Analytical Data
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Gene name
UGT78D1
- Application
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Alternative Names
UGT78D1；Flavonol-3-O-rhamnosyltransferase
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Species
E.coli
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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
Q9S9P6
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Expression Region
1-453aa
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AA Sequence
MTKFSEPIRDSHVAVLAFFPVGAHAGPLLAVTRRLAAASPSTIFSFFNTARSNASLFSSDHPENIKVHDVSDGVPEGTMLGNPLEMVELFLEAAPRIFRSEIAAAEIEVGKKVTCMLTDAFFWFAADIAAELNATWVAFWAGGANSLCAHLYTDLIRETIGLKDVSMEETLGFIPGMENYRVKDIPEEVVFEDLDSVFPKALYQMSLALPRASAVFISSFEELEPTLNYNLRSKLKRFLNIAPLTLLSSTSEKEMRDPHGCFAWMGKRSAASVAYISFGTVMEPPPEELVAIAQGLESSKVPFVWSLKEKNMVHLPKGFLDRTREQGIVVPWAPQVELLKHEAMGVNVTHCGWNSVLESVSAGVPMIGRPILADNRLNGRAVEVVWKVGVMMDNGVFTKEGFEKCLNDVFVHDDGKTMKANAKKLKEKLQEDFSMKGSSLENFKILLDEIVKV
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Molecular Weight
55.6 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
Related Products
Protein Description
UGT78D1, a member of the UDP-glucuronosyltransferase (UGT) enzyme family, plays a crucial role in the glucuronidation process, which involves the conjugation of endogenous and exogenous compounds with glucuronic acid. This enzymatic reaction is essential for the metabolism and detoxification of various substances, including drugs, bile acids, and bilirubin. Research on UGT78D1 has gained significant attention due to its potential implications in pharmacogenomics, where genetic variations in UGT enzymes can influence drug response and toxicity. Furthermore, UGT78D1 is involved in the metabolism of flavonoids and phytohormones, impacting plant growth and development. Understanding the structural and functional characteristics of UGT78D1 through recombinant protein studies can provide insights into its substrate specificity and regulatory mechanisms. Additionally, elucidating the biochemical pathways involving UGT78D1 may pave the way for the development of therapeutic strategies aimed at enhancing drug efficacy and minimizing adverse effects. As such, the recombinant expression and characterization of UGT78D1 is not only vital for expanding our knowledge of metabolic processes but also for advancing applications in pharmaceutical and agricultural biotechnology.
