Analytical Data
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Gene name
EEF1a2
- Application
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Alternative Names
EEF1a2；EEF1AL；STN；Elongation factor 1-alpha 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
Q05639
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Expression Region
1-463aa
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AA Sequence
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNVCGDSKSDPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK
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Molecular Weight
50.4 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
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Protein Description
EEF1A2, a member of the eukaryotic elongation factor 1 (EEF1) family, plays a critical role in protein synthesis by facilitating the elongation phase of translation. It is known to be involved in various cellular processes beyond its classical role, including cell proliferation, differentiation, and apoptosis. Studies indicate that EEF1A2 is overexpressed in several types of cancers, suggesting its potential as an oncogene and a promising target for therapeutic intervention. Researchers have focused on the biochemical properties of EEF1A2, including its ability to bind aminoacyl-tRNAs and participate in the assembly of ribosomes. Advances in recombinant protein technology have enabled the production of EEF1A2 for in vitro studies, allowing for detailed investigations into its functional mechanisms and interactions with other cellular components. Understanding the role of EEF1A2 in both normal physiology and disease states is crucial, as it may provide insights into novel strategies for cancer treatment and broader implications for the regulation of protein synthesis in eukaryotic cells. As ongoing research delves into its structure, function, and interactions, EEF1A2 continues to attract attention in the fields of molecular biology and oncology.
