Analytical Data
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Gene name
OTUD6A
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简介
The OTUD5 protein is a deubiquitinating enzyme with complex regulatory functions that acts as a negative regulator in the innate immune system. It exhibits peptidase activity against "Lys-48" and "Lys-63" linked polyubiquitin chains, and in vitro, it can cleave "Lys-11" linked ubiquitin chains. OTUD6A Protein, Human is the recombinant human-derived OTUD6A protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
OTUD6A; OTU domain-containing protein 6A; DUBA-2
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7L8S5
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Expression Region
M1-L288
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Protein Length
Full Length
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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
OTUD6A (OTU deubiquitinase 6A) is a member of the ovarian tumor (OTU) family of deubiquitinating enzymes (DUBs) known for their role in regulating protein ubiquitination, a crucial post-translational modification that influences various cellular processes, including protein degradation, signaling pathways, and immune responses. As a DUB, OTUD6A specifically removes ubiquitin chains from target proteins, thus reversing the ubiquitination process and potentially stabilizing proteins that are involved in critical cellular functions. Recent studies have highlighted its importance in cancer biology, as OTUD6A has been implicated in the modulation of oncogenic pathways and tumor suppression. The dysregulation of this enzyme is associated with various malignancies, indicating that it may serve as a potential therapeutic target. The need for a recombinant form of OTUD6A arises from the necessity to study its enzymatic activity, substrate specificity, and interactions with other molecular partners in vitro. By utilizing recombinant OTUD6A proteins, researchers can explore its mechanistic roles in cell signaling and development, paving the way for novel therapeutic strategies that exploit its regulatory functions in both normal and diseased states. Studies focusing on the production and functional characterization of OTUD6A recombinant protein are essential for advancing our understanding of its biological significance and therapeutic potential in various diseases, particularly cancer. The development of reliable assays for OTUD6A activity and the identification of its substrates may ultimately lead to the discovery of new biomarkers and treatment options that could improve patient outcomes.
