Analytical Data
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Gene name
USP2
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简介
USP2 catalytic domain proteins act as hydrolases and target polyubiquitinated proteins such as MDM2, MDM4, and CCND1. Both isoform 1 and isoform 4 exhibit ubiquitin-specific peptidase and isopeptidase activities. USP2 Protein, Human is the recombinant human-derived USP2 protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
USP2; Ubiquitin carboxyl-terminal hydrolase 2; 41 kDa ubiquitin-specific protease; Deubiquitinating enzyme 2; Ubiquitin thioesterase 2; Ubiquitin-specific-processing protease 2
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Species
Human
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Source
E. coli
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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
O75604
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Expression Region
N259-M605
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Protein Length
Partial
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Molecular Weight
40 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
USP2 (Ubiquitin-Specific Protease 2) is a deubiquitinating enzyme that plays a crucial role in the regulation of ubiquitination, a post-translational modification that affects protein stability, localization, and function. The study of USP2 is particularly significant in the context of various diseases, including cancer, where aberrant ubiquitination can lead to the misregulation of oncogenic and tumor suppressor proteins. USP2 has been shown to specifically deubiquitinate several substrates, including the tumor suppressor p53 and the androgen receptor, which are vital for cell proliferation and apoptosis. The overexpression of USP2 has been linked to increased cancer cell survival and resistance to therapies, making it an attractive target for therapeutic intervention. Additionally, understanding the structural and functional dynamics of USP2 is essential for developing inhibitors that can selectively modulate its activity. Research into recombinant USP2 proteins aims to elucidate their biochemical properties, substrate specificity, and regulatory mechanisms, contributing to a deeper understanding of cell signaling pathways and the development of novel cancer therapeutics. By producing and characterizing recombinant USP2, scientists hope to explore its roles in cellular processes and its potential as a biomarker or therapeutic target in oncology.
