Recombinant Human Dihydroorotate dehydrogenase (DHODH) Protein (His)

Beta LifeScience SKU/CAT #: BLC-08141P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Dihydroorotate dehydrogenase (DHODH) Protein (His)

Beta LifeScience SKU/CAT #: BLC-08141P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Dihydroorotate dehydrogenase (DHODH) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q02127
Target Symbol DHODH
Synonyms DHOdehase; Dhodh; Dihydroorotate dehydrogenase (quinone); Dihydroorotate dehydrogenase; Dihydroorotate dehydrogenase mitochondrial; Dihydroorotate oxidase; Human complement of yeast URA1; mitochondrial; POADS; PYRD_HUMAN; URA1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence TGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR
Expression Range 31-395aa
Protein Length Partial
Mol. Weight 43.6kDa
Research Area Metabolism
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Subcellular Location Mitochondrion inner membrane; Single-pass membrane protein.
Protein Families Dihydroorotate dehydrogenase family, Type 2 subfamily
Database References
Associated Diseases Postaxial acrofacial dysostosis (POADS)

Gene Functions References

  1. This case with grossly raised plasma DHO represents the first biochemical confirmation of functional DHODH deficiency. DHO was also easily detectable in dried plasma and blood spots. PMID: 27370710
  2. This is the first study to report on conformational changes of the HsDHODH N-terminal microdomain through a combination of CD and DEER spectroscopic techniques PMID: 26086954
  3. Considering that pyrimidine deficiency alone does not induce craniofacial dysmorphism, the DHODH mutations may contribute to the Miller syndrome in part through somehow altered mitochondrial function. PMID: 23216091
  4. Carriage of a six-marker DHODH haplotype was associated with a reduced treatment response (p = 0.008). PMID: 22966891
  5. The G202A and R346W mutation causes deficient protein stability, and the R135C mutation impairs the substrate-induced enzymatic activity, suggesting that impairment of DHODH activity is linked to the Miller syndrome phenotype. PMID: 22967083
  6. biallelic DHODH mutations in four unrelated families with typical clinical features of Miller syndrome. PMID: 22692683
  7. DHODH inhibition led to a marked decrease in melanoma growth both in vitro and in xenograft studies PMID: 21430780
  8. DHODH recessively causes Miller syndrome. PMID: 20220176
  9. required for N-(4-hydroxyphenyl)retinamide-induced reactive oxygen species production and apoptosis of cancer epithelial cells PMID: 20399851
  10. Data confirmed the presence of DHODH mutations in families with Miller syndrome. PMID: 19915526
  11. biophysical analysis of hydrogen bonding pathways in human dihydroorotate dehydrogenase PMID: 17004840
  12. Data provide new insights into the dynamic features of the DHODH reaction and suggest new approaches to the design of inhibitors against DHODH. PMID: 18672895
  13. DHODH polymorphism may be associated with incireased remiaaion in leflunomide treatment in rheumatoid arthritis patients. PMID: 19207032
  14. we report a new association of DHODH A40C polymorphism with leflunomide toxicity in patients with Rheumatoid Arthritis. PMID: 19605743

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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