Analytical Data
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Gene name
USP11
- Application
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Alternative Names
Deubiquitinating enzyme 11; Ubiquitin carboxyl-terminal hydrolase 11; Ubiquitin carboxyl-terminal hydrolase X linked; ubiquitin specific peptidase 11; Ubiquitin specific protease 11; Ubiquitin thiolesterase 11; Ubiquitin-specific-processing protease 11; UBP11_HUMAN; UHX1; USP11
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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
P51784
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Expression Region
201-300 aa
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AA Sequence
LVRHNDLGKSHTVQFSHTDSIGLVLRTARERFLVEPQEDTRLWAKNSEGSLDRLYDTHITVLDAALETGQLIIMETRKKDGTWPSAQLHVMNNNMSEEDE
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Molecular Weight
36.74 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
USP11 (Ubiquitin-specific protease 11) is a member of the deubiquitinating enzyme family, which plays a crucial role in the regulation of protein degradation and signaling pathways through the removal of ubiquitin moieties from target proteins. Understanding the functional implications of USP11 is particularly important given its involvement in various cellular processes, including cell cycle regulation, DNA repair, and responses to stress. Recent studies have highlighted its potential role in cancer biology, suggesting that USP11 may contribute to tumorigenesis by regulating the stability of oncogenic proteins and influencing apoptosis. The interest in USP11 extends to its potential as a therapeutic target, prompting research into its molecular mechanisms and interactions with substrates. The production and study of recombinant USP11 protein are essential for elucidating its biochemical properties, substrate specificity, and functional roles within the cell. By generating purified USP11 through recombinant DNA technology, researchers can conduct in vitro assays to explore its enzymatic activity and investigate how it modulates various cellular pathways. This research not only enhances our understanding of USP11's biological significance but also opens avenues for developing novel therapeutic strategies aimed at targeting the dysregulation of ubiquitin-proteasome systems in diseases such as cancer.
