The antiserum was produced against synthesized peptide derived from human FOXO4 around the phosphorylation site of Thr451. AA range:417-466

Phospho-FoxO4 (T451) Polyclonal Antibody detects endogenous levels of FoxO4 protein only when phosphorylated at T451.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):LGtPV

FOXO4 AFX AFX1 MLLT7

Forkhead box protein O4

FOXO4 ;
AFX ;
AFX1 ;
MLLT7 ;
Forkhead box protein O4 ;
Fork head domain transcription factor AFX1

This gene encodes a member of the O class of winged helix/forkhead transcription factor family. Proteins encoded by this class are regulated by factors involved in growth and differentiation indicating they play a role in these processes. A translocation involving this gene on chromosome X and the homolog of the Drosophila trithorax gene, encoding a DNA binding protein, located on chromosome 11 is associated with leukemia. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2010],

Disease:A chromosomal aberration involving FOXO4 is found in acute leukemias. Translocation t(X;11)(q13;q23) with MLL/HRX. The result is a rogue activator protein.,Function:Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle.,pharmaceutical:A constitutively active FOXO4 mutant where phosphorylation sites Thr-32, Ser-187 and Ser-262 have been mutated to alanine may have therapeutic potential in ERBB2/HER2-overexpressing cancers as it inhibits ERBB2-mediated cell survival, transformation and tumorigenicity.,PTM:Acetylation by CBP, which is induced by peroxidase stress, inhibits transcriptional activity. Deacetylation by SIRT1 is NAD-dependent and stimulates transcriptional activity.,PTM:Phosphorylation by PKB/AKT1 inhibits transcriptional activity and is responsible for cytoplasmic localization.,similarity:Contains 1 fork-head DNA-binding domain.,subcellular location:When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation.,subunit:Interacts with CBP, MYOCD, SIRT1, SRF and YWHAZ. Acetylated by CBP and deacetylated by SIRT1. Binding of YWHAZ inhibits DNA-binding.,tissue specificity:Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform zeta is most abundant in the liver, kidney, and pancreas.,

Cytoplasm. Nucleus. When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm.

>>Ras signaling pathway ;
>>FoxO signaling pathway ;
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