Analytical Data
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基因名
RPL37
- Application
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别名
RPL37; 60S ribosomal protein L37; G1.16; Large ribosomal subunit protein eL37
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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
P61927
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表达区间
2-97 aa
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氨基酸序列
TKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS
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分子量
11.0 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
RPL37, a ribosomal protein belonging to the large ribosomal subunit, plays a crucial role in the assembly and function of ribosomes, the cellular machines responsible for protein synthesis. Recent studies have highlighted its significance in various cellular processes and its potential implications in diseases, particularly cancer. The reassembly and post-translational modifications of RPL37 are vital for maintaining ribosomal integrity and efficiency. Research has shown that aberrations in RPL37 expression or function can lead to disruptions in protein synthesis, affecting cell growth and proliferation. Furthermore, RPL37 has been implicated in the regulation of apoptosis and stress responses, indicating its broader role beyond ribosome biogenesis. Given its involvement in these critical processes, the characterization of recombinant RPL37 protein has garnered interest for understanding its structure-function relationships, enabling insights into ribosome assembly and the underlying mechanisms of diseases linked to ribosomal dysfunctions. Exploring the recombinant expression of RPL37 can facilitate therapeutic developments and provide a foundation for targeting ribosomal proteins as potential biomarkers or therapeutics in cancer treatment and beyond. Overall, understanding RPL37 through recombinant protein studies can unveil new avenues for biomedical research and therapeutic innovations.
