Analytical Data
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Gene name
EIF5A2
- Application
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Alternative Names
EIF5A2;Eukaryotic translation initiation factor 5A-2
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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
Q9GZV4
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Expression Region
1-153aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMADEIDFTTGDAGASSTYPMQCSALRKNGF VVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD VPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAG EDVQVSVMCAMSEEYAVAIKPCK
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Molecular Weight
19 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
EIF5A2, or Eukaryotic Translation Initiation Factor 5A2, is a highly conserved protein involved in the translation process and plays a crucial role in cellular growth and proliferation. Recent studies have highlighted its significance in various cellular functions, including the regulation of mRNA stability and translation of specific proteins, particularly in response to stress conditions. Notably, EIF5A2 is implicated in several cancers, where its overexpression is associated with tumor progression and poor prognosis, making it a potential target for therapeutic intervention. Furthermore, the protein undergoes unique post-translational modifications, such as hypusination, which are essential for its activity, suggesting a complex regulatory mechanism at play. As research continues to unravel its multifaceted roles, recombinant EIF5A2 proteins are being produced to explore their functional dynamics in cellular pathways and assess their potential as biomarkers or therapeutic agents in malignancies. Understanding the structural and functional properties of EIF5A2 through recombinant techniques is vital for elucidating its contribution to oncogenesis and could pave the way for novel cancer treatment strategies.
