Analytical Data
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基因名
MTR_4g091020
- Application
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别名
(Putative LysM domain-containing protein)
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种属
Medicago truncatula
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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
G7JRT6
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表达区间
26-87aa
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分子量
19.7 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
The study of the MTR_4g091020 recombinant protein is rooted in the ongoing exploration of microbial physiology and metabolic pathways, particularly in the context of environmental adaptations. MTR_4g091020, encoded by a gene in the *Methylophilus methylotrophus* genome, is hypothesized to play a crucial role in the organism’s ability to utilize methanol as a carbon source. Understanding this protein's structure and function can provide insights into how methylotrophic bacteria contribute to carbon cycling and potentially enhance biotechnological applications, such as biofuel production and bioremediation. Given the increasing interest in sustainable practices and the need for innovative solutions to environmental challenges, examining the MTR_4g091020 protein could reveal novel enzymatic functions or regulatory mechanisms that could be harnessed for industrial purposes. Recent advancements in recombinant DNA technology allow for the efficient production and characterization of this protein, facilitating its functional analysis. Investigations into MTR_4g091020 not only aim to delineate its biological role but also seek to assess its potential as a biocatalyst in synthetic biology applications. Therefore, the research on this protein could bridge fundamental microbial research and practical biotechnological advances, providing a deeper understanding of methylotrophy and its implications for ecological and industrial processes.












