Analytical Data
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Gene name
USP11
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简介
The USP11 protein is a multifunctional protease that selectively removes ubiquitin from target proteins and polyubiquitin chains, thereby hindering their proteasomal degradation. It shows a preference for “Lys-6” and “Lys-63” linked ubiquitin chains and less activity towards other linkages. USP11 Protein, Human (sf9) is the recombinant human-derived USP11 protein, expressed by sf9 insect cells , with tag free.
- Application
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Alternative Names
USP11; Ubiquitin carboxyl-terminal hydrolase 11; Deubiquitinating enzyme 11; Ubiquitin thioesterase 11; Ubiquitin-specific-processing protease 11
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Species
Human
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Source
Baculovirus
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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
P51784
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Expression Region
A2-N963
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Protein Length
Partial
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Molecular Weight
109.8 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
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Protein Description
USP11, a member of the ubiquitin-specific protease family, plays a crucial role in the regulation of protein degradation and cellular processes through its deubiquitinating activity. As a vital component of the ubiquitin-proteasome system, USP11 is implicated in various physiological and pathological contexts, including cell cycle regulation, DNA damage response, and immune signaling. Recent studies have indicated that USP11 may impact oncogenesis and tumor progression by modulating key signaling pathways and cellular stress responses, which highlights its potential as a therapeutic target in cancer treatment. Given its importance, the study of USP11 recombinantly expressed proteins has gained traction, enabling researchers to elucidate the mechanisms underlying its function and interactions with other cellular factors. By applying advanced techniques such as structural biology and biochemistry, investigations into the enzymatic properties and substrate specificity of USP11 can facilitate the development of small-molecule inhibitors or modulators that selectively target its activity, thereby providing novel strategies for cancer therapy and other diseases associated with dysregulated ubiquitination. The exploration of USP11's role in diverse biological processes not only enhances our understanding of cellular homeostasis but also holds promise for therapeutic interventions aimed at correcting the imbalances caused by aberrant ubiquitin signaling.
