Analytical Data
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基因名
GNPNAT1
- Application
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别名
GNPNAT1;GNA1;Glucosamine 6-phosphate N-acetyltransferase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96EK6
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表达区间
1-184aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMGSMKPDETPMFDPSLLKEVDWSQNTATFS PAISPTHPGEGLVLRPLCTADLNRGFFKVLGQLTETGVVSPEQFMKSFEH MKKSGDYYVTVVEDVTLGQIVATATLIIEHKFIHSCAKRGRVEDVVVSDE CRGKQLGKLLLSTLTLLSKKLNCYKITLECLPQNVGFYKKFGYTVSEENY MCRRFLK
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分子量
23 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.
Quality inspection process
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Protein Description
GNPNAT1 (GlcNAc-1-phosphate transferase 1) is an enzyme that plays a critical role in glycosylation, specifically in the modification of proteins and lipids through the addition of N-acetylglucosamine (GlcNAc) moieties. This process is essential for various cellular functions, including protein stability, signaling, and cellular interactions. Recent studies have highlighted the importance of GNPNAT1 in the context of several diseases, particularly in neurodegenerative disorders and certain cancers, where aberrant glycosylation patterns are observed. Understanding the structure and function of GNPNAT1 is crucial for deciphering its biological significance and potential as a therapeutic target. Recombinant GNPNAT1 proteins have been produced to facilitate detailed biochemical studies, including enzyme kinetics, substrate specificity, and interactions with other glycosylation-related enzymes. These studies aim to elucidate the mechanistic pathways involving GNPNAT1 and its contribution to cellular homeostasis. Furthermore, the generation of antibodies against GNPNAT1 has enabled its localization and role in various biological contexts to be explored. The ongoing research into GNPNAT1 not only broadens our understanding of glycosylation but also opens avenues for developing novel diagnostic and therapeutic strategies for diseases associated with glycosylation abnormalities.












