FHAD1
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Official Full Name
forkhead-associated (FHA) phosphopeptide binding domain 1 -
Synonyms
B230311F11;2900090M10Rik
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| FHAD1-3800Z | Recombinant Zebrafish FHAD1 | Mammalian Cell | Zebrafish | His |
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| FHAD1-5872M | Recombinant Mouse FHAD1 Protein | Mammalian Cell | Mouse | His |
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| FHAD1-3248M | Recombinant Mouse FHAD1 Protein, His (Fc)-Avi-tagged | HEK293 | Mouse | His&Fc&Avi |
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| FHAD1-3248M-B | Recombinant Mouse FHAD1 Protein Pre-coupled Magnetic Beads | HEK293 | Mouse |
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Involved Pathway
FHAD1 involved in several pathways and played different roles in them. We selected most pathways FHAD1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with FHAD1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
FHAD1 has several biochemical functions, for example, molecular_function. Some of the functions are cooperated with other proteins, some of the functions could acted by FHAD1 itself. We selected most functions FHAD1 had, and list some proteins which have the same functions with FHAD1. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| molecular_function | TNKS1BP1,FANCE,RNFT1,ZC3H3,GM3750,D6WSU163E,ASF1BB,MUP11,CCDC63,PTTG1IP |
Interacting Protein
FHAD1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with FHAD1 here. Most of them are supplied by our site. Hope this information will be useful for your research of FHAD1.
Ywhae
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References
- Xu, QP; Deller, MC; et al. Structural Insights into the Recognition of Phosphopeptide by the FHA Domain of Kanadaptin. PLOS ONE 9:-(2014).
- Pershad, K; Wypisniak, K; et al. Directed Evolution of the Forkhead-Associated Domain to Generate Anti-Phosphospecific Reagents by Phage Display. JOURNAL OF MOLECULAR BIOLOGY 424:88-103(2012).
