Analytical Data
-
Gene name
rpmJ
- Application
-
Alternative Names
Ribosomal protein B
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0A7Q6
-
Expression Region
1-38aa
-
Molecular Weight
31.4 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
The study of recombinant proteins has gained significant traction in the field of molecular biology and biotechnology due to their potential applications in therapeutics, diagnostics, and industrial processes. Among these proteins, RPMJ (also known as RpmJ) is a ribosomal protein found in various bacteria, including pathogens of clinical relevance. Research into RPMJ has been prompted by its critical role in ribosome assembly and function, which are essential for protein synthesis. The significance of RPMJ extends beyond basic biology; it is also a promising target for antibiotic development, as inhibiting its function could potentially disrupt bacterial growth. Recent advancements in genetic engineering techniques have made it possible to produce RPMJ as a recombinant protein, allowing researchers to study its structure and function in detail. This research not only enhances our understanding of ribosomal dynamics but also opens new avenues for developing innovative antibiotic strategies against antibiotic-resistant bacteria. Furthermore, the production of recombinant RPMJ enables the exploration of its interactions with other cellular components, shedding light on its broader biological roles. Ultimately, the study of RPMJ and its recombinant form is integral to advancing our knowledge of protein synthesis machinery and developing novel therapeutic approaches in the fight against bacterial infections.
