Analytical Data
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Gene name
OTUD4
- Application
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Alternative Names
OTU domain-containing protein 4. EC:3.4.19.12. HIV-1-induced protein HIN-1
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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
Q01804
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Expression Region
1-401 aa
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AA Sequence
MWAPHSYLYPLHQAYLAACRMYPKVPVPVYPHNPWFQEAPAAQNESDCTCTDAHFPMQTEASVNGQMPQPEIGPPTFSSPLVIPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKNMFPQPSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDEKGELDLSLENLDLSKDCGSVSTVDEFPEARGEHVHSLPEASVSSKPDEGRTEQSSQTRKADTALASIPPVAEGKAHPPTQILNRERETVPVELEPKRTIQSLKEKTEKVKDPKTAADVVSPGANSVDSRVQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGYSGRGGYQHVRSEESWKGQPSRSRDEGYQYHRNVRGRPFRGDRRRSGMGDGHRGQHT
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Molecular Weight
71.2 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
OTUD4, a member of the OTU deubiquitinase family, plays a crucial role in the cellular regulation of protein stability and signaling pathways through its ability to hydrolyze ubiquitin chains. In recent years, it has gained attention due to its involvement in various physiological and pathological processes, including immune responses, cellular stress responses, and tumorigenesis. The dysregulation of OTUD4 has been implicated in several diseases, including cancer, where it may modulate the degradation of key regulatory proteins affecting cell proliferation and apoptosis. Additionally, OTUD4's unique substrate specificity and mechanism of action make it an attractive target for therapeutic intervention. Understanding the structure-function relationship of OTUD4 and its interactions with substrates and other cellular components is essential for elucidating its biological roles. Consequently, researchers have focused on the characterization of OTUD4 recombinant protein, utilizing techniques such as protein expression, purification, and enzymatic activity assays. These studies aim to provide insights into its functional mechanisms, thus paving the way for potential clinical applications in modulating ubiquitin signaling pathways in various diseases.
