The antiserum was produced against synthesized peptide derived from human FKHR around the phosphorylation site of Ser256. AA range:223-272

Phospho-FoxO1 (S256) Polyclonal Antibody detects endogenous levels of FoxO1 protein only when phosphorylated at S256.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 When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports.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):AAsMD

FOXO1

Forkhead box protein O1

FOXO1 ;
FKHR ;
FOXO1A ;
Forkhead box protein O1 ;
Forkhead box protein O1A ;
Forkhead in rhabdomyosarcoma

This gene belongs to the forkhead family of transcription factors which are characterized by a distinct forkhead domain. The specific function of this gene has not yet been determined; however, it may play a role in myogenic growth and differentiation. Translocation of this gene with PAX3 has been associated with alveolar rhabdomyosarcoma. [provided by RefSeq, Jul 2008],

Disease:Chromosomal aberrations involving FOXO1 are a cause of rhabdomyosarcoma 2 (RMS2) [MIM:268220]; also known as alveolar rhabdomyosarcoma. Translocation (2;13)(q35;q14) with PAX3; translocation t(1;13)(p36;q14) with PAX7. The resulting protein is a transcriptional activator.,Function:Transcription factor.,PTM:Phosphorylated by AKT1; insulin-induced (By similarity). IGF1 rapidly induces phosphorylation of Ser-256, Thr-24, and Ser-319. Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24, and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CK1, leading to nuclear exclusion and loss of function. Phosphorylation of Ser-329 is independent of IGF1 and leads to reduced function. Phosphorylated upon DNA damage, probably by ATM or ATR.,similarity:Contains 1 fork-head DNA-binding domain.,subcellular location:Shuttles between cytoplasm and nucleus.,subunit:Interacts with LRPPRC.,tissue specificity:Ubiquitous.,

Cytoplasm . Nucleus . Shuttles between the cytoplasm and nucleus. Largely nuclear in unstimulated cells (PubMed:11311120, PubMed:12228231, PubMed:19221179, PubMed:21245099, PubMed:20543840, PubMed:25009184). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus (By similarity). Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-256 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteosomal pathway (PubMed:11237865, PubMed:12228231). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (PubMed:18356527). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (PubMed:19221179, PubMed:21245099). SGK1-mediated phosphorylation also results in nuclear translocation (By similarity). Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide (By similarity). Retained in the nucleus on methylation (By similarity). PPIA/CYPA stimulates its nuclear accumulation (PubMed:31063815). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (PubMed:25009184). .

Ubiquitous.

>>FoxO signaling pathway ;
>>AMPK signaling pathway ;
>>Longevity regulating pathway ;
>>Longevity regulating pathway - multiple species ;
>>Cellular senescence ;
>>Insulin signaling pathway ;
>>Thyroid hormone signaling pathway ;
>>Glucagon signaling pathway ;
>>Insulin resistance ;
>>AGE-RAGE signaling pathway in diabetic complications ;
>>Alcoholic liver disease ;
>>Shigellosis ;
>>Human papillomavirus infection ;
>>Pathways in cancer ;
>>Transcriptional misregulation in cancer ;
>>Prostate cancer