Analytical Data
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Gene name
ERG
- Application
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Alternative Names
Transforming protein ERG
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11308
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Expression Region
1-486aa
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Molecular Weight
56.6 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
Related Products
Protein Description
The study of ERG (E26 transformation-specific related gene) recombinant proteins has garnered significant attention due to their critical role in various biological processes and disease mechanisms, particularly in cancer. ERG is a member of the ETS transcription factor family, which is involved in regulating gene expression during development and differentiation. Its overexpression has been implicated in several malignancies, most notably prostate cancer, where it is often fused with the androgen-regulated TMPRSS2 gene, creating a novel oncoprotein that promotes tumor growth and progression. Researchers have focused on developing recombinant ERG proteins to better understand their structure-function relationships, post-translational modifications, and interaction with other cellular proteins. By producing these proteins using recombinant DNA technology, scientists can investigate their biochemical properties, signaling pathways, and roles within the tumor microenvironment. Moreover, these studies aim to identify potential therapeutic targets and develop strategies for intervention that could lead to more effective treatments for cancers driven by ERG. The ongoing research surrounding ERG recombinant proteins not only sheds light on the molecular underpinnings of oncogenesis but also holds promise for innovative approaches in cancer diagnosis and therapy.
