Recombinant Mouse Alpha-ketoglutarate-dependent dioxygenase FTO (Fto)

Code CSB-YP806828MO
MSDS
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Source Yeast
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Code CSB-EP806828MO
MSDS
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Source E.coli
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Code CSB-EP806828MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP806828MO
MSDS
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Source Baculovirus
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Code CSB-MP806828MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Fto
Uniprot No.
Alternative Names
Fto; Kiaa1752Alpha-ketoglutarate-dependent dioxygenase FTO; Fat mass and obesity-associated protein; Protein fatso; U6 small nuclear RNA; 2'-O-methyladenosine-N(6)-)-demethylase FTO; EC 1.14.11.-; U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO; EC 1.14.11.-; mRNA; 2'-O-methyladenosine-N(6)-)-demethylase FTO; m6A(m)-demethylase FTO; EC 1.14.11.-; mRNA N(6)-methyladenosine demethylase FTO; EC 1.14.11.53; tRNA N1-methyl adenine demethylase FTO; EC 1.14.11.-
Species
Mus musculus (Mouse)
Expression Region
1-502
Target Protein Sequence
MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD VSLKSFDPAV LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL EGLWKKMESM TNAVLREVKR EGLPVEQRSE ILSAILVPLT VRQNLRKEWH ARCQSRVVRT LPVQQKPDCR PYWEKDDPSM PLPFDLTDVV SELRGQLLEA RS
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. M6A demethylation by FTO affects mRNA expression and stability. Also able to demethylate m6A in U6 small nuclear RNA (snRNA). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA. Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping. Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs. Has no activity towards 1-methylguanine. Has no detectable activity towards double-stranded DNA. Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine. Ability to repair alkylated DNA and RNA is however unsure in vivo. Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation. Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells. Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs.
Gene References into Functions
  1. In C57bl/6 model, glycaemic index of maternal dietary carbohydrates differentially alters Fto and Lep expression in offspring. PMID: 30241328
  2. Mutations in genes implicated in body mass and timing of puberty in the general population may contribute to the pathogenesis of self-limited delayed puberty. Fto+/- mice displayed a significantly delayed timing of pubertal onset as well. PMID: 29161441
  3. FTO demethylase activity is essential for normal bone development and mineralization, a previously unreported FTO function. PMID: 29203346
  4. FTO is critically involved in insulin defects-related Alzheimer's disease. PMID: 29501742
  5. This is the first study revealing the presence of a parallel increase in expressions of FTO and HNRNPK proteins. This increase may codictate the metabolic changes occurring in the cell and may attribute a significance to HNRNPK in FTO-associated transformations. PMID: 28555196
  6. Contextual fear conditioning decreased FTO levels in neurons from the hippocampus. PMID: 28205605
  7. The involvement of mTOR-PGC-1alpha pathway in the connection between FTO and muscle differentiation is displayed. PMID: 28333151
  8. In vivo experiments revealed that Fto(-/-) and Fto(+/-) mice were more susceptible to thiopurine-induced myelosuppression than wild-type mice. PMID: 27558924
  9. propose that PKCbeta acts to suppress the degradation of FTO protein and reveals the associated role of PKCbeta and FTO in adipogenesis, suggesting a new pathway that affects the development of obesity and metabolic diseases PMID: 28626026
  10. the results of this study indicate that the effects of FTO-associated SNPs on energy homeostasis are due in part to the effects of these genetic variations on hypothalamic FTO, RPGRIP1L, and possibly other genes. PMID: 27064284
  11. FTO may have a deleterious role in hepatic cells during lipotoxic conditions, and up-regulation of FTO may contribute to the increased liver damage in non-alcoholic steatohepatitis PMID: 27651333
  12. Fto deficiency affects the gene and miR130/miR378 expression involved in brown adipogenesis and browning of white adipose tissue in mice. PMID: 27827997
  13. Here we show that FTO expression is increased after ureteral obstruction and renal fibrosis. PMID: 26727661
  14. Taken together, the results suggest that Fto regulates the proliferation and differentiation of 3T3-L1 cells via multiple mechanisms, including PPARgamma and PI3K/Akt signaling. PMID: 26907332
  15. These results reveal that FTO regulates fatty acid mobilization in adipocytes and thus body weight in part through posttranscriptional regulation of Angptl4. PMID: 26671148
  16. FTO-dependent N6-methyladenosine demethylation may be affected by betaine. PMID: 26078098
  17. FTO modulates circadian rhythms and inhibits the CLOCK-BMAL1-induced transcription. PMID: 26188089
  18. FTO expression and N6-methyladenosine levels are inversely correlated during adipogenesis. FTO depletion blocks differentiation and only catalytically active FTO restores adipogenesis. PMID: 25412662
  19. FTO is present in both the nucleus and cytoplasm, with a mobile fraction that shuttles between both cellular compartments, possibly by interaction with XPO2. PMID: 25242086
  20. FTO plays an important role in the development of metabolic disorders and is an interesting target for therapeutic agents. PMID: 25144618
  21. data suggest that IRX3 is a functional long-range target of obesity-associated variants within FTO and represents a novel determinant of body mass and composition PMID: 24646999
  22. FTO silencing did not modify PPARgamma2 mRNA levels. Partial reduction of FTO did not influence the first step of 3T3-L1 adipocyte differentiation. PMID: 23913730
  23. Downregulation was seen only with essential amino-acid deficiency and not with non-essential amino acids. These data suggest that FTO might have a role in the sensing of essential amino-acid availability. PMID: 22614055
  24. Data suggest that Fto-deficient white adipocytes exhibit some metabolic functions similar to brown adipocytes; expression of Ucp1 (uncoupling protein-1) is up-regulated and mitochondrial uncoupling is increased in Fto-deficient adipocytes. PMID: 23751871
  25. Inactivation of the Fto gene impairs dopamine receptor types 2 & 3 control of neuronal activity & behavioral responses. FTO regulates the demethylation of specific mRNAs in vivo, and this activity relates to the control of DA transmission. PMID: 23817550
  26. altered levels of FTO have multiple and diverse consequences on RNA modifications and the transcriptome PMID: 22872099
  27. Our data suggest that Fto may have a critical role in the control of lean mass, independent of its effect on food intake. PMID: 23300482
  28. These results provide important evidence that FTO-variant linked obesity may be associated with altered metabolic functions through activation of downstream metabolic mediators. PMID: 22675562
  29. FTO plays a wide functional role in extracellular ligand-induced neuronal plasticity via NTRK2/BDNF. PMID: 22087873
  30. The widespread expression of FTO in neurones also suggests that physiological studies of this protein should not be limited to the hypothalamus. PMID: 22140494
  31. Fto, a proposed transcription co-factor, influences expression of the gene encoding a satiety mediator, oxytocin. PMID: 21514276
  32. Results demonstrate that Fto plays an essential role in postnatal growth. PMID: 21103374
  33. This study provides the first direct evidence that increased Fto expression causes obesity in mice. PMID: 21076408
  34. The coactivator role of FTO in modulating the transcriptional regulation of adipogenesis by C/EBPs is consistent with the temporal progressive loss of adipose tissue in the Fto-deficient mice. PMID: 20858458
  35. Hepatic Fto may participate in the feedback regulation of glucose metabolism via gluconeogenesis. PMID: 20816934
  36. bioinformatics analysis shows FTO shares sequence motifs with Fe(II)- & 2-oxoglutarate-dependent oxygenases; recombinant Fto catalyzes the Fe(II)- & 2OG-dependent demethylation of 3-methylthymine in single-stranded DNA; Fto mRNA is most abundant in brain PMID: 17991826
  37. Examined Fto/Ftm expression in obese mice exposed to overfeeding,underfeeding and cold. PMID: 18256137
  38. Data show that the expression of FTO gene was reduced in adipocytes from db/db mice. PMID: 18647953
  39. FTO can catalyze the demethylation of 3-meU in ssRNA with a slightly higher efficiency over that of 3-meT in ssDNA, suggesting that methylated RNAs are the preferred substrates for FTO. PMID: 18775698
  40. first direct demonstration that Fto is functionally involved in energy homeostasis by the control of energy expenditure PMID: 19234441
  41. A dominant missense mutation (I367F) in the mouse Fto gene results in a lean phenotype of reduced body weight and fat mass. PMID: 19680540
  42. FTO mRNA is present mainly in sites related to hunger/satiation control; changes in hypothalamic FTO expression are associated with cues related to energy intake rather than feeding reward. Also, neurons involved in feeding termination express FTO. PMID: 19860904

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Subcellular Location
Nucleus. Nucleus speckle. Cytoplasm.
Protein Families
Fto family
Tissue Specificity
Ubiquitous. Detected in brain, brain cortex, hypothalamus, cerebellum, liver, pancreas, heart, kidney, white adipose tissue and skeletal muscle. Most abundant in the brain, particularly in hypothalamic nuclei governing energy balance.
Database Links
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