FHOD1 (Thr-1141), phospho-specific polyclonal, anti-human, mouse, rat

Background:
Formins include several families of proteins that regulate actin cytoskeletal dynamics via two conserved formin homology domains, FH1 and FH2. The FH1 region contains poly-proline stretches that promote interactions with profilin. The FH2 domain, located C-terminally to the FH1 domain, is highly conserved in formin proteins and possesses actin nucleation and polymerization activities. Through cooperation of FH1 and FH2, formins construct actin-based structures comprising linear, unbranched filaments that are used in stress fibers, actin cables, microspikes, and contractile rings. Several mammalian formins, including mDia1, FRL, and formin homology domain protein 1 (FHOD1) are inhibited through an intramolecular interaction between the C-terminal Dia autoregulatory domain (DAD) and its recognition region at the N-terminus. In FHOD1, this autoinhibitory interaction is disrupted through phosphorylation of Ser-1131, Ser-1137, and Thr-1141 by ROCK. Subsequent FHOD1 activation leads to stress fiber formation. In endothelial cells, thrombin activates this ROCK pathway, leading to FHOD1-mediated stress fiber formation.

Immunogen: Phospho-FHOD1 (Thr-1141) synthetic peptide (coupled to KLH) corresponding to amino acid residues surrounding Thr-1141 in human FHOD1. This peptide sequence is highly conserved in rat and mouse FHOD1, and is well conserved in FHOD3 (Thr-1399).

Specificity: This antibody was cross-adsorbed to unphosphorylated FHOD1 (Thr-1141) peptide before affinity purification using phospho-FHOD1 (Thr-1141) peptide (without carrier). The antibody detects a 140 kDa* protein corresponding to the apparent molecular mass of FHOD1 on SDS-PAGE immunoblots of human K562 and mouse C2C12 cells treated with calyculin A.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.