Analytical Data
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Gene name
EIF5A2
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简介
EIF5A2 is a translation factor critical for promoting elongation and termination, helping stalled ribosomes encounter specific amino acid environments. EIF5A2 is located between the ribosome exit (E) and peptidyl (P) sites and rescues stalled ribosomes, especially those translating polyproline-containing peptides. EIF5A2 Protein, Human (His) is the recombinant human-derived EIF5A2 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
Eukaryotic translation initiation factor 5A-2; Eukaryotic initiation factor 5A isoform 2; EIF5A2
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9GZV4
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Expression Region
M1-K153
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Protein Length
Full Length
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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
EIF5A2, or Eukaryotic Translation Initiation Factor 5A2, is a crucial protein involved in the regulation of translation and cellular stress responses. Research on EIF5A2 has gained momentum due to its significant role in various cellular processes, including cell proliferation, differentiation, and apoptosis. This protein is unique in containing a modified amino acid, hypusine, which is essential for its function in translation initiation and elongation. Aberrant expression of EIF5A2 has been implicated in several cancers, highlighting its potential as a therapeutic target and a biomarker for tumor progression. In recent studies, the recombinant expression of EIF5A2 has been utilized to investigate its functional properties and interaction with other cellular components, paving the way for understanding the molecular mechanisms underlying its role in health and disease. Furthermore, the study of EIF5A2 in the context of stress conditions, such as hypoxia and nutrient deprivation, has revealed its adaptive functions that are critical for cellular survival. Given these findings, ongoing research aims to elucidate the precise mechanisms by which EIF5A2 contributes to oncogenesis and its potential utility in clinical applications, including cancer diagnosis and therapy.











