Analytical Data
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Gene name
USP47
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简介
The USP47 protein is a ubiquitin-specific protease that deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizes POLB, and regulates base excision repair (BER). In addition to DNA repair, USP47 is an important regulator of cell growth and genome integrity. USP47 Protein, Human (sf9, His, FLAG) is the recombinant human-derived USP47 protein, expressed by sf9 insect cells , with C-Flag, N-8*His labeled tag.
- Application
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Alternative Names
USP47; Ubiquitin carboxyl-terminal hydrolase 47; Deubiquitinating enzyme 47; Ubiquitin thioesterase 47; Ubiquitin-specific-processing protease 47
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Species
Human
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Source
Baculovirus
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Tag
C-Flag;N-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96K76
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Expression Region
V2-D1375
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Protein Length
Partial
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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
USP47, a member of the ubiquitin-specific protease (USP) family, plays a crucial role in the regulation of various cellular processes by deubiquitinating target proteins and modulating their stability and function. This enzyme is particularly significant in the context of cancer biology and immune response, as it can influence key signaling pathways and cellular survival mechanisms by removing ubiquitin moieties from critical regulatory proteins. Recent studies have highlighted USP47's involvement in maintaining cellular homeostasis and its potential as a therapeutic target for diseases characterized by dysregulated ubiquitination. The investigation of USP47's structure and function offers insights into its specific substrate interactions and the molecular mechanisms underlying its enzymatic activity. Developing recombinant USP47 protein allows for detailed biochemical studies to elucidate its functional role, substrate specificity, and regulatory mechanisms. Additionally, the therapeutic potential of targeting USP47 in drugs aimed at restoring normal cellular functions or combating malignancies is an emerging area of interest, prompting ongoing research to explore its pharmacological implications. Understanding USP47's biology not only enhances our knowledge of cellular regulation but may also pave the way for novel therapeutic interventions in cancer and other ubiquitination-related diseases.
