Analytical Data
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Gene name
UGPA
- Application
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Alternative Names
UGPA；UGP1；UTP--glucose-1-phosphate uridylyltransferase
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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
Q9SDX3
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Expression Region
1-467aa
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AA Sequence
MADAKIAKLQSAVAELNQISENEKSGFISLVSRYLSGEAEQIEWSKIQTPTDEVVVPYDTLSPPPEDLEATKKLLDKLAVLKLNGGLGTTMGCTGPKSVIEVRNGFTFLDLIVIQIESLNKKYGCNVPLLLMNSFNTHDDTQKIVEKYANSNIEIHTFNQSQYPRLVMEDFQPLPSKGHAGKDGWYPPGHGDVFPSLMNSGKLDALLSQGKEYVFIANSDNLGAIVDIKILNHLINNQNEYCMEVTPKTLADVKGGTLISYEGRVQLLEIAQVPDAHVNEFKSIEKFKIFNTNNLWVNLKAIKRLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDHAIGINVPRSRFLPVKATSDLLLVQSDLYMLVDGFVIRNKARTNPSNPSIELGPEFKKVANFLSRFKSIPSIVELDSLKVSGDVWFGEGVVLKGNVSIAAKSGVKLEISDGAVLENKVINGPEDI
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Molecular Weight
58.8 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
UGPA (urease-like glutamine protease A) is a distinctive protein that has garnered attention in the field of biochemistry and molecular biology due to its unique enzymatic properties and potential applications. Initially identified in certain prokaryotic organisms, UGPA is characterized by its ability to hydrolyze peptide bonds, drawing parallels to ureases in terms of structural features and catalytic mechanisms. This protein exhibits significant activity under specific environmental conditions, which has implications for understanding nitrogen metabolism in microbes and its evolutionary adaptations. Recent research has focused on the recombinant expression of UGPA in various host systems, leveraging molecular cloning and protein engineering techniques to produce large quantities of the protein for detailed biochemical studies. The recombinant UGPA is being examined for its stability, activity profile, and substrate specificity, with the aim to elucidate its role in microbial ecology and its potential utility in biotechnological applications, such as bioremediation, agricultural enhancement, and industrial enzyme production. Additionally, recombinant UGPA serves as a model for investigating the folding, stability, and function of urease-like proteins, contributing to a broader understanding of enzyme evolution and functional diversity. This ongoing research underscores the significance of UGPA as both a biological model and a valuable tool in various scientific fields.
