Analytical Data
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Gene name
DC-UbP
- Application
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Alternative Names
UBTD2; DCUBP; SB72; Ubiquitin domain-containing protein 2; Dendritic cell-derived ubiquitin-like protein; DC-UbP; Ubiquitin-like protein SB72
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WUN7
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Expression Region
1-190aa
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AA Sequence
MTDGQLRSKRDEFWDTAPAFEGRKEIWDALKAAAHAFESNDHELAQAIIDGANITLPHGALTECYDELGNRYQLPVYCLAPPINMIEEKSDIETLDIPEPPPNSGYECQLRLRLSTGKDLKLVVRSTDTVFHMKRRLHAAEGVEPGSQRWFFSGRPLTDKMKFEELKIPKDYVVQVIVSQPVQNPTPVEN
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Molecular Weight
46.64 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
DC-UbP, or Deubiquitinating Enzyme C-terminal ubiquitin-like protein, has garnered significant attention in recent years due to its crucial role in regulating protein homeostasis and cellular signaling pathways. Ubiquitination, a post-translational modification involving the addition of ubiquitin to proteins, is essential for various cellular processes, including protein degradation, cell cycle regulation, and stress responses. Dysregulation of ubiquitination has been implicated in numerous diseases, including cancer, neurodegeneration, and inflammatory disorders. DC-UbP appears to play a vital role in counteracting ubiquitination by removing ubiquitin moieties from target proteins, thus modulating their stability and function. Research into DC-UbP has revealed its potential as a therapeutic target, as enhancing its activity could restore normal cellular functions disrupted by aberrant ubiquitination. Current studies focus on elucidating the structural and functional characteristics of DC-UbP, exploring its interaction with various substrates, and examining its regulatory mechanisms within the ubiquitin-proteasome system. Understanding the detailed biochemistry of DC-UbP will not only enhance our knowledge of ubiquitin-mediated processes but also open new avenues for the development of targeted therapies in diseases related to ubiquitin dysregulation. This is critical as the demand for novel therapeutic strategies is urgent in light of the rising prevalence of conditions linked to ubiquitin system malfunction.
