Analytical Data
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Gene name
USP27X
- Application
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Alternative Names
USP22L; USP27
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Species
Human
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Source
Baculovirus
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A6NNY8
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Expression Region
C2-Y438
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Protein Length
Full Length
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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
USP27X is a deubiquitinating enzyme that has garnered attention in recent years due to its roles in various cellular processes, including protein stability, cell signaling, and the regulation of gene expression. The research surrounding USP27X is primarily motivated by its implications in cancer biology and other diseases associated with dysregulated protein ubiquitination. Ubiquitination is a crucial post-translational modification that can tag proteins for degradation or alter their function and activity. Investigations have revealed that USP27X can stabilize specific target proteins by removing ubiquitin molecules, thereby preventing their degradation. This mechanism is particularly significant in cancer, where the aberrant expression of USP27X has been linked to tumor progression and poor patient prognosis. Furthermore, USP27X has shown potential interactions with key oncogenic pathways, making it a candidate for therapeutic targeting. Understanding the precise molecular mechanisms of USP27X and its interactions could provide valuable insights into developing novel cancer therapies and contribute to a broader comprehension of ubiquitin-mediated regulation in health and disease. As research progresses, USP27X may emerge as a crucial player in the ubiquitin-proteasome system, influencing not only cancer biology but also various physiological processes.
