Analytical Data
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Gene name
Wnt4
- Application
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Species
Human
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P56705
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Expression Region
23-351aa
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Molecular Weight
43.6 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
The eukaryotic translation initiation factor 4E (eIF4E) is a crucial regulator of protein synthesis, playing a significant role in the initiation phase of translation. Abnormal expression and activity of eIF4E have been associated with various diseases, particularly cancer, making it a target of intense research. This protein binds to the 5' cap of mRNA, facilitating ribosome recruitment and subsequent translation of capped mRNAs. Overexpression of eIF4E has been linked to increased malignancy and poor patient prognosis, as it can lead to preferential translation of oncogenes and survival factors. Conversely, reduced eIF4E levels are implicated in certain diseases, highlighting its dual role in cellular function. Researchers have focused on the structural and functional characterization of eIF4E, including its interactions with other initiation factors and regulatory proteins. Understanding the mechanisms governing eIF4E activity is crucial for developing targeted therapeutic strategies, given its pivotal role in controlling gene expression and cell proliferation. Recent studies have also explored the potential of eIF4E as a biomarker for cancer diagnosis and prognosis, further underscoring its relevance in translational medicine. As the insights into eIF4E's role in pathophysiology deepen, the prospect of designing eIF4E inhibitors or modulators offers exciting avenues for innovative cancer treatments and other related diseases.
