Analytical Data
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基因名
MG
- Application
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别名
MG；AAG；ANPG；MID1；DNA-3-methyladenine glycosylase
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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
P29372
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表达区间
1-298aa
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氨基酸序列
MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSD AAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLAR AFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMF MKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTL RKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLE PSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQALE HHHHHH
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分子量
34 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
MG (Maltose-binding protein) fusion proteins have gained significant attention in molecular biology and biotechnology due to their ability to enhance the solubility and stability of recombinant proteins. Initially derived from the Escherichia coli maltose operon, MG acts as a ligand for maltose, facilitating the purification of target proteins through affinity chromatography. The use of MG as a fusion partner can dramatically improve the yield of functional proteins that might otherwise be insoluble or misfolded when expressed in bacterial systems. Furthermore, MG fusion proteins can be employed in various applications, including structural studies, enzymatic assays, and the development of targeted therapeutics. Research into MG has evolved to explore its role not only as a purification tag but also as a tool for protein characterization and stabilization. Studies have indicated that the incorporation of MG can impact the biological activity and folding kinetics of fused proteins, leading to insights into protein-protein interactions and functional mechanisms at the molecular level. As recombinant protein technologies advance, MG remains a pivotal component in overcoming challenges associated with protein expression, purification, and characterization, contributing to our understanding of complex biological processes and the development of biopharmaceuticals.
