Analytical Data
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Gene name
EEF1E1
- Application
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Alternative Names
EEF1E1；MARS;Methionine--tRNA ligase. cytoplasmic
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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
O43324
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Expression Region
1-174aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAAAAELSLLEKSLGLSKGNKYSAQGERQI PVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVT QVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIVD LTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH
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Molecular Weight
22 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
EEF1E1, or Elongation Factor Tu EEF1E1, is a protein that plays a crucial role in the process of protein synthesis by facilitating the translation of mRNA into peptides in the ribosome. Its involvement in the elongation phase of translation makes it essential for cellular function and growth. Recent studies have highlighted EEF1E1's dual role as not only a translation factor but also as a potential regulator in various cellular processes, including apoptosis and cell proliferation.
Research has indicated that dysregulation of EEF1E1 can be implicated in several diseases, including various forms of cancer, where its overexpression is often observed, suggesting a link to tumorigenesis and cancer progression. Additionally, EEF1E1 has been associated with stress responses in cells, indicating its involvement in cellular adaptation mechanisms under adverse conditions. The recombinant expression of EEF1E1 enables the study of its functional properties in vitro, which can provide insights into its mechanistic role at the cellular level and contribute to the development of therapeutic strategies targeting EEF1E1-related pathways. The potential of EEF1E1 as a biomarker for cancer diagnosis and prognosis further underscores the importance of this protein in biomedical research. Understanding the structural and functional characteristics of EEF1E1, along with its interactions with other cellular components, remains a significant avenue of investigation, with the aim of elucidating its complete role in both normal physiology and disease states. Consequently, the study of recombinant EEF1E1 not only furthers our understanding of fundamental biological processes but also holds promise for the innovation of targeted cancer therapies.
