Analytical Data
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Gene name
UGT88A1
- Application
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Alternative Names
UGT88A1；UDP-glycosyltransferase 88A1
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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
Q9LK73
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Expression Region
1-462aa
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AA Sequence
MGEEAIVLYPAPPIGHLVSMVELGKTILSKNPSLSIHIILVPPPYQPESTATYISSVSSSFPSITFHHLPAVTPYSSSSTSRHHHESLLLEILCFSNPSVHRTLFSLSRNFNVRAMIIDFFCTAVLDITADFTFPVYFFYTSGAACLAFSFYLPTIDETTPGKNLKDIPTVHIPGVPPMKGSDMPKAVLERDDEVYDVFIMFGKQLSKSSGIIINTFDALENRAIKAITEELCFRNIYPIGPLIVNGRIEDRNDNKAVSCLNWLDSQPEKSVVFLCFGSLGLFSKEQVIEIAVGLEKSGQRFLWVVRNPPELEKTELDLKSLLPEGFLSRTEDKGMVVKSWAPQVPVLNHKAVGGFVTHCGWNSILEAVCAGVPMVAWPLYAEQRFNRVMIVDEIKIAISMNESETGFVSSTEVEKRVQEIIGECPVRERTMAMKNAAELALTETGSSHTALTTLLQSWSPK
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Molecular Weight
58.6 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
The UGT88A1 protein, a member of the UDP-glucuronosyltransferase (UGT) family, plays a crucial role in the glucuronidation process, which is a key mechanism in the metabolism and detoxification of various endogenous and exogenous compounds. This enzyme is predominantly expressed in the Arabidopsis thaliana species, where it is involved in the regulation of plant hormones and secondary metabolites. Research surrounding UGT88A1 has garnered interest due to its potential implications in improving plant resilience to stress conditions, enhancing growth, and influencing phytochemical production. A deeper understanding of UGT88A1 could lead to advancements in agricultural biotechnology, enabling the development of crop varieties with improved stress tolerance and resource use efficiency. Moreover, insights into the enzymatic pathways mediated by UGT88A1 could facilitate the engineering of plants for increased production of valuable secondary metabolites, benefiting pharmaceutical and cosmetic industries. As such, studies focusing on the functional characterization of UGT88A1 and its recombinant expression are essential to uncover the molecular mechanisms by which this enzyme operates, paving the way for its practical applications in both agronomy and biotechnology.
