Analytical Data
-
Gene name
gadA
- Application
-
Alternative Names
gadA; gadS; b3517; JW3485Glutamate decarboxylase alpha; GAD-alpha; EC 4.1.1.15
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P69908
-
Expression Region
1-466aa
-
Molecular Weight
56.7 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 study of gadA recombinants has emerged as a significant area of interest in microbiology and molecular biology, primarily due to the role of gadA in the metabolism of certain bacteria, notably Escherichia coli. GadA encodes glutamate decarboxylase, an enzyme that catalyzes the decarboxylation of glutamate to gamma-aminobutyric acid (GABA), contributing to the organism’s response to acidic environments and playing a vital role in acid resistance. Understanding gadA's function and regulation is crucial for delineating the mechanisms of microbial survival under stress conditions, which has implications for pathogenicity and food safety. Furthermore, gadA’s involvement in GABA synthesis highlights its potential applications in biotechnology, particularly in developing probiotics and bioengineering microbial strains for enhanced production of valuable metabolites. Recent advances in recombinant DNA technology have facilitated the expression and characterization of gadA proteins, enabling researchers to investigate their biochemical properties and interactions within metabolic pathways. Such studies not only provide insights into microbial physiology but also open avenues for innovative applications in agriculture and pharmaceuticals, making gadA a key target for research in microbial genetics and biotechnological advancements.
