Analytical Data
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Gene name
GART
- Application
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Alternative Names
/
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Species
Human
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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
P22102
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Expression Region
111–318aa
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Molecular Weight
26.5 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
Related Products
Protein Description
GART (Phosphoribosylglycinamide transformylase) is a crucial enzyme involved in the purine biosynthesis pathway, facilitating the conversion of phosphoribosylglycinamide to formylglycinamidine, an essential step in the de novo synthesis of purines. Research on GART has garnered significant attention due to its pivotal role in cellular metabolism and its potential implications in various diseases, particularly cancer, where altered nucleotide synthesis can lead to uncontrolled cell proliferation. The enzyme is part of a multi-functional protein complex that also includes aminoimidazole ribonucleotide (AIR) synthetase and phosphoribosylaminoimidazole carboxylase, collectively known as the GART-like proteins, which are studied for their complex regulation and interactions. Understanding GART’s structure and function at a molecular level can pave the way for novel therapeutic strategies aimed at inhibiting its activity in malignant tumors, as well as for the development of antibiotics targeting bacterial GART homologs. Recent advances in structural biology techniques, including X-ray crystallography and cryo-electron microscopy, have provided valuable insights into the enzyme's active site and substrate interactions, furthering the exploration of small-molecule inhibitors. As the understanding of purine metabolism deepens, GART continues to be an attractive target for drug discovery, with ongoing studies aimed at elucidating its role in health and disease.
