Analytical Data
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Gene name
EIF4A2
- Application
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Alternative Names
ATP-dependent RNA helicase eIF4A-2
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14240
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Expression Region
1-407aa
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Molecular Weight
73.4 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
Related Products
Protein Description
EIF4A2, or Eukaryotic Translation Initiation Factor 4A2, is a member of the eIF4A family, which plays a critical role in the initiation of protein synthesis by unwinding the secondary structure of mRNA. This factor is vital for translation regulation, influencing cellular responses to stress, growth signals, and other environmental cues. Recent studies have highlighted the importance of EIF4A2 in various cancers, where its overexpression is often associated with enhanced tumorigenicity and poor prognosis. This has made EIF4A2 a potential therapeutic target, as inhibiting its function could disrupt aberrant protein synthesis in cancer cells. Moreover, EIF4A2 has been implicated in the regulation of specific mRNAs that encode for proteins involved in cell proliferation and survival. Research into recombinant EIF4A2 proteins aims to better understand their structure, function, and interaction with other translation initiation factors and regulatory proteins. Such studies may lead to the development of small molecules or biologics that can specifically target EIF4A2 in cancer therapy, offering a promising avenue for improving treatment outcomes. Understanding the precise molecular mechanisms by which EIF4A2 modulates translation could also provide insights into broader regulatory networks in cellular metabolism and homeostasis.
