Analytical Data
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Gene name
UBA3
- Application
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Alternative Names
UBA3；UBE1C；NEDD8-activating enzyme E1 catalytic subunit
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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
Q8TBC4
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Expression Region
1-463aa
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AA Sequence
MADGEEPEKKRRRIEELLAEKMAVDGGCGDTGDWEGRWNHVKKFLERSGP FTHPDFEPSTESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVID MDTIDVSNLNRQFLFRPKDIGRPKAEVAAEFLNDRVPNCNVVPHFNKIQD FNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSSIVPLID GGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEHCI EYVRMLQWPKEQPFGEGVPLDGDDPEHIQWIFQKSLERASQYNIRGVTYR LTQGVVKRIIPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDG LYTYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSP AITATLEGKNRTLYLQSVTSIEERTRPNLSKTLKELGLVDGQELAVADVT TPQTVLFKLHFTS
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Molecular Weight
73 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
UBA3 is a key enzyme involved in the ubiquitin-proteasome system, which plays a critical role in protein degradation and regulation within cells. As a member of the E1 enzyme family, UBA3 activates ubiquitin and transfers it to E2 conjugating enzymes, thus initiating the ubiquitination process that tags proteins for proteolytic degradation. Research into UBA3 has gained momentum due to its implications in various cellular processes, including cell cycle regulation, DNA repair, and apoptosis. Abnormalities in ubiquitination pathways have been linked to multiple diseases, including cancer, neurodegenerative disorders, and immune dysfunctions. Consequently, understanding the structure and function of the UBA3 protein could provide insights into its role in these conditions and contribute to the development of innovative therapeutic strategies. Recent studies have focused on characterizing UBA3's enzymatic activity, identifying its substrates, and elucidating its interaction with other components of the ubiquitin pathway. Investigating UBA3’s potential as a drug target is of particular interest, as modulation of its activity could offer novel approaches to treat diseases associated with proteostasis imbalance. Overall, the research surrounding UBA3 recombinant protein aims to unravel the complexities of ubiquitination and its broader implications in cellular health and disease.
