Analytical Data
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基因名
UGGT2
- Application
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别名
HUGT2; UGCGL2; UGT2; UDP-glucose ceramide glucosyltransferase-like 1
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种属
Human
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表达系统
E. coli
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标签
Two N- s, His- & SUMO-
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9NYU1
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表达区间
His1221~Arg1408
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分子量
29kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
UGGT2 (UDP-glucose: glycoprotein glucosyltransferase 2) is an essential enzyme involved in the quality control of glycoprotein folding in the endoplasmic reticulum (ER). It plays a critical role in the glycoprotein maturation process by transferring glucose residues to improperly folded glycoproteins, which serves as a signal for their retention in the ER and eventual refolding or degradation through the ER-associated degradation (ERAD) pathway. The study of UGGT2 is particularly relevant given the increasing recognition of the importance of glycosylation in protein function and its implications in various diseases, including cancer and neurodegenerative disorders. Researchers have also shown that UGGT2 is involved in the viral life cycle of several pathogens, affecting their virulence and host immune responses, which highlights its potential as a therapeutic target. With advancements in recombinant DNA technology, scientists are now able to produce UGGT2 as a recombinant protein for structural and functional analyses. This allows for a deeper understanding of its enzymatic mechanisms, substrate specificities, and interactions with other cellular components. The ongoing research into UGGT2 not only enhances our comprehension of protein folding and modification but also paves the way for the development of novel strategies aimed at modulating glycoprotein functions for therapeutic interventions.












