Analytical Data
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Gene name
USP1
- Application
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Alternative Names
UBP; Ubiquitin Carboxyl-Terminal Hydrolase 1; Ubiquitin Specific Protease 1; Deubiquitinating enzyme 1; Ubiquitin thioesterase 1; Ubiquitin-specific-processing protease 1
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Species
Rat
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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
Q569C3
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Expression Region
Met1~His198
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Molecular Weight
31kDa
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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
USP1 (Ubiquitin-specific protease 1) is a critical deubiquitinating enzyme involved in various cellular processes, including DNA damage repair, cell cycle regulation, and protein homeostasis. Recent studies have highlighted its essential role in the regulation of the Fanconi anemia (FA) pathway, which is crucial for the repair of DNA cross-links. The dysregulation of USP1 has been implicated in various cancers, making it a potential target for therapeutic intervention. Research into USP1 has revealed that it stabilizes several key proteins involved in DNA repair, such as FANCD2, by removing ubiquitin moieties that mark them for proteasomal degradation. The characterization of USP1's structure and enzymatic activity has paved the way for understanding its precise mechanisms and interactions within the cell. Furthermore, the development of small-molecule inhibitors targeting USP1 is gaining traction, aiming to enhance the efficacy of existing cancer treatments by interfering with the repair pathways that cancer cells exploit to survive genotoxic stress. Continued investigation of USP1 not only promises to elucidate its biological functions but also holds potential for advancing new therapeutic strategies in oncology.
