Analytical Data
-
Gene name
OTUD6B
- Application
-
Alternative Names
CGI-77; DUBA-5; DUBA5; OTU domain containing protein 6B; OTU domain-containing protein 6B; OTU6B_HUMAN; OTUD6B
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8N6M0
-
Expression Region
1-293 aa
-
AA Sequence
MEAVLTEELD EEEQLLRRHR KEKKELQAKI QGMKNAVPKN DKKRRKQLTE DVAKLEKEME QKHREELEQL KLTTKENKID SVAVNISNLV LENQPPRISK AQKRREKKAA LEKEREERIA EAEIENLTGA RHMESEKLAQ ILAARQLEIK QIPSDGHCMY KAIEDQLKEK DCALTVVALR SQTAEYMQSH VEDFLPFLTN PNTGDMYTPE EFQKYCEDIV NTAAWGGQLE LRALSHILQT PIEIIQADSP PIIVGEEYSK KPLILVYMRH AYGLGEHYNS VTRLVNIVTE NCS
-
Molecular Weight
33.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 is a deubiquitinating enzyme (DUB) that plays a crucial role in the regulation of various cellular processes, including protein degradation, signal transduction, and cell cycle progression. Emerging evidence suggests that dysregulation of OTUD6B is associated with several diseases, particularly cancers, where it may influence tumor growth and response to therapies by modulating the ubiquitin-proteasome system. The ability of OTUD6B to remove ubiquitin moieties from substrate proteins can affect their stability and function, thereby impacting key signaling pathways such as NF-κB and p53. Given its important biological functions, OTUD6B has become a focus of research in the fields of cancer biology and proteostasis. Understanding its biochemical mechanisms and regulatory networks could provide insights into novel therapeutic strategies to target various malignancies. Research efforts are also directed toward characterizing the overall structure and enzymatic activity of OTUD6B, as well as identifying its substrates and interacting partners. Thus, the study of OTUD6B recombinants is not only fundamental for grasping the intricacies of ubiquitin signaling but also holds potential for advancing cancer treatment and enhancing our understanding of cellular homeostasis.
