Analytical Data
-
Gene name
rplF
- Application
-
Alternative Names
rplF;Large ribosomal subunit Protein uL6
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0AG55
-
Expression Region
2-175aa
-
AA Sequence
SRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGADKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAK
-
Molecular Weight
45.5 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
RplF, a critical protein component of the ribosomal subunit, plays an essential role in the translation process of protein synthesis in bacteria. As a part of the 50S ribosomal subunit, RplF is involved in the assembly and function of the ribosome, facilitating the interaction between ribosomal RNA and various proteins. Research on RplF has garnered significant attention due to its potential implications in antibiotic resistance, as many antibiotics target bacterial ribosomes to inhibit protein synthesis. Understanding the structure and function of RplF can provide insights into the mechanisms of ribosome assembly and the effects of ribosomal inhibitors. Furthermore, studies exploring the recombinant expression of RplF allow for the production of sufficient quantities of the protein for further biochemical and structural analyses. Through these investigations, researchers aim to elucidate the protein's role in ribosome biogenesis and its interactions with antibiotics, ultimately paving the way for developing novel therapeutic strategies against bacterial infections. This research is especially crucial in the context of rising antibiotic resistance, where enhancing our understanding of ribosomal components like RplF may lead to innovative approaches in combating resistant bacterial strains. Thus, the exploration of RplF not only contributes to fundamental molecular biology but also holds significant promise for applications in drug development and the fight against infectious diseases.











