Analytical Data
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Gene name
ERV1
- Application
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Alternative Names
(14 kDa regulatory protein)(Essential for respiration and vegetative growth protein 1)
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Species
Saccharomyces cerevisiae
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Source
Yeast
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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
P27882
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Expression Region
1-189aa
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Molecular Weight
22.5 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
ERV1 (Endogenous Retrovirus 1) is a member of the class of endogenous retroviruses that are integrated into the genomes of many mammals, including humans. Research on ERV1 recombinant proteins has gained significance due to their potential roles in various biological processes and disease mechanisms. These proteins are believed to be involved in immune responses, with mechanisms that can modulate host cell activities. Furthermore, understanding ERV1 proteins can provide insights into the evolution of retroviruses and their interactions with host genomes. The study of ERV1 also extends to its implications in cancer biology, where its expression patterns may correlate with malignancies, suggesting a potential use as a biomarker or therapeutic target. Additionally, advances in recombinant DNA technology have enabled the production and characterization of ERV1 proteins, facilitating the exploration of their structure-function relationships. As a result, research on ERV1 recombinant proteins not only enhances our understanding of retroviral biology but also opens up avenues for innovative therapeutic strategies in treating diseases influenced by these viral components.
