Analytical Data
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Gene name
OTUD1
- Application
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Alternative Names
DUBA7; OTDC1
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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
Q5VV17
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Expression Region
Lys309~Ser481
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Molecular Weight
23kDa
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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
OTUD1, a member of the ovarian tumor domain-containing protein family, has emerged as a significant focus of research due to its crucial role in regulating cellular ubiquitination processes. Ubiquitination, a post-translational modification, is fundamental for various cellular functions, including protein degradation, cell cycle regulation, and DNA repair mechanisms. Recent studies have indicated that OTUD1 functions as a deubiquitinating enzyme (DUB), removing ubiquitin moieties from target proteins and thereby influencing their stability and activity. This has implications in multiple physiological and pathological contexts, including cancer and neurodegenerative diseases, where dysregulation of ubiquitination pathways is frequently observed. Furthermore, OTUD1 is involved in the modulation of immune responses and has been linked to viral infections, underscoring its potential as a therapeutic target. Research into OTUD1 and its recombinant protein form has provided insights into its enzymatic mechanisms and interaction partners, paving the way for a deeper understanding of its biological significance and potential applications in targeted therapies. The ongoing exploration of OTUD1's functions and its role in cellular processes positions it as a promising candidate for further investigation in both basic and applied biomedical research.
