Analytical Data
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基因名
LFNG
- Application
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别名
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8NES3
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表达区间
1-250aa
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分子量
55.2 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
LFNG (Lunatic Fringe) is a notable member of the Fringe family of glycosyltransferases, which play a critical role in the Notch signaling pathway, a fundamental mechanism for cell communication and differentiation in various biological processes, including embryogenesis and tissue homeostasis. The modification of Notch ligands by LFNG is essential for regulating the interaction between Notch receptors and their ligands, thus modulating cell fate decisions. Given its pivotal role in developmental biology and potential implications in diseases such as cancer, neurodegeneration, and other disorders influenced by aberrant Notch signaling, LFNG has garnered significant research interest. Studies have demonstrated that LFNG not only affects cell proliferation and differentiation but also participates in the regulation of stem cell populations and organ development. Moreover, understanding LFNG's structure and function is paramount for developing targeted therapies that can manipulate Notch signaling in various pathologies. Researchers have embarked on characterizing the recombinant LFNG protein to elucidate its enzymatic activity, substrate specificity, and overall impact on signaling pathways. Investigations into LFNG's crystal structure and its interaction with glycoproteins are crucial for designing small molecules or biologics that could selectively modulate LFNG's activity, presenting new avenues for therapeutic intervention in Notch-related diseases.












