Analytical Data
-
Gene name
GltI/YbeJ
- Application
-
Alternative Names
gltI; ybeJ; yzzK; b0655; JW5092Glutamate/aspartate import solute-binding protein
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P37902
-
Expression Region
23-302aa
-
Molecular Weight
47.2 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
GltI/YbeJ is a membrane-associated protein involved in the transport of amino acids in bacteria, specifically playing a critical role in the glutamate transport system. Studies have shown that this protein is essential for bacterial growth and survival under various environmental conditions, particularly in nutrient-limited situations. GltI/YbeJ is considered a part of the large family of solute transporters, which are pivotal for cellular homeostasis and metabolic functions. Its function has garnered interest due to its implications in bacterial physiology and potential roles in antibiotic resistance mechanisms. Given the increasing concern over multidrug-resistant bacterial strains, understanding the structure and function of GltI/YbeJ offers potential for novel therapeutic strategies targeting amino acid transport pathways. Recent advances in recombinant protein technology have enabled the production of GltI/YbeJ for detailed biochemical and structural analyses. These studies aim to elucidate the transport mechanism, substrate specificity, and regulatory factors that govern the activity of this protein. Furthermore, insights derived from GltI/YbeJ research may contribute to the development of inhibitors designed to disrupt amino acid transport in pathogenic bacteria, thus offering a new avenue for antimicrobial interventions. Overall, the investigation of GltI/YbeJ serves not only to deepen our understanding of bacterial transport systems but also to inform the broader context of infectious disease management in an era of antibiotic resistance.
