Analytical Data
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Gene name
purF
- Application
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Alternative Names
(ATase(Glutamine phosphoribosylpyrophosphate amidotransferase)(GPATase)
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Species
Mycobacterium tuberculosis
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WHQ6
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Expression Region
35-527aa
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Molecular Weight
56.5 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
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Protein Description
The purF gene encodes an enzyme involved in the de novo synthesis pathway of purine nucleotides, which are essential for various cellular functions, including DNA and RNA synthesis, energy metabolism, and cell signaling. Research on purF recombinant protein has garnered attention due to its role in regulating purine metabolism and its potential implications in understanding certain diseases, such as cancer and metabolic disorders. Recombinant purF protein is instrumental for studying the enzyme's structure, function, and interactions, allowing scientists to elucidate the mechanisms that govern purine biosynthesis. Moreover, by producing purF in a heterologous system, researchers can investigate its enzymatic properties, explore its potential as a therapeutic target, and develop inhibitors that could selectively modulate purine metabolism. This research is also crucial for synthetic biology applications, where purF can be utilized to engineer metabolic pathways in microorganisms for bioproduction of nucleotides or pharmaceuticals. Overall, the exploration of purF recombinant protein is pivotal for advancing our understanding of cellular metabolism and developing novel biotechnological solutions.
