Analytical Data
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Gene name
purD
- Application
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Alternative Names
GARS Glycinamide ribonucleotide synthetase Phosphoribosylglycinamide synthetase
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Species
Escherichia coli O157:H7
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8X612
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Expression Region
1-429aa
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Molecular Weight
62 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 research on purD recombinant protein focuses on the purine biosynthesis pathway, particularly the enzyme encoded by the purD gene, which plays a crucial role in the synthesis of purine nucleotides. PurD, or phosphoribosylaminoimidazole carboxylase, catalyzes a key step in the conversion of phosphoribosylaminoimidazole to aminoimidazole ribonucleotide, a precursor for adenine and guanine nucleotides. Understanding the structure and function of PurD is essential due to its implications in microbial metabolism and potential targets for antibiotic development, as inhibiting purine biosynthesis in pathogens can effectively hinder their growth and viability. The recombinant expression of purD allows for the production of the enzyme in a controlled laboratory setting, facilitating detailed studies on its enzymatic properties, structure-function relationships, and interactions with substrates and inhibitors. This research not only enhances our understanding of purine metabolism but also contributes to the development of novel therapeutic strategies against bacterial infections, thereby advancing both microbiology and pharmacology.
