Analytical Data
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Gene name
EEF1a2
- Application
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Alternative Names
STN; EF1A; EEF1AL; EF-1-alpha-2; HS1; STNL; Statin-Like; Statin-S1; Eukaryotic elongation factor 1 A-2
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Species
Human
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Source
E. coli
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Tag
N-His
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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
Gly213~Lys463
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Molecular Weight
36&34kDa
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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, or Eukaryotic Translation Elongation Factor 1 Alpha 2, is a crucial protein involved in the translation process, facilitating the delivery of aminoacyl-tRNA to the ribosome during protein synthesis. Recent studies have highlighted its significant role not only in protein synthesis but also in various cellular processes such as cell proliferation, differentiation, and apoptosis. Alterations in the expression levels of EEF1A2 have been implicated in several diseases, including cancer, where it is often found to be overexpressed, contributing to tumor growth and metastasis. The interest in recombinant EEF1A2 stems from its potential as a therapeutic target and a biomarker for cancer progression. Additionally, the ability to produce this protein in a recombinant form allows for detailed structural and functional studies, which can further elucidate its role in disease mechanisms. Understanding the functional dynamics of EEF1A2 can offer insights into developing novel therapeutic strategies, particularly in oncology. Thus, ongoing research focusing on the characterization, regulation, and potential applications of recombinant EEF1A2 is essential for advancing our understanding of its contributions to cellular biology and disease pathology.
