Analytical Data
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Gene name
UPP1
- Application
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Alternative Names
UPP1;UP;Uridine phosphorylase 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16831
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Expression Region
1-310aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAATGANAEK AESHNDCPVR LLNPNIAKMK EDILYHFNLT TSRHNFPALF GDVKFVCVGG SPSRMKAFIR CVGAELGLDC PGRDYPNICA GTDRYAMYKV GPVLSVSHGM GIPSISIMLH ELIKLLYYAR CSNVTIIRIG TSGGIGLEPG TVVITEQAVD TCFKAEFEQI VLGKRVIRKT DLNKKLVQEL LLCSAELSEF TTVVGNTMCT LDFYEGQGRL DGALCSYTEK DKQAYLEAAY AAGVRNIEME SSVFAAMCSA CGLQAAVVCV TLLNRLEGDQ ISSPRNVLSE YQQRPQRLVS YFIKKKLSKA
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Molecular Weight
36 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
Related Products
Protein Description
UPP1, or Ubiquitin-specific protease 1, is a vital enzyme involved in regulating protein degradation and cellular homeostasis through the ubiquitin-proteasome pathway. This pathway plays a crucial role in a variety of cellular processes, including cell cycle regulation, signal transduction, and the response to stress. Research has shown that UPP1 is implicated in various diseases, particularly cancer and neurodegenerative disorders, where its dysregulation can lead to the accumulation of misfolded proteins or damaged cellular components. As a result, UPP1 has gained attention as a potential therapeutic target; understanding its structure and function could provide insights into developing novel interventions for related pathologies. Recent advances in recombinant protein technology have enabled the production and purification of UPP1, facilitating biochemical assays and structural studies. By elucidating the enzyme’s mechanism of action and its interactions with substrates and inhibitors, researchers aim to uncover the therapeutic potential of modulating UPP1 activity. This area of study not only contributes to basic biological knowledge but also holds promise for innovative treatments that harness the ubiquitin-proteasome system's regulatory capabilities.











