Analytical Data
-
Gene name
ssuE
- Application
-
Alternative Names
(NADPH)(FMN reductase)(Sulfate starvation-induced protein 4)(SSI4)
-
Species
Escherichia coli
-
Source
Baculovirus
-
Tag
C- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P80644
-
Expression Region
1-191aa
-
Molecular Weight
26.9 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
ssuE, a gene coding for the ssuE protein, has garnered research interest due to its pivotal role in sulfur metabolism within various microorganisms. This protein is part of the sulfate assimilation pathway, which is crucial for organisms that rely on sulfate as a sulfur source. Understanding the function and regulation of ssuE can shed light on the complex biochemical processes that enable these organisms to thrive in sulfur-limited environments. The significance of ssuE extends beyond microbial ecology; it is also relevant in biotechnological applications, such as bioleaching and bioremediation, where sulfur compounds play a critical role. Recent studies have aimed to characterize the biochemical properties of the ssuE protein, including its enzymatic activity, structural features, and interactions with other cellular components. By utilizing advanced techniques such as recombinant protein expression and purification, researchers have begun to elucidate the detailed mechanisms by which ssuE functions in sulfur assimilation. This research not only enhances our understanding of microbial physiology but also has implications for environmental sciences and industrial biotechnology, where optimizing sulfur-related processes can lead to more sustainable practices. Thus, the study of ssuE and its recombinant protein forms represents a promising avenue for both basic and applied research in microbiology and biochemistry.











