Analytical Data
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Gene name
UTE
- Application
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Alternative Names
UTE；HUT11；JK；RACH1；Urea transporter 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
Q13336
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Expression Region
1-389aa
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AA Sequence
MEDSPTMVRVDSPTMVRGENQVSPCQGRRCFPKALGYVTGDMKELANQLKDKPVVLQFIDWILRGISQVVFVNNPVSGILILVGLLVQNPWWALTGWLGTVVSTLMALLLSQDRSLIASGLYGYNATLVGVLMAVFSDKGDYFWWLLLPVCAMSMTCPIFSSALNSMLSKWDLPVFTLPFNMALSMYLSATGHYNPFFPAKLVIPITTAPNISWSDLSALELLKSIPVGVGQIYGCDNPWTGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLWGFNSSLACIAMGGMFMALTWQTHLLALGCALFTAYLGVGMANFMAEVGLPACTWPFCLATLLFLIMTTKNSNIYKMPLSKVTYPEENRIFYLQAKKRMVESPL
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Molecular Weight
42.5 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
UTE (ubiquitin-like tandem of E2) proteins are a fascinating area of research due to their crucial roles in various cellular processes, including protein degradation, cell cycle regulation, and stress responses. Found in diverse organisms, these proteins are part of the ubiquitin-proteasome system, which is essential for maintaining cellular homeostasis by controlling protein turnover and signaling pathways. UTE proteins function by forming protein complexes through their unique UTE domain, facilitating the ubiquitination of target proteins, which marks them for degradation. The dysregulation of UTE proteins has been implicated in numerous diseases, including cancer and neurodegenerative disorders, highlighting their potential as therapeutic targets. Recent advancements in structural biology and molecular techniques have enabled researchers to elucidate the mechanisms by which UTE proteins exert their functions, paving the way for the development of innovative treatments that could modulate these pathways. Understanding the structural and functional dynamics of UTE proteins is therefore vital for advancing our knowledge of cellular regulation and developing new strategies in disease management.
