Analytical Data
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Gene name
elF5A
- Application
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Alternative Names
elF5A;Eukaryotic translation initiation factor 5A-1
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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
Q9XI91
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Expression Region
1-158aa
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AA Sequence
MSDEEHHFES SDAGASKTYP QQAGTIRKNG YIVIKNRPCK VVEVSTSKTG KHGHAKCHFV AIDIFTSKKL EDIVPSSHNC DVPHVNRTDY QLIDISEDGY VSLLTDNGST KDDLKLPNDD TLLQQIKSGF DDGKDLVVSV MSAMGEEQIN ALKDIGPK
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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
eIF5A, or eukaryotic translation initiation factor 5A, is a highly conserved protein that plays a critical role in cellular processes, particularly in translation initiation and elongation. Its unique structure, characterized by the presence of the uncommon amino acid hypusine, is integral to its function in promoting the translation of specific mRNAs, especially those involved in cell proliferation and stress response. Research on eIF5A has gained momentum due to its implications in various diseases, including cancer and viral infections, where altered expression levels of eIF5A have been linked to tumorigenesis and viral replication. The study of recombinant eIF5A protein allows for a deeper understanding of its biochemical properties, interaction with other cellular components, and its role in regulating translation under different cellular stresses. By utilizing advanced molecular biology techniques to produce and analyze recombinant eIF5A, researchers aim to elucidate its mechanism of action, potential therapeutic targets, and its significance in disease pathology. This research not only contributes to the fundamental understanding of translation regulation but also opens avenues for developing novel interventions in diseases where eIF5A is implicated.
