Analytical Data
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Gene name
DHODH
- Application
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Alternative Names
DHODH;Dihydroorotate dehydrogenase (quinone). mitochondrial
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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
Q02127
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Expression Region
31-395aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTGDER FYAEHLMPTL QGLLDPESAH RLAVRFTSLG LLPRARFQDS DMLEVRVLGH KFRNPVGIAA GFDKHGEAVD GLYKMGFGFV EIGSVTPKPQ EGNPRPRVFR LPEDQAVINR YGFNSHGLSV VEHRLRARQQ KQAKLTEDGL PLGVNLGKNK TSVDAAEDYA EGVRVLGPLA DYLVVNVSSP NTAGLRSLQG KAELRRLLTK VLQERDGLRR VHRPAVLVKI APDLTSQDKE DIASVVKELG IDGLIVTNTT VSRPAGLQGA LRSETGGLSG KPLRDLSTQT IREMYALTQG RVPIIGVGGV SSGQDALEKI RAGASLVQLY TALTFWGPPV VGKVKRELEA LLKEQGFGGV TDAIGADHRR
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Molecular Weight
42 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
Dihydroorotate dehydrogenase (DHODH) is a key enzyme in the de novo pyrimidine biosynthesis pathway, catalyzing the conversion of dihydroorotate to orotate while simultaneously reducing flavin mononucleotide (FMN) to FMNH2. Given its crucial role in nucleotide synthesis, DHODH has garnered significant attention as a potential therapeutic target for various diseases, including cancer, autoimmune disorders, and viral infections. Research has shown that inhibiting DHODH can effectively hinder the proliferation of rapidly dividing cells, such as tumor cells and activated lymphocytes, making it a promising candidate for drug development. Furthermore, DHODH is implicated in the regulation of mitochondrial respiration and reactive oxygen species (ROS) production, contributing to its potential as a multi-faceted target in treating metabolic disorders. Recent advancements in recombinant protein technology have enabled the production of DHODH in various expression systems, facilitating detailed biochemical characterization and high-throughput screening for inhibitors. Understanding the structure-function relationship of DHODH is essential for designing selective inhibitors that minimize off-target effects. Consequently, ongoing research focuses on elucidating the enzyme's mechanism of action, exploring its pharmacological potential, and defining its role in various pathological conditions, thereby paving the way for novel therapeutic strategies that leverage DHODH modulation.
