Analytical Data
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Gene name
UROD
- Application
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Alternative Names
UROD；Uroporphyrinogen decarboxylase
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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
P06132
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Expression Region
1-367aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN
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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
UROD (Uroporphyrinogen Decarboxylase) is a key enzyme in the heme biosynthesis pathway, responsible for converting uroporphyrinogen to coproporphyrinogen, a crucial step in the production of heme. Deficiency in UROD activity is associated with a rare genetic disorder known as porphyria cutanea tarda (PCT), which leads to the accumulation of porphyrins and manifests in skin lesions and photosensitivity. Research into UROD recombinant protein aims to better understand its structure, function, and regulatory mechanisms, as well as to develop potential therapeutic strategies for managing PCT and other related disorders. Advances in recombinant DNA technology have allowed for the expression and purification of UROD, enabling detailed biochemical characterization and studies on its enzymatic activity, stability, and interactions with other biomolecules. This research not only enhances our understanding of porphyrin metabolism but also opens avenues for novel therapeutic interventions, including enzyme replacement therapy and pharmacological modulation of UROD activity. By elucidating the molecular basis of UROD function and its role in porphyrin disorders, scientists aspire to develop targeted treatments that could significantly improve the quality of life for affected individuals. Additionally, understanding UROD's structure-function relationship is critical for the design of inhibitors that could be used in other pathological contexts where heme synthesis is dysregulated, underscoring its relevance in both basic and applied biomedical research.
