Arp2 (C-terminal region) polyclonal, anti-human, mouse, rat, chicken, frog

Background:
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 inhibit membrane protrusions. Thus, phosphorylation may be another mode of Arp2/3 complex regulation in addition to the activity of nucleation-promoting factors.

Immunogen: Arp2 (C-terminal region) synthetic peptide (coupled to KLH) corresponding to amino acid residues in the C-terminal region of human Arp2. This peptide sequence is highly conserved in rat, mouse, chicken, and frog Arp2 proteins.

Specificity: This antibody was affinity purified using Arp2 (C-terminal region) peptide (without carrier). The antibody detects 44 and 32 kDa* proteins corresponding to the molecular mass of Arp2 on SDS-PAGE immunoblots of human A431, HUVEC, HeLa, and Jurkat cells as well as rat PC12, mouse C2C12, and rabbit fibroblasts.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100ml phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20oC. Do not aliquot. Stable for 1 year.