Analytical Data
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Gene name
USP14
- Application
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Alternative Names
TGT; tRNA-Guanine Transglycosylase; Ubiquitin Specific Protease 14; Deubiquitinating enzyme 14; Ubiquitin carboxyl-terminal hydrolase 14
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Species
Human
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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
P54578
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Expression Region
Met1~Gln494
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Molecular Weight
60kDa
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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
Related Products
Protein Description
USP14 (Ubiquitin Specific Peptidase 14) is a pivotal deubiquitinating enzyme involved in the regulation of protein degradation, particularly in the context of the ubiquitin-proteasome system (UPS). It plays a crucial role in maintaining cellular protein homeostasis by removing ubiquitin tags from proteins destined for destruction, thereby modulating their stability and function. Research has increasingly highlighted the significance of USP14 in various physiological and pathological processes, including neurodegeneration, cancer, and immune responses. The aberrant activity of USP14 has been linked to the accumulation of misfolded proteins, which is a hallmark of debilitating diseases like Alzheimer's and Parkinson's. Consequently, there is growing interest in characterizing the biochemical properties of USP14, understanding its regulatory mechanisms, and exploring its potential as a therapeutic target. Recent studies utilizing recombinant USP14 proteins have facilitated insights into its enzymatic activity, substrate specificity, and interactions with other cellular components. These investigations not only enhance our understanding of the UPS but also open avenues for developing novel strategies to modulate USP14 function in disease contexts, emphasizing its relevance in drug discovery and developmental biology.
