Analytical Data
-
Gene name
rpsF
- Application
-
Alternative Names
rpsF; b4200; JW4158; 30S ribosomal protein S6; Small ribosomal subunit protein bS6) [Cleaved into: 30S ribosomal protein S6; fully modified isoform; 30S ribosomal protein S6; non-modified isoform]
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P02358
-
Expression Region
1-131aa
-
Molecular Weight
42.2 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
RpsF is a crucial component of the ribosomal protein family, specifically known as protein S6 in bacteria, playing a vital role in protein synthesis and ribosome assembly. Research into the recombinant form of RpsF has gained significance due to its essential function in maintaining ribosomal stability and facilitating translation processes in prokaryotes. Investigating RpsF's structure and function can provide insights into the ribosomal machinery, aiding in the development of new antibiotics targeting bacterial ribosomes, which is increasingly important in the context of rising antibiotic resistance. Additionally, understanding the interactions between RpsF and ribosomal RNA may elucidate the mechanisms of ribosome biogenesis and regulation, opening pathways for genetic engineering applications and synthetic biology. Given its importance, the recombinant expression of RpsF in model systems allows for detailed biophysical and biochemical characterization, providing a basis for potential therapeutic strategies and biotechnological innovations. Consequently, RpsF serves as a critical model for studying ribosomal function and offers promising avenues for research in microbiology and medicinal chemistry.
