Analytical Data
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Gene name
EIF1B
- Application
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Alternative Names
EIF1B;Eukaryotic translation initiation factor 1b
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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
O60739
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Expression Region
1-113aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSTIQNLQSFDPFADATKGDDLLPAGTEDY IHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYG EVIQLQGDQRKNICQFLLEVGIVKEEQLKVHGF
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Molecular Weight
15 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
EIF1B, or eukaryotic translation initiation factor 1B, plays a pivotal role in the initiation phase of translation, acting as a key component that facilitates the binding of the ribosome to the mRNA. Recent studies have highlighted its significance in various biological processes, including cell proliferation, differentiation, and stress response. Aberrations in EIF1B expression and function have been implicated in several cancers, suggesting its potential as a therapeutic target. To further investigate the molecular mechanisms of EIF1B and its interactions within the translational machinery, researchers are increasingly focusing on the production of recombinant EIF1B protein. This enables detailed structural and functional analyses, paving the way for a better understanding of its role in translation and its contribution to disease pathology. Furthermore, the ability to produce large quantities of pure EIF1B protein allows for the exploration of its biochemical properties, interaction with other translation factors, and the development of EIF1B-targeted therapies. Thus, the study of recombinant EIF1B not only enhances our comprehension of fundamental cellular processes but also offers promising avenues for clinical applications in oncology and other fields.
