Catalog # AX3875
phospho-Arp2 (Thr-237/Thr-238) Peptide
Blocking Peptide
| Blocking | 1:1000 |
| ELISA | 50 ng/well |
Size 50 μg
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. Arp2 has two phosphosites, Thr-237 and Thr-238, that are evolutionarily conserved, and are phosphorylated along with Tyr-202 in response to growth factor stimulation. These phosphorylation events may regulate binding to the pointed end of actin filaments, and alanine substitutions of these Arp2 phosphosites inhibits membrane protrusions. Thus, phosphorylation may be another mode of Arp2/3 complex regulation in addition to the activity of nucleation-promoting factors.
References
Soderling, S.H. (2009). Sci Signal. 2(55):pe5 (Review).
LeClaire, L.L. et al (2008). J Cell Biol. 182(4):647.
Kelleher, J.F. et al. (1995). J Cell Biol. 131(2):385.
*For more information, see UniProt Accession P61160
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:
