Analytical Data
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Gene name
EIF5
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简介
The EIF5 protein is a key member of the 43S pre-initiation complex (43S PIC) and actively participates in mRNA cap-proximal binding, scanning 5'-untranslated regions and locating start codons. EIF5 Protein, Human (GST) is the recombinant human-derived EIF5 protein, expressed by E. coli , with N-GST labeled tag.
- Application
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Alternative Names
Eukaryotic translation initiation factor 5; eIF-5
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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 95% as determined by SDS-PAGE.
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Uniprot
P55010
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Expression Region
M1-D150
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Protein Length
Partial
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Molecular Weight
18 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
EIF5, or Eukaryotic Translation Initiation Factor 5, plays a crucial role in the initiation phase of eukaryotic protein synthesis. It is essential for the recruitment of the initiator tRNA to the ribosome, facilitating the assembly of the translation initiation complex. Research on EIF5 has gained significant attention due to its involvement in various cellular processes and its potential implications in diseases such as cancer. Abnormalities in EIF5 expression or function can disrupt normal protein synthesis and contribute to oncogenesis and tumor progression. Furthermore, EIF5 has been identified as a promising target for therapeutic intervention, as modulating its activity may influence the translation of specific oncogenes. The recombinant production of EIF5 has emerged as a powerful approach to study its structure, function, and interaction with other translational components. By generating a high-quality recombinant EIF5 protein, researchers can perform in-depth biochemical assays, investigate the conformational changes during translation initiation, and screen for small molecules that can selectively modulate EIF5 activity. This research could enhance our understanding of the fundamental mechanisms controlling gene expression and open new avenues for cancer therapy, making EIF5 a significant focus in the field of molecular biology and medical research.
