Anti-FHOD1 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | Q9Y613 |
Host | Mouse |
Clonality | Mouse Monoclonal |
Isotype | IgG1 |
Clone Names | M352 |
Calculated MW | 126551 Da |
Gene ID | 29109 |
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Other Names | FHOS, formin |
Target/Specificity | 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. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Anti-FHOD1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |
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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.
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