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FoxO4 (Acetyl Lys407) rabbit pAb

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.

Product Specifications

Background

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.

UniProt

P98177

Swiss Prot

P98177

Reactivity

Human; Mouse

Immunogen

Synthesized peptide derived from human FoxO4 (Acetyl Lys407)

Clonality

Polyclonal

Source

Rabbit

Applications

WB; ELISA

Concentration

1 mg/ml

Dilution

WB 1:1000-2000 ELISA 1:5000-20000

Molecular Weight

55kD

Storage Conditions

-20°C/1 year

Observed Molecular Weight

55kD

Fragment

IgG

Subcellular Location

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

Other Product Names

Forkhead box protein O4 (Fork head domain transcription factor AFX1)

Gene ID (Human)

4303

Available Sizes

Curated Selection

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