Analytical Data
-
基因名
RPL28
- Application
-
别名
RPL28；Large ribosomal subunit Protein eL28
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P46779
-
表达区间
2-137aa
-
氨基酸序列
SAHLQWMVVRNCSSFLIKRNKQTYSTEPNNLKARNSFRYNGLIHRKTVGVEPAADGKGVVVVIKRRSGQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVMVKRKRTRPTKSS
-
分子量
42.6 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
RPL28, a critical component of the ribosomal subunit, plays a significant role in the assembly and function of the ribosome, the cellular machinery responsible for protein synthesis. Research into RPL28 often focuses on its involvement in ribosome biogenesis, as well as its importance in cellular growth and proliferation. Abnormalities in RPL28 expression or function have been implicated in various diseases, including cancer, where dysregulated protein synthesis is a hallmark. Additionally, RPL28 is subject to post-translational modifications that may influence its interaction with other ribosomal proteins and RNA, thereby affecting ribosome stability and translational accuracy. Recent studies have employed recombinant DNA technology to express and purify RPL28, allowing for detailed investigations into its structural properties and interactions with other ribosomal components. This research is essential not only for understanding the fundamental mechanisms of protein synthesis but also for exploring potential therapeutic interventions targeting ribosomal dysfunctions in diseases. Furthermore, advances in techniques such as cryo-electron microscopy have provided insights into the structural organization of ribosomes and the specific role of RPL28, offering new avenues for research in ribosomal biology and its implications for health and disease.
