Analytical Data
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基因名
rsrIM
- Application
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别名
rsrIM；Type II methyltransferase M.RsrI
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种属
E.coli
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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
P14751
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表达区间
1-319aa
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氨基酸序列
MANRSHHNAGHRAMNALRKSGQKHSSESQLGSSEIGTTRHVYDVCDCLDTLAKLPDDSVQLIICDPPYNIMLADWDDHMDYIGWAKRWLAEAERVLSPTGSIAIFGGLQYQGEAGSGDLISIISHMRQNSKMLLANLIIWNYPNGMSAQRFFANRHEEIAWFAKTKKYFFDLDAVREPYDEETKAAYMKDKRLNPESVEKGRNPTNVWRMSRLNGNSLERVGHPTQKPAAVIERLVRALSHPGSTVLDFFAGSGVTARVAIQEGRNSICTDAAPVFKEYYQKQLTFLQDDGLIDKARSYEIVEGAANFGAALQRGDVAS
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分子量
51.7 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
Resurrection proteins, particularly the RSRIM (Resurrection Protein Interacting Molecule), are key to understanding the mechanisms of desiccation tolerance in organisms, particularly in extremophiles and certain plants. These proteins play a crucial role in protecting cellular structures and macromolecules during periods of extreme drought or environmental stress. Research into RSRIM has gained momentum as scientists explore its potential applications in biotechnology, agriculture, and medicine. By studying the molecular interactions and stability of RSRIM, researchers aim to uncover how these proteins contribute to desiccation tolerance at the cellular level. This understanding could lead to advancements in developing crops that can withstand climate change-induced droughts, enhancing food security. Furthermore, investigating RSRIM's functionalities may provide insights into preserving biomolecules in pharmaceuticals, leading to improved shelf-life and stability of sensitive biologics. Overall, the study of RSRIM represents a significant intersection of plant biology, environmental science, and applied biotechnology, offering promising avenues for future research and practical applications.
