Analytical Data
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Gene name
UROD
- Application
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Alternative Names
PCT; Uroporphyrinogen III Decarboxylase
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P70697
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Expression Region
Met1~Asn367
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Molecular Weight
43kDa
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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
UROD (uroporphyrinogen decarboxylase) is a crucial enzyme involved in the heme biosynthesis pathway, facilitating the conversion of uroporphyrinogen to coproporphyrinogen. Its dysfunction leads to porphyria, a group of disorders characterized by the accumulation of porphyrins and their precursors, resulting in various clinical symptoms, including photosensitivity and abdominal pain. Research on recombinant UROD has gained traction due to its potential for therapeutic applications. By expressing UROD in heterologous systems, scientists aim to produce it in sufficient quantities for biochemical and pharmaceutical studies. This recombinant approach enables a better understanding of the enzyme's structure-function relationship and the molecular mechanisms underlying porphyria. Additionally, studies suggest that understanding UROD's activity could pave the way for developing novel treatments and gene therapies for diseases associated with its deficiency. By harnessing biotechnological advancements, researchers are investigating ways to stabilize and enhance UROD's activity, which could lead to promising strategies for managing porphyria and improving patient outcomes.
