Analytical Data
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Gene name
gltA
- Application
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Species
Rickettsia australis
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P51039
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Expression Region
1-411aa
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Molecular Weight
53.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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 the gltA gene, which encodes the enzyme citrate synthase, has garnered significant interest in the field of microbial physiology and biochemistry due to its critical role in the Krebs cycle and overall cellular metabolism. GltA is a key enzyme that catalyzes the condensation of acetyl-CoA and oxaloacetate to form citrate, a crucial step in energy production and biosynthesis in various organisms, including bacteria and eukaryotes. Research on recombinant gltA protein has primarily focused on understanding its structure-function relationships, enzyme kinetics, and regulatory mechanisms, as alterations in gltA activity can impact metabolic pathways and cellular growth. Furthermore, gltA has been identified as a potential target for antimicrobial drug development, particularly against pathogenic bacteria, as inhibiting its function could disrupt their metabolic processes. Recombinant expression of gltA allows for detailed studies of the protein's characteristics in a controlled environment, enabling researchers to investigate its role in metabolic regulation and host-pathogen interactions. As such, the exploration of gltA recombinant proteins not only advances our fundamental understanding of metabolic processes but also opens avenues for therapeutic interventions against diseases caused by gltA-expressing organisms.
