Analytical Data
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Gene name
PRPS1
- Application
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Alternative Names
PRPS1;Ribose-phosphate pyrophosphokinase 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60891
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Expression Region
2-318aa
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AA Sequence
PNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
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Molecular Weight
35 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
Identification
Protein Description
PRPS1 (Phosphoribosyl pyrophosphate synthetase 1) is a critical enzyme involved in the de novo synthesis of purine nucleotides, playing a vital role in cellular metabolism and nucleotide homeostasis. Mutations in the PRPS1 gene are associated with a range of clinical disorders, including X-linked nonsyndromic intellectual disability and other metabolic diseases, underscoring its importance in human health. The study of PRPS1 recombinant proteins has gained significant interest as it enables researchers to explore the enzyme's structure-function relationship, mechanisms of action, and interaction with various substrates. By generating recombinant PRPS1, scientists can investigate the biochemical properties of the enzyme in vitro, assess the impact of specific mutations, and evaluate potential therapeutic interventions for associated disorders. Furthermore, recombinant PRPS1 serves as a valuable tool for high-throughput screening of small molecule inhibitors that could modulate its activity, providing insights into novel strategies for treating diseases linked to purine metabolism dysregulation. Thus, research on PRPS1 recombinant proteins not only enhances our understanding of fundamental biological processes but also opens avenues for developing targeted therapies for genetic and metabolic conditions related to this enzyme.
