Analytical Data
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Gene name
Eef1akmt2
- Application
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Alternative Names
Eef1akmt2；C10orf138；METTL10；EEF1A lysine methyltransferase 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5JPI9
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Expression Region
1-236aa
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AA Sequence
MSSGADGGGGAAVAARSDKGSPGEDGFVPSALGTREHWDAVYERELQTFREYGDTGEIWFGEESMNRLIRWMQKHKIPLDASVLDIGTGNGVFLVELAKFGFSNITGIDYSPSAIQLSGSIIEKEGLSNIKLKVEDFLNLSTQLSGFHICIDKGTFDAISLNPDNAIEKRKQYVKSLSRVLKVKGFFLITSCNWTKEELLNEFSEGFELLEELPTPKFSFGGRSGNSVAALVFQKM
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Molecular Weight
25.9 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
Eef1akmt2, also known as elongation factor 1 alpha 2 lysine methyltransferase 2, is an enzyme that plays a significant role in the regulation of protein synthesis through the methylation of elongation factor 1 alpha (Eef1a), a crucial component of the translation machinery. The dysregulation of Eef1akmt2 has been implicated in various pathological conditions, including cancer, where altered protein synthesis can contribute to tumorigenesis. Researchers have increasingly focused on Eef1akmt2 due to its potential as a therapeutic target; understanding its biochemical properties and interaction with other cellular components could pave the way for novel cancer treatments. The study of Eef1akmt2 encompasses its structural biology, enzymatic activity, and regulation, as well as the broader implications of its function in cellular metabolism and stress responses. Additionally, the expression patterns of Eef1akmt2 in different tissues and developmental stages reveal its importance in cellular function and differentiation. Given the rising interest in epigenetic modifications and their influence on gene expression, investigating the role of Eef1akmt2 in methylation dynamics offers valuable insights into the interconnected networks governing cellular processes, making it a compelling subject for ongoing research in molecular biology and oncology.
