Analytical Data
-
Gene name
ODC1
- Application
-
Alternative Names
ODC1;Ornithine decarboxylase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P11926
-
Expression Region
1-461aa
-
AA Sequence
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
-
Molecular Weight
71.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
ODC1, coding for ornithine decarboxylase 1, plays a critical role in polyamine biosynthesis, which is essential for cell growth, differentiation, and tissue homeostasis. Its enzyme product, ornithine decarboxylase (ODC), catalyzes the decarboxylation of ornithine to putrescine, a precursor for other polyamines like spermidine and spermine. Dysregulation of ODC1 has been implicated in various pathological conditions, including cancer, where elevated levels of ODC are often observed in rapidly proliferating tumors, suggesting its potential as a therapeutic target. Furthermore, ODC1 is essential for normal development, as evidenced by studies showing that ODC1 deficiency leads to embryonic lethality in mice. Understanding the molecular mechanisms regulating ODC1 expression and activity is crucial, as it could provide insights into metabolic disorders and cancer development. Recent advancements in biotechnology, including the production of recombinant ODC1, have paved the way for detailed biochemical characterizations and structural studies to elucidate its function and regulation further. Research in this area not only enhances our knowledge of polyamine metabolism but also opens avenues for developing targeted therapies to modulate ODC1 activity in disease contexts, making it a significant focus of current biomedical research.











