Analytical Data
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Gene name
METTL25
- Application
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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
Q8N6Q8
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Expression Region
1-603aa
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Molecular Weight
75.7 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
METTL25, a member of the methyltransferase-like family, has garnered significant attention in recent years due to its pivotal role in regulating various cellular processes through RNA methylation. This protein is primarily known for its ability to catalyze the methylation of specific adenosine residues within RNA molecules, which can influence RNA stability, splicing, and translation efficiency. Understanding the function of METTL25 is essential, as dysregulation of RNA methylation is linked to several diseases, including cancer and neurodegenerative disorders. Recent studies suggest that METTL25 may play a crucial role in cellular stress responses and gene expression regulation. Moreover, the growing interest in RNA modifications and their implications in epitranscriptomics has propelled research into METTL25, prompting investigations into its molecular mechanisms, substrates, and interactions with other cellular factors. As such, characterizing the recombinant form of METTL25 is vital for elucidating its biological functions and therapeutic potentials, setting the stage for further studies aimed at targeting its methylation activity in disease contexts.
