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FHOD1 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9Y613 |
|---|---|
| Clone Names | 100318089 |
| Gene ID | 29109 |
|---|---|
| Other Names | FH1/FH2 domain-containing protein 1, Formin homolog overexpressed in spleen 1, FHOS, Formin homology 2 domain-containing protein 1, FHOD1, FHOS, FHOS1 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | FHOD1 |
|---|---|
| Synonyms | FHOS, FHOS1 |
| Function | Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing. |
| Cellular Location | Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, bleb. Note=Predominantly cytoplasmic |
| Tissue Location | Ubiquitous. Highly expressed in spleen. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a protein which is a member of theformin/diaphanous family of proteins. The gene is ubiquitouslyexpressed but is found in abundance in the spleen. The encodedprotein has sequence homology to diaphanous and formin proteinswithin the Formin Homology (FH)1 and FH2 domains. It also containsa coiled-coil domain, a collagen-like domain, two nuclearlocalization signals, and several potential PKC and PKAphosphorylation sites. It is a predominantly cytoplasmic proteinand is expressed in a variety of human cell lines. [provided byRefSeq].
References
Hannemann, S., et al. J. Biol. Chem. 283(41):27891-27903(2008)Schulte, A., et al. Structure 16(9):1313-1323(2008)Takeya, R., et al. EMBO J. 27(4):618-628(2008)Schulte, A., et al. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (PT 10), 878-881 (2007) :Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)
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