Analytical Data
-
Gene name
RRP15
- Application
-
Alternative Names
RRP15-like protein. Ribosomal RNA-processing protein 15
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y3B9
-
Expression Region
1-259 aa
-
AA Sequence
MKMVTGAVASVLEDEATDTSDSEGSCGSEKDHFYSDDDAIEADSEGDAEPCDKENENDGESSVGTNMGWADAMAKVLNKKTPESKPTILVKNKKLEKEKEKLKQERLEKIKQRDKRLEWEMMCRVKPDVVQDKETERNLQRIATRGVVQLFNAVQKHQKNVDEKVKEAGSSMRKRAKLISTVSKKDFISVLRGMDGSTNETASSRKKPKAKQTEVKSEEGPGWTILRDDFMMGASMKDWDKESDGPDDSRPESASDSDT
-
Molecular Weight
55.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
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.
-
Storage & Shelf Life
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.
-
Shipping
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
RRP15, or Ribosome Regulation Protein 15, is a member of the ribosome-associated protein family that plays a crucial role in the regulation of protein synthesis and ribosome function. Recent studies have highlighted its significance in cellular stress responses and the modulation of gene expression. Abnormalities in RRP15 have been linked to various diseases, including cancer and neurodegenerative disorders, underscoring the necessity for detailed exploration of its molecular mechanisms. The understanding of RRP15’s structural and functional characteristics can reveal insights into ribosome assembly and the translational control of mRNA, thereby elucidating fundamental processes in cellular biology. Ongoing research focuses on the development of recombinant RRP15 proteins to facilitate in vitro studies, allowing researchers to dissect its role in ribosome dynamics and its interactions with other ribosomal proteins and factors. This research not only aims to enrich the understanding of ribosome biology but also holds the potential to identify novel therapeutic targets for diseases associated with ribosomal dysfunction. As the landscape of molecular biology progresses, the exploration of RRP15 and analogous proteins could pave the way for innovative approaches in the treatment of ribosome-related pathologies, making it a pivotal point of interest in contemporary biomedical research.
