Analytical Data
-
Gene name
relG
- Application
-
Alternative Names
relG；relE2；Toxin RelG
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O33348
-
Expression Region
1-87aa
-
AA Sequence
MPYTVRFTTTARRDLHKLPPRILAAVVEFAFGDLSREPLRVGKPLRRELAGTFSARRGTYRLLYRIDDEHTTVVILRVDHRADIYRR
-
Molecular Weight
26.2 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
RelG is a crucial protein associated with various biological processes, particularly in the context of bacterial stress responses and the regulation of gene expression. It is a member of the RelA/SpoT homolog (RSH) family, which plays a significant role in the synthesis and degradation of the signaling molecule guanosine tetraphosphate (ppGpp). This molecule is pivotal in the stringent response, enabling bacteria to adapt to nutrient deprivation and environmental stress by modulating metabolic processes and promoting survival. The study of RelG is particularly important in understanding bacterial resilience, pathogenesis, and the development of antimicrobial strategies, as it influences bacterial growth and survival under adverse conditions. Furthermore, its dual function in both nucleotide synthesis and degradation presents an intriguing target for pharmaceutical intervention. Investigating the structure, function, and regulatory mechanisms of RelG can provide valuable insights into bacterial physiology and contribute to the design of novel antibiotics that disrupt bacterial stress response pathways. As such, research on RelG and its associated pathways is not only significant for microbiology but also for broader applications in medicine and biotechnology, illustrating the interplay between protein function and health outcomes in both microbial and human systems.
