Analytical Data
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Gene name
N6AMT2
- Application
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Alternative Names
N(6)-adenine-specific DNA methyltransferase 2
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WVE0
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Expression Region
2-214aa
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Molecular Weight
40.4 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
N6AMT2, a methyltransferase enzyme, has emerged as a significant focus of research due to its role in the methylation of adenine residues in RNA, influencing various biological processes, including gene expression and RNA stability. Recent studies indicate that this enzyme is essential for the regulation of gene expression in mammalian cells, potentially impacting developmental processes and responses to environmental stimuli. The discovery of its involvement in post-transcriptional modifications has prompted investigations into its potential connections with diseases, particularly cancer, where dysregulation of RNA methylation patterns can result in aberrant gene expression profiles. Understanding the structure and function of N6AMT2 is crucial for elucidating its biological roles and therapeutic potential. Research efforts are increasingly geared towards characterizing its enzymatic activity, identifying its substrate specificity, and exploring its interactions with other cellular components. As a result, N6AMT2 is not only a crucial player in fundamental RNA biology but also a promising target for novel therapeutic strategies aimed at manipulating RNA methylation for disease intervention.
