Analytical Data
-
Gene name
eutC
- Application
-
Alternative Names
Ethanolamine ammonia-lyase small subunit
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P19636
-
Expression Region
1-295aa
-
Molecular Weight
35.8 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
EutC is a crucial enzyme involved in the ethanolamine utilization (Eut) pathway, which enables certain bacteria to utilize ethanolamine as a nitrogen and carbon source. This pathway plays an essential role in the metabolism of microbial communities, influencing their survival and adaptability in various environments, such as the gastrointestinal tract of mammals. The study of recombinant EutC protein is significant for understanding its biochemical properties, enzyme kinetics, and structural characteristics. By employing molecular cloning and expression techniques, researchers can produce EutC in heterologous systems, enabling comprehensive analyses of its functionality. The insights gained from these studies are vital for unraveling the mechanisms of microbial metabolism and can have broader implications in fields like biotechnology, where microbial systems are harnessed for bioremediation or biofuel production. Furthermore, investigating the role of EutC in microbial interactions can shed light on its potential impact on host-microbe relationships, particularly in health and disease contexts. Overall, the exploration of recombinant EutC protein holds promise for advancing our understanding of microbial ecology and its applications.
