FTO Antibody - #DF8421

Product: | FTO Antibody |
Catalog: | DF8421 |
Description: | Rabbit polyclonal antibody to FTO |
Application: | WB IHC |
Reactivity: | Human |
Prediction: | Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog |
Mol.Wt.: | 58 kDa; 58kD(Calculated). |
Uniprot: | Q9C0B1 |
RRID: | AB_2841669 |
Related Downloads
Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF8421, RRID:AB_2841669.
Fold/Unfold
AlkB homolog 9; ALKBH9; Alpha-ketoglutarate-dependent dioxygenase FTO; AW743446; Fat mass and obesity-associated protein; FATSO, MOUSE, HOMOLOG OF; Fto; FTO_HUMAN; GDFD; KIAA1752; mKIAA1752; Protein fatso;
Immunogens
Ubiquitously expressed, with relatively high expression in adrenal glands and brain; especially in hypothalamus and pituitary (PubMed:17434869, PubMed:17496892). Highly expressed in highly expressed in acute myeloid leukemias (AML) with t(11;11)(q23;23) with KMT2A/MLL1 rearrangements, t(15;17)(q21;q21)/PML-RARA, FLT3-ITD, and/or NPM1 mutations (PubMed:28017614).
- Q9C0B1 FTO_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCDDVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLPVEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP
Predictions
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - Q9C0B1 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
T4 | Phosphorylation | Uniprot | |
T6 | Phosphorylation | Uniprot | |
T32 | Phosphorylation | Uniprot | |
K45 | Ubiquitination | Uniprot | |
K48 | Ubiquitination | Uniprot | |
S55 | Phosphorylation | Uniprot | |
K88 | Ubiquitination | Uniprot | |
C104 | S-Nitrosylation | Uniprot | |
Y106 | Phosphorylation | Uniprot | |
K107 | Ubiquitination | Uniprot | |
Y108 | Phosphorylation | Uniprot | |
K121 | Ubiquitination | Uniprot | |
T150 | Phosphorylation | Uniprot | |
K160 | Ubiquitination | Uniprot | |
K162 | Ubiquitination | Uniprot | |
S173 | Phosphorylation | Uniprot | |
S184 | Phosphorylation | Uniprot | |
Y185 | Phosphorylation | Uniprot | |
K194 | Ubiquitination | Uniprot | |
Y199 | Phosphorylation | Uniprot | |
K211 | Ubiquitination | Uniprot | |
K216 | Acetylation | Uniprot | |
K216 | Sumoylation | Uniprot | |
K216 | Ubiquitination | Uniprot | |
Y220 | Phosphorylation | Uniprot | |
S229 | Phosphorylation | Uniprot | |
S256 | Phosphorylation | Uniprot | |
S260 | Phosphorylation | Uniprot | |
S355 | Phosphorylation | Uniprot | |
S458 | Phosphorylation | Uniprot |
Research Backgrounds
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 (By similarity). Plays an oncogenic role in a number of acute myeloid leukemias by enhancing leukemic oncogene-mediated cell transformation: acts by mediating m6A demethylation of target transcripts such as MYC, CEBPA, ASB2 and RARA, leading to promote their expression.
Nucleus. Nucleus speckle. Cytoplasm.
Note: Localizes mainly in the nucleus, where it is able to demethylate N(6)-methyladenosine (m6A) and N(6),2'-O-dimethyladenosine cap (m6A(m)) in U6 small nuclear RNA (snRNA), N(1)-methyladenine from tRNAs and internal m6A in mRNAs (PubMed:30197295). In the cytoplasm, mediates demethylation of m6A and m6A(m) in mRNAs and N(1)-methyladenine from tRNAs (PubMed:30197295).
Ubiquitously expressed, with relatively high expression in adrenal glands and brain; especially in hypothalamus and pituitary. Highly expressed in highly expressed in acute myeloid leukemias (AML) with t(11;11)(q23;23) with KMT2A/MLL1 rearrangements, t(15;17)(q21;q21)/PML-RARA, FLT3-ITD, and/or NPM1 mutations.
Monomer (By similarity). May also exist as homodimer (By similarity).
The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases.
Belongs to the fto family.
References
Application: IHC Species: Human Sample:
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