Analytical Data
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Gene name
pyrG
- Application
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Alternative Names
pyrG；CTPS；CTP synthase 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
P65925
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Expression Region
1-267aa
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AA Sequence
MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITDALKEKIKRAASTTDSDVIITEVGGTVGDIESLPFLEALRQMKADVGSENVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEEPVEQGIKNKLAQFCDVNSEAVIESRDVEHLYQIPLNLQAQSMDQIVCDHLKL
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Molecular Weight
49.6 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
The pyrG gene, found in various organisms, encodes a key enzyme involved in the purine biosynthetic pathway, specifically regulating guanine nucleotide synthesis. Research on pyrG recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. By using recombinant DNA technology, scientists can produce large quantities of pyrG proteins, which can then be utilized to better understand the enzyme's structure, function, and regulatory mechanisms. Additionally, the study of pyrG has implications for genetic engineering and metabolic engineering, enabling the development of strains with improved growth characteristics or enhanced production of valuable metabolites. Furthermore, the exploration of pyrG in pathogenic organisms can aid in the identification of novel drug targets, contributing to the fight against infectious diseases. Investigating pyrG proteins helps to unravel the complexities of nucleotide metabolism, offering insights that could lead to innovative strategies for disease treatment and the optimization of industrial bioprocesses. Consequently, the ongoing research on recombinantly expressed pyrG proteins is pivotal for advancing our understanding of fundamental biological processes and developing practical applications in various fields, including pharmaceuticals, agriculture, and energy production.
