Analytical Data
-
Gene name
rpmB
- Application
-
Alternative Names
rpmB; b3637; JW3612; 50S ribosomal protein L28; Large ribosomal subunit protein bL28
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0A7M2
-
Expression Region
2-78aa
-
Molecular Weight
35.9 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
RPMB is a recombinant protein derived from Rhodopseudomonas palustris, a photosynthetic bacterium known for its metabolic versatility. The research on RPMB is primarily motivated by its potential applications in biotechnology and industrial processes. Due to its unique enzymatic properties, RPMB can play a crucial role in bioenergy production, particularly in the conversion of organic materials into renewable energy sources like biofuels. Additionally, RPMB has garnered attention for its possible involvement in microbial interactions and environmental bioremediation, helping to mitigate pollutants through bioconversion processes. Understanding the structure-function relationship of RPMB can lead to the development of engineered proteins with enhanced stability and activity, making it a valuable target for genetic and protein engineering studies. Furthermore, the insights gained from RPMB research can contribute to advancements in synthetic biology, allowing for the creation of more efficient microbial systems for various applications. Hence, the investigation of RPMB not only provides fundamental knowledge about microbial physiology but also presents opportunities for innovation in sustainable technologies.
