Rabbit Polyclonal
ELISA | 1:2000 |
ICC | 1:200 |
IP | 1:100 |
WB | 1:1000 |
Size 100 μl
Species Reactivity Hu, Rt, Ms, Ck
MW 41 kDa
Cellular morphology, adhesion, and motility occur through dynamic reorganization of actin-based superstructures. Actin-binding proteins are critical for regulating actin polymerization and superstructure formation. The Arp2/3 complex is an actin polymerization-inducing complex that includes Arp2, Arp3, p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc. Several nucleation promoting factors, such as WASP and coronin, regulate the activity of the Arp2/3 complex. In addition, the Arp2/3 complex may be regulated by phosphorylation of specific subunits in the complex. The p41-Arc (Arpc1) subunit has two isoforms in humans, Arpc1a and Arpc1b. PAK1 can bind and phosphorylate Thr-21 in Arpc1b leading to growth factor-stimulated cell motility. In addition, Arpc1b colocalizes with γ-tubulin at centrosomes and stimulates Aurora A activity. Aurora A phosphorylates Arpc1b on Thr-21 and a nonphosphorylatable Arpc1b mutant cannot activate Aurora A kinase and centrosome amplification. Thus, Arpc1b has roles in cytoskeletal dynamics during cell motility and mitosis, and these activities are regulated by phosphorylation at Thr-21.
References
Vadlamudi, R.K. et al. (2004) EMBO Rep. 5(2):154.
Welch, M.D. et al. (1997) J Cell Biol. 138(2):375.
*For more information, see UniProt Accession O15143
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: