Analytical Data
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基因名
relG
- Application
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别名
Putative endoribonuclease RelG
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种属
Mycobacterium tuberculosis
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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
O33348
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表达区间
1-87aa
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分子量
26.2 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
RelG, a protein from the Rel family, is a crucial element involved in the regulation of stress response and bacterial virulence. Research into RelG has gained momentum due to its role in mediating the stringent response, a survival mechanism activated under nutrient-limiting conditions. This response is critical for bacterial adaptation, allowing pathogens to persist in hostile environments and contribute to their persistence in infections. The unique structure and function of RelG, particularly in the synthesis of guanosine tetra- and pentaphosphate (p)ppGpp, have made it a target for exploration in antimicrobial drug development. Understanding the molecular mechanisms governing RelG's activity could provide insights into its potential as a therapeutic target. Moreover, the study of RelG's interactions with other cellular components is essential for elucidating its role in pathogenicity and resistance to antibiotics. Given the rising incidence of antibiotic-resistant bacteria, research into the RelG protein may yield novel strategies for combating bacterial infections by disrupting its function. Consequently, elucidating the properties and mechanisms of RelG is not only fundamental for microbiology but also holds significant implications for public health.
