Analytical Data
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Gene name
UDP
- Application
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Alternative Names
UDP；UGT2B11；UDP-glucuronosyltransferase 2B4
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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
P12758
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Expression Region
1-253aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSKSDVFHLGLTKNDLQGATLAIVPGDPDR VEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEE LAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPA VADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYDTYSGRVVRHF KGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPN AETMKQTESHAVKIVVEAARRLL
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Molecular Weight
29 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
UDP (Uridine Diphosphate) linked glycosylation is a vital process in the post-translational modification of proteins, significantly influencing their functionality and stability. The study of UDP-linked glycoproteins has garnered increasing attention due to their critical roles in various biological processes, including cell signaling, adhesion, and immune response. These glycoproteins are essential for maintaining cellular homeostasis and mediating intercellular communication. Moreover, aberrations in glycosylation patterns are implicated in numerous diseases, including cancer, neurodegenerative disorders, and infectious diseases. Understanding the structure and function of UDP-linked glycoproteins is crucial not only for elucidating fundamental biological mechanisms but also for developing therapeutic strategies. Recent advances in mass spectrometry and glycomic analysis have facilitated the detection and characterization of these complex molecules, enabling researchers to explore their roles in health and disease. As a result, the study of UDP-linked glycoproteins is a burgeoning field that holds promise for uncovering novel biomarkers and potential therapeutic targets. Through a combination of biochemical, structural, and computational approaches, ongoing research aims to unravel the intricacies of glycoprotein functionality and their contributions to physiological and pathological processes, paving the way for innovations in disease diagnosis and treatment.
