DATASHEET
Host:
Rabbit
Target Protein:
WAVE1 (Tyr-125)
Specificity:
This antibody was cross-adsorbed to phospho-WAVE (Tyr-150) and unphosphorylated WAVE (Tyr-125) peptides before affinity purification using phospho-WAVE (Tyr-125) peptide.
Modification Site:
Tyr-125
Clonality:
Polyclonal
Isotype:
IgG
Swiss Prot:
Q92558
Source:
Phospho-WAVE (Tyr-125) peptide (coupled to KLH) corresponding to amino acid residues surrounding Tyr-125 in human WAVE1.
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:
The Wiskott–Aldrich syndrome protein (WASP) family is involved in various pathways that regulate actin cytoskeletal organization. This family includes WASP, N-WASP, and three WAVE/SCAR isoforms, WAVE1, 2, and 3. WAVE proteins play key roles in actin-mediated cell events, such as membrane ruffling and lamellipodia formation. WAVEs contain an N-terminal WAVE homology domain, a basic domain, a Proline-rich region, and carboxy terminal verprolin, cofilin, and acidic (VCA) region. WAVEs are thought to act downstream of the Rac GTPase, connecting Rac activation to induction of Arp 2/3-mediated actin polymerization. Regulation of WAVE activity can occur through tyrosine phosphorylation. Src phosphorylation of WAVE1 at Tyr-125 enhances binding to the Arp2/3 complex, and is required for WAVE inhibition of Arp2/3-mediated stress fiber formation. By contrast, WAVE2 phosphorylation of Tyr-150 by Abl may enhance Arp2/3 complex actin nucleation and microspike formation in fibroblasts. Thus, site-specific tyrosine phosphorylation may be important for controlling specific activities of WAVE proteins.