Analytical Data
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Gene name
UBE2L3
- Application
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Alternative Names
UBE2L3；UBCE7；UBCH7；Ubiquitin-conjugating enzyme E2 L3
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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
P68036
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Expression Region
1-154aa
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AA Sequence
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGA FRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATK TDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEK RPVD
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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
UBE2L3, a member of the ubiquitin-conjugating enzyme family, plays a crucial role in the post-translational modification of proteins through ubiquitination, a process essential for regulating various cellular functions, including protein degradation, cell cycle progression, and DNA repair. Research has increasingly highlighted UBE2L3’s involvement in numerous biological processes and diseases, including cancer, immune response, and viral infections. Elevated levels of UBE2L3 have been associated with various malignancies, suggesting that it may serve as a potential biomarker or therapeutic target. Furthermore, its interaction with different E3 ligases and substrates underscores its regulatory complexity in the ubiquitin-proteasome system. Understanding the precise functions and mechanisms of UBE2L3 through recombinant protein studies can provide insights into its role in cellular homeostasis and disease pathology. This knowledge may facilitate the development of novel interventions aimed at modulating UBE2L3 activity for therapeutic purposes, emphasizing the significance of UBE2L3 in both fundamental biology and translational medicine.
