Accelerate your actin research with Arp2/3—a critical actin nucleator for lamellipodia, motility, immune trafficking & development. Cited in 100+ studies—trusted and proven.

• Biochemical analysis of Arp2/3 function
• Study in vitro regulation of actin dynamics

The Arp2/3 complex (Actin-Related Proteins) is a highly conserved seven-subunit protein assembly that initiates the growth of branched actin filaments, playing a critical role in cell motility, endocytosis, and intracellular trafficking. Activated by nucleation-promoting factors, it binds to existing actin filaments and nucleates new branches, driving dynamic rearrangements of the actin cytoskeleton.

The Arp2/3 complex has been purified from porcine brain.

• Complex: consists of seven evolutionarily conserved protein subunits, all present in approximately equal stoichiometry
• Molecular weight: complex is ~224 kDa
• Composition: when resuspended to 5 mg/ml, the buffer composition is 20 mM Tris pH 7.5, 25 mM KCl, 1 mM MgCl2, 0.5 mM EDTA, 0.1 mM ATP, 1.0% (v/v) dextran, and 5% (v/v) sucrose
• Supplied as a white lyophilized powder

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 RP01P is determined by its ability to induce the branched polymerization of actin filaments in vitro at a molar ratio of 1:200 (Arp2/3:actin) in the presence of the VCA domain of N-WASP. Under the experimental conditions (see datasheet for details), the 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.