Analytical Data
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基因名
munIM
- 应用
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别名
Adenine-specific methyltransferase MunI ;M.MunI
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种属
Mycoplasma sp
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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
P43641
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表达区间
1-233aa
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分子量
42.9 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
The study of munIM recombinant proteins is situated within the broader context of biotechnology and protein engineering, aiming to understand and harness the functional capabilities of microbial proteins. MunIM, derived from certain microorganisms, has garnered interest due to its potential applications in industrial processes, environmental bioremediation, and therapeutic development. The recombinant expression of munIM enables the production of large quantities of this protein, allowing researchers to investigate its structural properties, enzymatic activities, and interactions with other biomolecules. This research is particularly relevant in the field of enzyme design, where modifications to the munIM protein can enhance its stability, specificity, and efficiency under varying conditions. By elucidating the mechanisms by which munIM operates, scientists can pave the way for innovative solutions in areas such as biofuel production, waste management, and drug discovery. Overall, the exploration of munIM recombinant proteins not only contributes to fundamental biological knowledge but also holds promise for numerous practical applications that could address global challenges in health and sustainability.
