Analytical Data
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Gene name
OTUD5
- Application
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Alternative Names
Deubiquitinating enzyme A;DUBA
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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
Q96G74
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Expression Region
1-571 aa
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AA Sequence
MTILPKKKPPPPDADPANEPPPPGPMPPAPRRGGGVGVGGGGTGVGGGDRDRDSGVVGARPRASPPPQGPLPGPPGALHRWALAVPPGAVAGPRPQQASPPPCGGPGGPGGGPGDALGAAAAGVGAAGVVVGVGGAVGVGGCCSGPGHSKRRRQAPGVGAVGGGSPEREEVGAGYNSEDEYEAAAARIEAMDPATVEQQEHWFEKALRDKKGFIIKQMKEDGACLFRAVADQVYGDQDMHEVVRKHCMDYLMKNADYFSNYVTEDFTTYINRKRKNNCHGNHIEMQAMAEMYNRPVEVYQYSTGTSAVEPINTFHGIHQNEDEPIRVSYHRNIHYNSVVNPNKATIGVGLGLPSFKPGFAEQSLMKNAIKTSEESWIEQQMLEDKKRATDWEATNEAIEEQVARESYLQWLRDQEKQARQVRGPSQPRKASATCSSATAAASSGLEEWTSRSPRQRSSASSPEHPELHAELGMKPPSPGTVLALAKPPSPCAPGTSSQFSAGADRATSPLVSLYPALECRALIQQMSPSAFGLNDWDDDEILASVLAVSQQEYLDSMKKNKVHRDPPPDKS
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Molecular Weight
63.4 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
OTUD5 is a member of the ovarian tumor (OTU) deubiquitinating enzyme family, which plays a critical role in cellular protein regulation through the removal of ubiquitin chains from target proteins. The research surrounding OTUD5 has garnered significant attention due to its involvement in various biological processes, including cell cycle regulation, DNA repair, and immune response. Dysregulation of OTUD5 has been linked to several diseases, including cancer, where it may influence tumor progression and metastasis by altering the stability and activity of key signaling proteins. Furthermore, OTUD5 has been identified as a potential therapeutic target, prompting investigations into its enzymatic mechanisms and interactions with other cellular pathways. Studies employing recombinant OTUD5 protein have been essential for elucidating its structure-function relationships and developing inhibitors that could modulate its activity in pathophysiological conditions. This growing body of evidence emphasizes the importance of OTUD5 as a critical player in the ubiquitin-proteasome system and its potential implications in therapeutic strategies for diseases characterized by aberrant ubiquitination. Overall, the research on OTUD5 not only enhances our understanding of post-translational modifications but also paves the way for novel interventions in disease management.
