Analytical Data
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Gene name
PRPSAP2
- Application
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Alternative Names
PRPSAP2;Phosphoribosyl pyrophosphate synthase-associated Protein 2
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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
O60256
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Expression Region
1-369aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFCVTPP ELETKMNITK GGLVLFSANS NSSCMELSKK IAERLGVEMG KVQVYQEPNR ETRVQIQESV RGKDVFIIQT VSKDVNTTIM ELLIMVYACK TSCAKSIIGV IPYFPYSKQC KMRKRGSIVS KLLASMMCKA GLTHLITMDL HQKEIQGFFN IPVDNLRASP FLLQYIQEEI PDYRNAVIVA KSPASAKRAQ SFAERLRLGI AVIHGEAQDA ESDLVDGRHS PPMVRSVAAI HPSLEIPMLI PKEKPPITVV GDVGGRIAII VDDIIDDVDS FLAAAETLKE RGAYKIFVMA THGLLSSDAP RRIEESAIDE VVVTNTIPHE VQKLQCPKIK TVDISMILSE AIRRIHNGES MSYLFRNIGL DD
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Molecular Weight
43 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
PRPSAP2 (phosphoribosyl pyrophosphate synthetase-associated protein 2) is a crucial protein involved in the regulation of nucleotide metabolism, specifically in the synthesis of purine and pyrimidine nucleotides. This protein plays a significant role in cellular processes such as DNA and RNA synthesis, cellular signaling, and energy metabolism. The study of PRPSAP2 has gained attention due to its potential implications in various diseases, including cancer and metabolic disorders, where dysregulation of nucleotide metabolism is often observed. Research on PRPSAP2 recombinant proteins aims to elucidate its structure, function, and interaction with other cellular components, which could provide insights into its role in health and disease. Additionally, producing PRPSAP2 as a recombinant protein facilitates the development of specific antibodies and inhibitors, enhancing our understanding of its biological functions and paving the way for targeted therapeutic interventions. The investigation into PRPSAP2 and its recombinant forms is thus essential for advancing our knowledge of cellular metabolic pathways and their implications in disease pathogenesis.











