Analytical Data
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Gene name
UBE2E3
- Application
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Alternative Names
UBE2E3；UBCE4；Ubiquitin-conjugating enzyme E2 E3
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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
Q969T4
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Expression Region
2-207aa
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AA Sequence
SSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK LSSKTTAKLS TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP PGSVYEGGVF FLDITFSSDY PFKPPKVTFR TRIYHCNINS QGVICLDILK DNWSPALTIS KVLLSICSLL TDCNPADPLV GSIATQYLTN RAEHDRIARQ WTKRYAT
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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
UBE2E3, a member of the ubiquitin-conjugating enzyme (E2) family, plays a critical role in the ubiquitin-proteasome system, which regulates various cellular processes by tagging proteins for degradation, thus maintaining protein homeostasis. Research has shown that UBE2E3 is involved in the modification of a variety of substrates, influencing processes such as cell cycle regulation, apoptosis, and DNA damage repair. Its aberrant expression has been linked to several diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. The functional characterization of UBE2E3, including its substrate specificity and interaction with E3 ligases, is essential for understanding its role in cellular signaling pathways. Recent studies have focused on the structural biology of UBE2E3 to elucidate its enzymatic mechanisms and interactions at the molecular level. Furthermore, the development of UBE2E3 inhibitors or modulators holds promise for novel strategies in disease intervention, making it a significant focus within the fields of molecular biology and pharmacology. As research continues to unveil the complexities of UBE2E3 function and its implications in health and disease, it remains a crucial component for investigating the ubiquitin-mediated regulatory networks within cells.
