Analytical Data
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基因名
rnj
- Application
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别名
rnj；Ribonuclease J
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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
P54123
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表达区间
1-640aa
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氨基酸序列
MAKNTQTQALKILPLGGLHEIGKNTCVFEYDDEILLLDAGLAFPTDDMHG VNVVLPDMTYLRENREKIKGMVVTHGHEDHIGGIAYHLKQFDIPIIYGPR LAMALLRDKLEEAGMLERTNLQTVSPREMVRLGKSFVVEFIRNTHSIADS YCLAIHTPLGVVMHSGDFKIDHTPIDGEFFDLQKVAEYGEKGVLCLLSDS TNAEVPGITPSEASVIPNLDRVFSQAEGRLMVTTFASSVHRVNIILSLAQ KHQRKVAVVGRSMLNVIAHARKLGYIKCPDNLFVPLKAARNLPDQQQLIL TTGSQGEPLAAMTRISNGEHPQIKIRQGDTVVFSANPIPGNTIAVVNTID RLMMQGANVIYGKHQGIHVSGHASQEEHKMLLALTRPKFFVPVHGEHRML VKHSQMAQAQGIPSENIVIVNNGDVIELTGDRIRVAGQVPSGIELVDQAG IVHESTMAERQQMAEDGLVTVAAALSKTGTLLAYPEVHCRGVVMTIQPKL LEELIVRTIENFLTERWSEFTHGSNGSTEVSWNALQKELESSLQRLIKRE LQSSPMVLLMLQTDTPIELDQVPQNVSTVSATSATPAPRKKVVLTKTPEP KVKAKPEKKVVTTAEPSAQPVSTTKVYRRSRKRSTTSVSS
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分子量
86 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 recombinant RNJ proteins has garnered significant interest in the fields of molecular biology and biotechnology due to their potential applications in various industries, including pharmaceuticals and agriculture. RNJ proteins, derived from diverse organisms, play essential roles in critical biological processes such as cell signaling, protein folding, and immune responses. The ability to engineer these proteins using recombinant DNA technology allows researchers to produce large quantities of pure proteins with specific modifications for experimental or therapeutic purposes. Moreover, understanding the structure-function relationships of RNJ proteins provides insights into their mechanisms of action, paving the way for the development of novel therapeutic agents and biotechnological innovations. Research efforts are increasingly focused on optimizing expression systems, improving purification techniques, and characterizing the biological activity of RNJ proteins. The advancement of high-throughput screening methods and structural biology techniques, such as X-ray crystallography and NMR spectroscopy, further enhances our understanding of these proteins. The potential for RNJ proteins in targeted drug delivery, vaccine development, and enzyme engineering underscores their importance in modern scientific research. As a result, the ongoing investigations into the properties and applications of recombinant RNJ proteins promise to contribute significantly to advancements in medicine, agriculture, and environmental sustainability.
