| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Alpha-ketoglutarate-dependent dioxygenase FTO|Fat mass and obesity-associated protein|U6 small nuclear RNA|2'-O-methyladenosine-N(6)-)-demethylase FTO|U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO|mRNA|2'-O-methyladenosine-N(6)-)-demethylase FTO|m6A(m)-demethylase FTO|mRNA N(6)-methyladenosine demethylase FTO|tRNA N1-methyl adenine demethylase FTO|FTO|KIAA1752 |
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| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
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Background
human FTO (Alpha-ketoglutaRate-dependent dioxygenase FTO) is a molecular target commonly studied in biomedical research. Many proteins are studied as molecular readouts that can change with cellular state, tissue remodeling, or stress responses.
Biological role and mechanism
The biological role of FTO is typically understood in terms of its molecular category and interaction network. Depending on the model system, it may participate in cell–cell communication, intracellular signaling, enzymatic processing, or regulation of gene expression programs. Mechanistic interpretation is often strengthened by considering upstream regulators and downstream readouts rather than relying on a single marker.
Expression and abundance of FTO can vary by tissue, cell type, and physiological state. In many systems, levels are influenced by factors such as developmental stage, immune activation, metabolic status, and cellular stress. Because sample matrix and pre-analytical handling can affect measured concentrations, interpretation is typically strongest when experiments keep collection and processing consistent across groups.
Nomenclature and related terms
FTO (Alpha-ketoglutaRate-dependent dioxygenase FTO) may also be referenced as Alpha-ketoglutarate-dependent dioxygenase FTO, Fat mass and obesity-associated protein, and U6 small nuclear RNA in the literature or in databases. When comparing results across studies, confirm that the reported analyte refers to the same molecule, species context, and molecular form (e.g., precursor vs mature protein, or soluble vs membrane-associated forms).
Why it matters in research
- Understanding how FTO relates to signal transduction, tissue homeostasis, stress responses, and disease-model biology in biomedical research.
- Interpreting shifts in FTO levels alongside other pathway components or complementary markers.
- Connecting molecular changes to phenotypes such as inflammation, remodeling, metabolism shifts, or cell-state transitions (context-dependent).
Molecular forms and interpretation
For some targets, isoforms, proteolytic processing, or post-translational modifications (such as phosphorylation or glycosylation) can influence function and apparent abundance. If multiple molecular forms are expected in your model, align interpretation with the form most relevant to the biological question.
Disease and translational relevance
FTO has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with biomedical studies. These associations are interpreted as research findings rather than diagnostic or therapeutic claims, and they should be evaluated alongside model-specific covariates and study design.
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Association of adiponectin and fat mass and obesity genetic variants with breast cancer risk in Egyptian females
IF: 2.4 Journal: Gene Author: Medical Biochemistry & Molecular Biology, Faculty of Medicine, Menoufia University, Egypt. Cited Date: 2025-10-24
Association of FTO protein with hyperandrogenism metabolic disturbances in women with polycystic ovary syndrome
IF: Journal: Endocrine Regulations Author: Department of Biochemistry, Integral Institute of Medical Sciences & Research (IIMSR), Integral University, Lucknow, Uttar Pradesh, India. Cited Date: 2025-05-02