Analytical Data
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Gene name
ubiC
- Application
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Alternative Names
CL (CPL)
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Species
Escherichia coli
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P26602
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Expression Region
2-165aa
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Molecular Weight
19.5 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 study of Ubiquitin (UbiC) recombinant proteins has gained significant attention in molecular biology and biochemistry due to their crucial role in the ubiquitin-proteasome system, which regulates protein degradation, cell cycle progression, and various cellular processes. UbiC is a key player in tagging proteins for degradation, thereby maintaining cellular homeostasis and responding to stress signals. The exploration of UbiC recombinant proteins is particularly important for understanding the mechanisms of diseases linked to misregulated protein homeostasis, such as cancer and neurodegenerative disorders. Advances in recombinant protein technology have facilitated the production and purification of UbiC, allowing researchers to investigate its functional dynamics and interactions with other proteins in vitro and in vivo. These studies can elucidate the molecular pathways involved in protein turnover and potentially pave the way for therapeutic interventions targeting the ubiquitin-proteasome system. Furthermore, UbiC's ability to form multifaceted complexes highlights its importance in cellular signaling and regulation, making it a vital subject of research across various fields, including drug development and synthetic biology. As the understanding of UbiC and its mechanisms deepens, it holds promise for novel strategies in combating diseases linked to dysfunctional protein degradation pathways.
