Analytical Data
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Gene name
ulp1
- Application
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Alternative Names
Ubiquitin-like-specific protease 1; ulp1; Schizosaccharomyces pombe (strain 972 / ATCC 24843); Fission yeast; Hydrolase; Protease; Thiol protease
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Species
Others
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O42957
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Expression Region
E344-Y568
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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
ULP1 (Ubiquitin-like protein 1) is a member of the ubiquitin-like protein family, primarily involved in post-translational modifications that play crucial roles in various cellular processes, including DNA repair, cell cycle regulation, and protein degradation. Given its significance, understanding ULP1's structure and function is vital for elucidating its role in cellular physiology and pathology. Researchers have identified ULP1 as a potential target for therapeutic intervention in diseases linked to dysfunctional ubiquitination processes, such as cancer and neurodegenerative disorders. The recombinant expression of ULP1 protein allows for detailed studies of its biochemical properties and interactions with other cellular components, paving the way for the development of novel biomolecular tools and potential drugs. Advances in protein engineering techniques have facilitated the production of ULP1 in various expression systems, enabling large-scale purification and functional analysis. This research not only enhances our understanding of ULP1’s biological functions but also opens avenues for exploring its applications in biotechnology and medicine. Ultimately, elucidating the mechanisms of ULP1 action may lead to innovative strategies for targeting specific diseases associated with ubiquitin-like pathways.
