bsm-70499M

DATASHEET

Host: Mouse

Target Protein: FHOD1

Specificity: The antibody detects a 140 kDa* protein corresponding to the apparent molecular mass of FHOD1 on SDS-PAGE immunoblots of human K562 and Jurkat, and has weak reactivity to FHOD1 in mouse C2C12.

Clonality: Monoclonal

Isotype: IgG1

Swiss Prot: Q9Y613

Source: FHOD1 recombinant protein that included the full length human FHOD1 sequence. This sequence has 50% homology to human FHOD3, and low homology to other formin family members.

Purification: Purified by Protein A.

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:

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.