Analytical Data
-
Gene name
entD
- Application
-
Alternative Names
SED
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P20723
-
Expression Region
26-258aa
-
Molecular Weight
42.9 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
The entD gene, part of the bacteriophage-encoded gene clusters, plays a crucial role in the biosynthesis of enterobactin, a siderophore produced by many Enterobacteriaceae for iron acquisition. Understanding the entD gene and its corresponding recombinant protein is vital, as it facilitates the study of iron metabolism in pathogenic bacteria, which can inform the development of novel antimicrobial strategies. Enterobactin binds iron with high affinity, enabling bacteria to thrive in iron-limited environments, such as within a mammalian host. The recombinant entD protein can be expressed in various systems, enabling researchers to investigate its biochemical properties, structural features, and interaction mechanisms involved in enterobactin synthesis. Additionally, studying entD can provide insights into bacterial virulence and its potential as a target for therapeutic intervention. By unraveling the functional aspects of entD and its protein product, scientists aim to combat infections caused by iron-dependent pathogens, contributing to a deeper understanding of microbial ecology and the development of innovative approaches in infectious disease management.
