 3-5 fold. Actin polymerization is assessed by kinetic fluorescence enhancement of pyrene actin at Ab: 360 nm, Em: 405 nm.