Analytical Data
-
Gene name
gadA
- Application
-
Alternative Names
gadA；Glutamate decarboxylase A
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P69908
-
Expression Region
1-466aa
-
AA Sequence
MDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
-
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, a glutamate decarboxylase enzyme, has gained significant attention due to its pivotal role in the acid tolerance response of various microorganisms, particularly in foodborne pathogens like Escherichia coli. GadA catalyzes the conversion of glutamate to gamma-aminobutyric acid (GABA), a process that not only helps in maintaining pH homeostasis under acidic conditions but also contributes to microbial survival and virulence. Recombinant GadA proteins have been expressed in heterologous systems to facilitate detailed investigations into their enzymatic properties, structural characteristics, and functional mechanisms. These studies are crucial for understanding the adaptive strategies of bacteria in acidic environments, as well as for potential applications in food safety and biotechnology. Furthermore, the insights gained from GadA research can inform the development of novel antimicrobial strategies and the enhancement of probiotic formulations, thereby leveraging its biological functions for health benefits. Ongoing research aims to elucidate the regulation of GadA expression, its interaction with other cellular pathways, and its effect in different microbial species, highlighting its significance in both basic and applied microbiology.
