bs-70348R

DATASHEET

Host: Rabbit

Target Protein: Arpc1b/p41-Arc (Thr-21)

Specificity: The antibody detects a 41 kDa* protein corresponding to the molecular mass of Arpc1b on SDS-PAGE immunoblots of human A431 and mouse C2C12 treated with calyculin A. This reactivity is removed with lambda phosphatase treatment. This peptide sequence is highly conserved in rat, mouse, chicken, and fish Arpc1b, and has some homology to the conserved site in isoform Arpc1a.

Modification Site: Thr-21

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: O15143

Source: Phospho-Arpc1b/p41-Arc (Thr-21) synthetic peptide (coupled to KLH) corresponding to amino acid residues surrounding threonine 21 in human Arpc1b.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

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. p41-Arc (Arpc1b) subunit Arpc1 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