Analytical Data
-
Gene name
RPLP0
- Application
-
Alternative Names
RPLP0；Large ribosomal subunit Protein uL10
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P05388
-
Expression Region
2-317aa
-
AA Sequence
MASMTGGQQMGRGHHHHHHENLYFQGGEFPREDRATWKSNYFLKIIQLLD DYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENN PALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVT VPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEA TLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNV ASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADP SAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD
-
Molecular Weight
37 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
RPLP0, also known as ribosomal protein LPO or ribosomal protein P0, is a critical component of the ribosomal structure, playing an essential role in the assembly and function of the ribosome, the cellular machinery for protein synthesis. Research into RPLP0 has gained significance due to its involvement in various cellular processes and its implications in disease states, especially cancer. Alterations in ribosomal proteins, including RPLP0, can disrupt normal ribosome function, leading to aberrations in protein synthesis that are often associated with tumorigenesis. Additionally, RPLP0 is a member of a highly conserved family of proteins, underscoring its fundamental role in cellular biology across species. Investigations into RPLP0 reorganization and its interactions with other ribosomal proteins and translation factors can provide deeper insights into ribosome biogenesis and the regulatory mechanisms governing protein synthesis. Furthermore, understanding the molecular dynamics of RPLP0 may open new avenues for therapeutic interventions, particularly in targeting cancers that exhibit dysregulated ribosomal biogenesis. As ribosomal proteins often undergo complex post-translational modifications, characterizing these modifications in RPLP0 can elucidate their functional impacts on ribosome activity and cellular homeostasis. Thus, the study of RPLP0 not only enhances our understanding of fundamental biological processes but also holds promise for developing novel strategies in cancer treatment and other diseases linked to ribosomal dysfunction.
