Analytical Data
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Gene name
OTUB1
- Application
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Alternative Names
OTUB1；OTB1；Ubiquitin thioesterase OTUB1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96FW1
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Expression Region
1-271aa
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AA Sequence
MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSE RLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSH LEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVE KQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTV KEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFP EGSEPKVYLLYRPGHYDILYK
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Molecular Weight
33 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
OTUB1 (Ovarian Tumor Domain-Containing Protein 1) is a deubiquitinating enzyme that plays a crucial role in regulating various cellular processes by removing ubiquitin moieties from target proteins, thus influencing protein stability, signaling, and activity. Research on OTUB1 has gained significant attention due to its involvement in key biological functions, including DNA repair, immune response, and cell cycle regulation. Dysregulation of OTUB1 has been implicated in various diseases, including cancer, where it can contribute to tumorigenesis by stabilizing oncoproteins and inhibiting pro-apoptotic factors. Studies have shown that OTUB1 can modulate the activity of several key signaling pathways, including the NF-κB and p53 pathways, further highlighting its potential as a therapeutic target. The recombinant production of OTUB1 serves as a vital tool for elucidating its biochemical mechanisms and exploring its interactions with other cellular proteins. Understanding the structure-function relationship of OTUB1 and developing small molecules or peptides that can modulate its activity could provide new avenues for therapeutic intervention in cancer and other diseases where OTUB1 is dysregulated. Thus, the exploration of OTUB1 as a recombinant protein not only enhances our comprehension of its functional role in cellular homeostasis but also opens up prospects for novel therapeutic strategies.
