Analytical Data
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Gene name
USP31
- Application
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Alternative Names
Deubiquitinating enzyme 31; KIAA1203; Ubiquitin carboxyl terminal hydrolase 31; Ubiquitin carboxyl-terminal hydrolase 31; Ubiquitin specific peptidase 31; Ubiquitin specific processing protease 31; Ubiquitin specific protease 31; Ubiquitin specific Proteinase 31; Ubiquitin thioesterase 31; Ubiquitin thiolesterase 31; Ubiquitin-specific-processing protease 31; UBP31_HUMAN; USP 31; USP31
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q70CQ4
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Expression Region
1254-1352 aa
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AA Sequence
AGGSSVKSVCKNTGDDEAERGHQPPASQQPNANTTGKEQLVTKDPASAKHSLLSARKSKSSQLDSGVPSSPGGRQSAEKSSKKLSSSMQTSARPSQKPQ
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Molecular Weight
36.63 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
Related Products
Protein Description
USP31, a member of the ubiquitin-specific protease family, has garnered significant attention in recent years due to its critical role in the regulation of cellular processes through the deubiquitination of substrate proteins. Ubiquitination, a post-translational modification, governs various cellular functions, including proteostasis, signal transduction, and the cell cycle. Dysregulation of deubiquitinating enzymes like USP31 is implicated in various diseases, including cancers and neurodegenerative disorders, making it a potential therapeutic target. Research into USP31 has revealed its involvement in modulating the stability and activity of key signaling proteins, thus influencing pathways such as the NF-κB and p53 signaling cascades. Additionally, USP31 has been shown to interact with viral proteins, suggesting a role in host-pathogen interactions. Understanding the structural and functional mechanisms of USP31 through the study of its recombinant protein could pave the way for the development of novel therapeutic strategies aimed at manipulating its activity, thereby providing new avenues for disease intervention. With ongoing investigations into its substrate specificity and regulatory mechanisms, USP31 continues to be a focal point of research in the quest to elucidate the complex landscape of protein regulation within cells.
