Analytical Data
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Gene name
UBC8
- Application
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Alternative Names
E2 ubiquitin-conjugating enzyme 8;UBCAT4A;Ubiquitin carrier protein 8;Ubiquitin-conjugating enzyme E2-17 kDa 8;Ubiquitin-protein ligase 8
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Species
Arabidopsis thaliana
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35131
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Expression Region
1-148aa
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Molecular Weight
24.0 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
The UBC8 protein, a member of the ubiquitin-conjugating enzyme family, plays a crucial role in the ubiquitin-proteasome system, which regulates protein degradation and is vital for various cellular processes, including cell cycle progression, signal transduction, and stress responses. Research into UBC8 has gained momentum due to its involvement in modifying target proteins through ubiquitination, subsequently influencing their stability, activity, and localization. Experiments have indicated that UBC8 is particularly significant in certain developmental stages and stress conditions, such as those encountered in plants, where it is implicated in responses to environmental stimuli. Understanding the functional mechanisms of UBC8 requires elucidating its interactions with other proteins and identifying its specific substrates, which can vary by organism and cellular context. The study of UBC8 not only enhances our comprehension of fundamental biological processes but also has implications in agriculture and biotechnology, where manipulating its pathways could improve stress resistance in crops. Furthermore, dysregulation of ubiquitin-conjugating enzymes like UBC8 has been linked to various diseases, including cancer, highlighting the importance of this protein in both basic and applied research. As such, UBC8 serves as an intriguing target for further investigations aimed at unraveling its complex roles in cellular physiology and potential therapeutic strategies.
