Analytical Data
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Gene name
PURG
- Application
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Alternative Names
PURG; Purine-rich element-binding protein gamma; Purine-rich element-binding protein G
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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
Q9UJV8
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Expression Region
1-347 aa
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AA Sequence
MERARRRGGG GGRGRGGKNV GGSGLSKSRL YPQAQHSHYP HYAASATPNQ AGGAAEIQEL ASKRVDIQKK RFYLDVKQSS RGRFLKIAEV WIGRGRQDNI RKSKLTLSLS VAAELKDCLG DFIEHYAHLG LKGHRQEHGH SKEQGSRRRQ KHSAPSPPVS VGSEEHPHSV LKTDYIERDN RKYYLDLKEN QRGRFLRIRQ TMMRGTGMIG YFGHSLGQEQ TIVLPAQGMI EFRDALVQLI EDYGEGDIEE RRGGDDDPLE LPEGTSFRVD NKRFYFDVGS NKYGIFLKVS EVRPPYRNTI TVPFKAWTRF GENFIKYEEE MRKICNSHKE KRMDGRKASG EEQECLD
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Molecular Weight
39.5 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
PURG protein, a member of the purine metabolic pathway, has garnered research interest due to its potential implications in cellular processes and diseases. This protein plays a crucial role in purine nucleotide synthesis, which is vital for various cellular functions, including DNA and RNA synthesis, cell signaling, and energy metabolism. Aberrations in purine metabolism have been linked to several pathological conditions, including cancer and metabolic disorders. Studies suggest that PURG may influence cell proliferation and apoptosis, making it a significant target for therapeutic exploration. As researchers strive to understand the molecular mechanisms governing PURG's function, the development of recombinant PURG protein has emerged as a key focus, enabling detailed investigations into its structure and activity. Characterizing this protein through recombinant techniques allows for better insights into its role in metabolic pathways and its potential as a biomarker or therapeutic target. The ongoing exploration of PURG protein not only fosters a deeper understanding of purine metabolism but also opens avenues for novel treatment strategies in diseases associated with metabolic dysregulation.
