Analytical Data
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Gene name
ODC1
- Application
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Alternative Names
DCOR_HUMAN; Dodc1; Odc 1; ODC; Odc1; ODC2; Ornithine decarboxylase 1; Ornithine decarboxylase 2; Ornithine decarboxylase; Ornithine decarboxylase structural 1; RNODC
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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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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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
Related Products
Protein Description
ODC1, or Ornithine Decarboxylase 1, is a key enzyme in the polyamine biosynthesis pathway, catalyzing the conversion of ornithine to putrescine, a crucial precursor for various polyamines like spermidine and spermine. The significance of ODC1 extends beyond basic cellular metabolism, as polyamines are implicated in a variety of physiological processes, including cell growth, differentiation, and apoptosis. Aberrant regulation or overexpression of ODC1 has been linked to several pathological conditions, particularly cancer, where enhanced polyamine synthesis can promote tumorigenesis and cell proliferation. Consequently, ODC1 has garnered attention as a potential therapeutic target in cancer treatment, leading to the development of ODC inhibitors. Over the years, researchers have made significant strides in understanding the structure, function, and regulation of ODC1, utilizing recombinant protein techniques to produce ODC1 for in-depth biochemical studies. This recombinant ODC1 protein not only facilitates the exploration of its enzymatic properties but also aids in investigating the impacts of various inhibitors, thus providing insights into its role in disease mechanisms. Additionally, elucidating the regulatory networks involving ODC1 can open avenues for novel therapeutic strategies aimed at modulating polyamine levels in pathological states. This accumulating body of knowledge underscores the importance of ODC1 in both fundamental biology and clinical applications, paving the way for innovative approaches in combating diseases influenced by polyamine dysregulation.
