Analytical Data
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Gene name
FTO
- Application
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Alternative Names
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;Short name: m6A(m)-demethylase FTO;mRNA N(6)-methyladenosine demethylase FTO;tRNA N1-methyl adenine demethylase FTO
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9C0B1
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Expression Region
1-505aa
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Molecular Weight
65.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
FTO (fat mass and obesity-associated protein) is a member of the alpha-ketoglutarate-dependent dioxygenase family and has garnered significant attention due to its involvement in regulating energy homeostasis and adiposity. Initially identified through genetic association studies linking its polymorphisms to obesity and metabolic disorders, FTO is now recognized for its role in RNA demethylation processes, particularly targeting N6-methyladenosine (m6A) modifications in mRNA. This activity is crucial for various biological functions, including gene expression regulation, cellular metabolism, and differentiation. The recombinant expression and purification of FTO protein are essential for elucidating its biochemical properties and functional mechanisms. This research involves the use of techniques such as molecular cloning and protein expression systems to produce active FTO, which can be utilized in biochemical assays and structural studies. Understanding the structure-function relationship of FTO and its interaction with substrates and cofactors will shed light on its physiological roles and potential therapeutic targets for obesity and related metabolic diseases. Moreover, these studies may provide insights into the broader implications of m6A modifications in epitranscriptomics and their influence on cellular processes in health and disease. Thus, the research surrounding FTO recombinant proteins is pivotal in the quest to decipher the molecular underpinnings of metabolism and obesity.
