Analytical Data
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Gene name
E1
- Application
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Alternative Names
ATP-dependent helicase E1
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Species
Human papillomavirus type 11
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Source
E. coli
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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
P04014
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Expression Region
452-602aa
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Molecular Weight
23.1 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
E1 recombinant protein, specifically related to the E1 enzyme of viruses, is a significant focus in biomedical research due to its critical role in viral replication and assembly. It serves as a pivotal component in the life cycle of various viruses, including those that cause serious diseases in humans and animals. The study of E1 recombinant proteins facilitates a deeper understanding of virus-host interactions and can provide insights into potential therapeutic targets. For instance, in the context of alphaviruses, the E1 protein is essential for membrane fusion and entry into host cells, making it a prime candidate for vaccine development and antiviral strategies. Researchers have been able to produce E1 proteins using recombinant DNA technology, allowing for the analysis of their structure and function in detail. Such studies have the potential to aid in the design of vaccines that elicit strong immune responses or in the development of inhibitors that disrupt viral life cycles, thereby mitigating the impacts of viral infections. Additionally, understanding the immunogenic properties of E1 proteins is crucial for the development of diagnostic tools and therapeutic agents. As global health concerns continue to rise, particularly in the context of emerging infectious diseases, research into E1 recombinant proteins remains a vital area of investigation for combating viral threats and enhancing public health safety.
