Analytical Data
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Gene name
E2
- Application
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Alternative Names
E2；UBCH8；Ubiquitin-conjugating enzyme E2 E2
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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
O14933
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Expression Region
1-153aa
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AA Sequence
MMASMRVVKE LEDLQKKPPP YLRNLSSDDA NVLVWHALLL PDQPPYHLKA FNLRISFPPE YPFKPPMIKF TTKIYHPNVD ENGQICLPII SSENWKPCTK TCQVLEALNV LVNRPNIREP LRMDLADLLT QNPELFRKNA EEFTLRFGVD RPS
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Molecular Weight
17.7 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
E2 recombinant proteins have garnered significant interest in the field of molecular biology and biomedicine due to their critical roles in various biological processes and potential therapeutic applications. The E2 protein, often associated with viral replication, particularly in the context of hepatitis C virus and other flaviviruses, functions as a key structural component in the viral envelope, influencing viral assembly and entry into host cells. Given the increasing prevalence of viral infections globally, understanding the structure and function of E2 proteins is essential for developing effective vaccines and antiviral therapies. Furthermore, E2 proteins serve as valuable tools in research and biotechnology, facilitating studies on protein interactions and vaccine development. Recent advancements in recombinant DNA technology have made it feasible to produce E2 proteins in heterologous systems, allowing researchers to investigate their properties in detail. This has led to insights into their immunogenicity and the potential for designing E2-based vaccines. As a result, E2 recombinant proteins are not only vital for unraveling the mechanisms of viral pathogenesis but also hold promise for translating research findings into clinical applications, highlighting their importance in combating viral diseases and advancing therapeutic innovations.
