Analytical Data
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Gene name
OTUD2
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简介
OTUD2 is a key hydrolase in cellular processes that actively participates in endoplasmic reticulum-associated degradation (ERAD) by deubiquitinating misfolded luminal proteins. It trims ubiquitin chains from the substrate, helping them pass through the VCP/p97 pore. OTUD2 Protein, Human is the recombinant human-derived OTUD2 protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
YOD1; Ubiquitin thioesterase OTU1; DUBA-8; HIV-1-induced protease 7; HIN-7; HsHIN7; OTU domain-containing protein 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
Q5VVQ6
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Expression Region
F2-V348
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Protein Length
Partial
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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
OTUD2 (OTU deubiquitinating enzyme 2) is a member of the ovarian tumor (OTU) family of deubiquitinating enzymes (DUBs), which play crucial roles in post-translational modifications, particularly in the regulation of protein ubiquitination and stability. The modification by ubiquitin can dictate protein fate, influencing processes like cell cycle progression, DNA repair, and signal transduction pathways. Research has indicated that OTUD2 may be involved in various cellular processes, including the modulation of immune responses and the regulation of protein degradation pathways. Its potential role in cancer biology has drawn significant interest, as aberrations in ubiquitination mechanisms are often linked to tumorigenesis. Furthermore, OTUD2's ability to interact with key signaling molecules suggests it could be a vital regulator in pathways associated with inflammation and infection. Given its functional importance, studying OTUD2's structure and biochemical properties through recombinant protein expression systems has become essential. These studies aim to elucidate the enzyme's mechanisms of action, substrate specificity, and regulatory domains, which could provide insights into its biological functions and potential as a therapeutic target. Understanding OTUD2 at the molecular level can pave the way for developing new strategies in treating diseases characterized by dysregulated ubiquitin-proteasome systems, particularly cancer and autoimmune disorders. Thus, OTUD2 presents a promising target for further investigation in both fundamental and applied research contexts.
