Analytical Data
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Gene name
ODC
- Application
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Alternative Names
SLC25A21;ODC;Mitochondrial 2-oxodicarboxylate carrier
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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
P11926
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Expression Region
1-461aa
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AA Sequence
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
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Molecular Weight
71.1 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
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Protein Description
ODC (ornithine decarboxylase) is a key enzyme in the polyamine biosynthesis pathway, catalyzing the conversion of ornithine to putrescine, which is crucial for cell growth, differentiation, and proliferation. Abnormal regulation of ODC has been implicated in various diseases, including cancer, as its overexpression can lead to enhanced cell division and tumor progression. Research into ODC has revealed its potential as a therapeutic target, particularly in the context of cancer treatment; inhibitors of ODC could effectively suppress tumor growth by disrupting polyamine synthesis. Moreover, ODC is known to undergo complex post-translational modifications and oligomerization, influencing its activity and stability. Understanding the structure and function of ODC, including its recombinant protein forms, is vital for developing novel inhibitors and therapeutic strategies. Recent advances in molecular biology techniques have enabled the production and characterization of recombinant ODC proteins, providing insights into their functional mechanisms and interactions. Thus, ongoing studies aim to elucidate the molecular dynamics of ODC and explore its implications in disease progression, ultimately contributing to the development of targeted therapies in oncology and other areas of medicine.
