Analytical Data
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Gene name
OTUD6B
- Application
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Alternative Names
DUB; OTUD6B; ovarian tumor domain
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Species
Human
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Source
E. coli
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Tag
N-His;Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A087X0W9
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Expression Region
E2-S323
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Protein Length
Full Length of Mature Protein
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Molecular Weight
38-42 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
OTUD6B (OTU deubiquitinating enzyme 6B) is a member of the OTU subfamily of deubiquitinating enzymes, which play critical roles in various cellular processes by removing ubiquitin from proteins, thereby regulating their stability, localization, and function. Research on OTUD6B has gained prominence due to its involvement in several biological pathways, including cell cycle regulation, DNA repair, and immune response, making it a potential target for therapeutic interventions. Dysregulation of OTUD6B has been linked to various diseases, including cancer, where altered ubiquitination can lead to abnormal protein function and tumorigenesis. Recent studies have highlighted its role in modulating key signaling pathways, further emphasizing its importance in cellular homeostasis. Given the increasing interest in the ubiquitin-proteasome system as a therapeutic target, understanding the functional mechanisms of OTUD6B and characterizing its recombinant protein is crucial for elucidating its biological significance and potential for drug development. Investigating OTUD6B's interactions with other cellular components may provide insights into its precise role in disease contexts and unveil novel strategies for targeting related pathways in clinical settings. As such, the study of OTUD6B recombinant protein is not only fundamental for basic biology but also bears significant implications for therapeutic advancements in human health.
