Analytical Data
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基因名
MGAT2
- Application
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别名
(Beta-1,2-N-acetylglucosaminyltransferase II)(GlcNAc-T II)(GNT-II)(Mannoside acetylglucosaminyltransferase 2)(N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II)
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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 & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q10469
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表达区间
30-447aa
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分子量
55.7 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
MGAT2, or Mono-1,4-mannosyl-glycoprotein 2-N-acetylglucosaminyltransferase, is an essential enzyme involved in the biosynthesis of complex N-glycans, playing a critical role in glycoprotein maturation. This enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to the mannose residue of glycoproteins, influencing their structural integrity and functional properties. Research on MGAT2 is driven by its significance in cellular processes, including protein folding, cell signaling, and immune response regulation. Aberrant glycosylation patterns due to MGAT2 dysregulation have been implicated in various diseases, including cancer, where altered glycan structures can affect tumor progression and metastasis. Additionally, the potential of MGAT2 as a therapeutic target has garnered attention, making the study of its recombinant protein increasingly important. By producing and analyzing MGAT2 recombinant proteins, researchers aim to elucidate the enzyme's activity, substrate specificity, and structural characteristics, ultimately seeking to develop strategies for modulating glycan synthesis in disease contexts. The exploration of MGAT2 not only enhances our understanding of glycosylation and its biological implications but also paves the way for innovative therapeutic interventions that could leverage glycan engineering to combat diseases associated with glycoprotein anomalies. This research holds promise for advancing both basic science and clinical applications in glycobiology and therapeutic development.












