Analytical Data
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Gene name
UBC10
- Application
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Alternative Names
E2 ubiquitin-conjugating enzyme 10 Ubiquitin carrier protein 10/12 Ubiquitin-conjugating enzyme E2-17 kDa 10/12 Ubiquitin-protein ligase 10/12
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Species
Arabidopsis thaliana
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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
P35133
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Expression Region
1-148aa
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Molecular Weight
20.6 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
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Protein Description
UBC10, a member of the E2 ubiquitin-conjugating enzyme family, plays a crucial role in the ubiquitin-proteasome system (UPS), which is essential for maintaining cellular homeostasis and regulating protein degradation. This small protein facilitates the transfer of ubiquitin, a small regulatory protein, to target substrates, marking them for degradation by the proteasome. The research surrounding UBC10 has gained momentum due to its significant involvement in various cellular processes, including cell cycle regulation, DNA repair, and stress responses. Abnormal functioning of UBC10 has been linked to several diseases, including cancer, where its altered expression can lead to the dysregulation of oncogenic proteins. Additionally, studies have shown that UBC10 is involved in the modulation of key signaling pathways, impacting processes such as apoptosis and cellular differentiation. Given these critical functions, understanding the molecular mechanisms of UBC10's activity and regulation is paramount for the development of therapeutic strategies targeting diseases associated with the UPS. Recent studies have focused on the structural insights into UBC10, its interactions with other proteins, and the implications of post-translational modifications on its functionality. This research not only elucidates the fundamental biology of UBC10 but also opens avenues for potential interventions in pathologies where the ubiquitin-proteasome system is compromised.
