Analytical Data
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Gene name
EIF1
- Application
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Alternative Names
EIF1；SUI1;Eukaryotic translation initiation factor 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
P41567
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Expression Region
1-113aa
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AA Sequence
MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLVEIGLAKDDQLKVHGF
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Molecular Weight
39.7kDa
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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
EIF1 (Eukaryotic Translation Initiation Factor 1) is a crucial protein involved in the early stages of protein synthesis in eukaryotic cells. It plays a significant role in the selection of the correct start codon during the initiation phase of translation, ensuring that proteins are synthesized accurately and efficiently. Research on EIF1 has gained prominence due to its implications in various biological processes and diseases, including cancer, where dysfunctional translation initiation can lead to uncontrolled cell proliferation. The ability to produce recombinant EIF1 protein has advanced our understanding of its molecular mechanisms, as well as its interactions with other translation factors. By employing techniques such as molecular cloning and heterologous expression systems, researchers are able to generate large quantities of EIF1 for biochemical assays and structural studies. These investigations help elucidate the role of EIF1 in the ribosome assembly and its influence on the fidelity of translation. Furthermore, understanding EIF1’s mechanisms may lead to the development of novel therapeutic strategies targeting translation initiation in diseases characterized by dysregulated protein synthesis. Overall, the study of recombinant EIF1 protein is a vital area of research that bridges basic biology and potential clinical applications.
