Recombinant human Ornithine Decarboxylase/ODC protein (Active) is a Human Full Length protein, in the 1 to 461 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
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Key facts
- Purity
- >95% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Alternative names
Ornithine decarboxylase, ODC, ODC1
Recommended products
Recombinant human Ornithine Decarboxylase/ODC protein (Active) is a Human Full Length protein, in the 1 to 461 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >95% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- 1 U/mg; unit will catalyze conversion of 1.0 micromole of ornithine to putrescine per minute at pH 7.6 and 37°C.
- Accession
- P11926-1
- Animal free
- Yes
- Species
- Human
- Concentration
- Storage buffer
pH: 7.4
Constituents: 10.269% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic
Sequence info
Amino acid sequence
- Accession
- P11926
- Protein length
- Full Length
- Predicted molecular weight
- 51.1 kDa
- Amino acids
- 1 to 461
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Lyophilized
General info
- Function
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
- Sequence similarities
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
- Post-translational modifications
S-Nitrosylation inhibits the enzyme. S-Nitrosylated in vitro on 4 cysteine residues.
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage conditions
- +4°C, -20°C
- Appropriate long-term storage conditions
- +4°C, -20°C
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Ornithine Decarboxylase also known as ODC or ODC1 is an enzyme that plays an important role in polyamine biosynthesis. This enzyme catalyzes the decarboxylation of ornithine to form putrescine a precursor for spermidine and spermine. ODC is a small protein with a molecular mass around 48 kDa. It is expressed in various tissues including the liver kidney and brain. ODC expression tends to be highest in rapidly growing tissues due to its involvement in cell growth and differentiation.
- Biological function summary
ODC actively participates in cell proliferation and differentiation by regulating the levels of polyamines which are essential for DNA stabilization and cellular processes. While ODC does not form part of a larger protein complex its activity requires the presence of cofactor pyridoxal 5'-phosphate. By controlling polyamine synthesis ODC influences gene expression ion channel functions and protein synthesis impacting cell cycle progression and apoptosis.
- Pathways
Ornithine decarboxylation connects with important biological processes such as the urea cycle and polyamine biosynthetic pathway. In these pathways enzymes like arginase and S-adenosylmethionine decarboxylase work closely with ODC. ODC's role in regulating polyamine levels makes it an important component of cellular metabolism and growth pathways. Through these pathways ODC coordinates with other proteins to ensure proper cellular function and response to growth signals.
- Associated diseases and disorders
ODC activity has been linked to cancer and neurological disorders. Overexpression and dysregulation of ODC can lead to increased polyamine levels which associate with tumor development and proliferation particularly in colorectal cancer. ODC also connects with proteins like c-Myc which regulates its expression and is often dysregulated in cancer. In neurological disorders abnormal ODC function affects neurodegeneration influencing proteins involved in neuronal survival and plasticity.
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2 product images
SDS-PAGE - Recombinant human Ornithine Decarboxylase/ODC protein (Active) (ab286069)
SDS-PAGE analysis of ab286069 under reducing conditions.
Functional Studies - Recombinant human Ornithine Decarboxylase/ODC protein (Active) (ab286069)
Enzyme activity of ab286069. The activity of the enzyme is 6 U/mg.
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