Analytical Data
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Gene name
UST2
- Application
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Alternative Names
UST2；Cytochrome c oxidase subunit 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
P00401
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Expression Region
1-534aa
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AA Sequence
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMHKLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFGHPEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIHGGSIRLATPMLYAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLNYNEKLAQIQFWLIFIGANVIFFPMHFLGINGMPRRIPDYPDAFAGWNYVASIGSFIATLSLFLFIYILYDQLVNGLNNKVNNKSVIYNKAPDFVESNTIFNLNTVKSSSIEFLLTSPPAVHSFNTPAVQS
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Molecular Weight
58.7 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
UST2, a member of the Ubiquitin-Specific Protease (USP) family, has garnered significant attention in recent years due to its crucial role in regulating cellular processes through deubiquitination. Ubiquitination is a post-translational modification that affects protein stability, localization, and activity, thus playing a pivotal role in various cellular functions including cell cycle regulation, DNA repair, and signal transduction. Abnormalities in deubiquitination processes mediated by USPs, including UST2, have been implicated in several diseases, particularly cancer. Research has shown that UST2 can influence the stability of key oncogenic and tumor suppressor proteins, making it a potential target for therapeutic intervention. Furthermore, the understanding of UST2's structural characteristics and its interaction with substrates opens new avenues for drug discovery. The focus on UST2 recombinant protein studies aims to elucidate its biological functions, regulatory mechanisms, and interactions with ubiquitin and target substrates. Such insights are vital for developing strategies that can modulate its activity for therapeutic purposes, ultimately contributing to more effective treatments for diseases associated with dysfunctional protein ubiquitination.
