Analytical Data
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Gene name
DME
- Application
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Alternative Names
DME；NDUFS2L；NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9. mitochondrial
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Species
E.coli
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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
Q8LK56
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Expression Region
1-320aa
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AA Sequence
MNSRADPGDRYFRVPLENQTQQEFMGSWIPFTPKKPRSSLMVDERVINQDLNGFPGGEFVDRGFCNTGVDHNGVFDHGAHQGVTNLSMMINSLAGSHAQAWSNSERDLLGRSEVTSPLAPVIRNTTGNVEPVNGNFTSDVGMVNGPFTQSGTSQAGYNEFELDDLLNPDQMPFSFTSLLSGGDSLFKVRQYGPPACNKPLYNLNSPIRREAVGSVCESSFQYVPSTPSLFRTGEKTGFLEQIVTTTGHEIPEPKSDKSMQSIMDSSAVNATEATEQNDGSRQDVLEFDLNKTPQQKPSKRKRKFMPKVVVEGKPKRKPRK
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Molecular Weight
51.4 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
DME, or Dimethylarginine Dimethylaminohydrolase, is an important enzyme involved in the metabolism of nitric oxide and polyamines, which play crucial roles in various physiological processes. The study of recombinant DME protein has gained prominence due to its potential therapeutic applications in cardiovascular diseases, neurodegenerative disorders, and cancer, where dysregulation of nitric oxide pathways is often implicated. Research has focused on elucidating the structure and function of DME, as understanding its catalytic mechanisms could lead to the development of novel inhibitors or activators as drug candidates. The ability to produce recombinant DME in host systems allows for detailed biochemical studies, facilitating insights into enzyme kinetics, interaction with substrates, and the effects of post-translational modifications. Furthermore, advances in protein engineering techniques enable the design of DME variants with enhanced stability and activity, paving the way for innovative therapeutic strategies. Overall, the exploration of DME recombinant protein represents a significant intersection of biochemistry, pharmacology, and translational medicine, with the promise of contributing to more effective treatments for diseases related to nitric oxide dysregulation.
