Analytical Data
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Gene name
Eef2kmt
- Application
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Alternative Names
Eef2kmt；FAM86A；Protein-lysine N-methyltransferase EEF2KMT
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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
Q96G04
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Expression Region
1-330aa
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AA Sequence
MAPEENAGTELLLQSFERRFLAARTLRSFPWQSLEAKLRDSSDSELLRDILHKTVKHPVCVKHPPSVKYARCFLSELIKKHEAVHTEPLDELYEALAETLMAKESTQGHRSYLLPSGGSVTLSESTAIISYGTTGLVTWDAALYLAEWAIENPAVFTNRTVLELGSGAGLTGLAICKMCRPRAYIFSDCHSRVLEQLRGNVLLNGLSLEADITAKLDSPRVTVAQLDWDVATVHQLSAFQPDVVIAADVLYCPEAIMSLVGVLRRLAACREHQRAPEVYVAFTVRNPETCQLFTTELGRAGIRWEVEPRHEQKLFPYEEHLEMAMLNLTL
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Molecular Weight
41.0 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
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Protein Description
Eef2kmt, or eukaryotic elongation factor 2 lysine methyltransferase, plays a crucial role in the regulation of protein synthesis by methylating elongation factor 2 (EF2), which is essential for the translation process in eukaryotic cells. Recent studies have indicated that Eef2kmt is implicated in various cellular functions, including cell growth, differentiation, and response to stress, suggesting its significance in maintaining cellular homeostasis. Dysregulation of Eef2kmt has been linked to several pathological conditions, including cancer, where altered protein synthesis can contribute to tumor progression and resistance to therapy. Understanding the structure-function relationship of Eef2kmt through the development of recombinant protein enables researchers to explore its enzymatic activity, identify potential substrates, and elucidate its role in translational control. Furthermore, the investigation of Eef2kmt's potential as a therapeutic target is of great interest, as modulating its activity could offer novel strategies for cancer treatment or other diseases characterized by aberrant protein synthesis. Thus, research on Eef2kmt and its recombinant form is essential for uncovering insights into fundamental biological processes and developing innovative therapeutic approaches.
