Analytical Data
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Gene name
ugd
- Application
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Alternative Names
ugd；UDP-glucuronic acid decarboxylase 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
O60701
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Expression Region
1-494aa
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AA Sequence
MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV
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Molecular Weight
71.0 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
UGD (UDP-glucose pyrophosphorylase) is an essential enzyme that plays a critical role in carbohydrate metabolism by catalyzing the conversion of UTP and glucose-1-phosphate into UDP-glucose and inorganic pyrophosphate. UDP-glucose serves as a precursor for various polysaccharides, glycoproteins, and nucleotide sugars, making UGD fundamental in biosynthetic pathways. Research on UGD has gained momentum due to its potential implications in agriculture, biotechnology, and medicine. For instance, manipulating UGD activity could enhance plant resistance to abiotic stress or improve biomass production. In the pharmaceutical domain, understanding UGD's structure and function can aid in developing drugs targeting metabolic disorders. Moreover, UGD from different organisms exhibits distinct characteristics, allowing for comparative studies that can reveal evolutionary insights and functional diversification. The advent of molecular cloning and recombinant DNA technology has facilitated the production of recombinant UGD proteins, enabling detailed biochemical characterization and the exploration of their enzymatic mechanisms. Additionally, synthetic biology approaches aim to engineer UGD pathways in microbial systems for the efficient production of value-added compounds. This growing body of research highlights the importance of UGD as a focal point in metagenomics and enzyme engineering, underlining its relevance in both fundamental biochemistry and applied sciences.
