关键信息
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基因名
OGT
- 应用
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别名
O-GlcNAc transferase subunit p110O-linked N-acetylglucosamine transferase 110KDA subunit ;OGT
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O15294
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表达区间
606-1022aa
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分子量
62.5 kDa
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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.
质检流程
相关产品
背景信息
OGT (O-GlcNAc transferase) is an essential enzyme that plays a critical role in the post-translational modification of proteins through the addition of O-Linked N-Acetylglucosamine (O-GlcNAc) residues. This modification is significant in cellular signaling, metabolism, and stress response, influencing various biological processes such as gene expression and cell differentiation. The dysregulation of OGT has been implicated in numerous diseases, including cancer, diabetes, and neurodegenerative disorders. Therefore, understanding the structure and function of OGT, as well as the mechanisms underlying its enzymatic activity, is crucial for developing potential therapeutic strategies. Recent advances in techniques such as X-ray crystallography and mass spectrometry have enhanced our ability to study OGT and its interactions with substrates and other cellular factors. Furthermore, the development of specific inhibitors and modulators of OGT is a promising area of research, which could pave the way for novel interventions in OGT-related diseases. Increasing evidence suggests that OGT's role as a molecular sensor linking nutrient availability to protein function is fundamental in maintaining cellular homeostasis, underlining the importance of continued investigation into this multifaceted enzyme.
