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AB270269

Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R]

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(1 Publication)

Rabbit Recombinant Monoclonal Ornithine Decarboxylase/ODC antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human ODC1.

View Alternative Names

Ornithine decarboxylase, ODC, ODC1

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R] (AB270269)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R] (AB270269)

Formalin-fixed, paraffin-embedded human prostate carcinoma tissue stained for Ornithine Decarboxylase/ODC using ab270269 at 0.5 μg/ml in imunnohistochemical analysis.

Western blot - Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R] (AB270269)
  • WB

Supplier Data

Western blot - Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R] (AB270269)

All lanes:

Western blot - Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R] (ab270269) at 1 µg/mL

All lanes:

PC3 cell lysate

Predicted band size: 51 kDa

false

  • Carrier free

    Anti-Ornithine Decarboxylase/ODC antibody [ODC1/3636R] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

ODC1/3636R

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, IHC-P

applications

Immunogen

Recombinant Full Length Protein corresponding to Human ODC1.

P11926

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "0.5-1 µg/mL", "WB-species-notes": "<p></p>", "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "0.25-0.5 µg/mL", "IHCP-species-notes": "<p></p>" }, "Mouse": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "", "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" }, "Rat": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "", "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A/G
Purification notes
Purified from Bioreactor Concentrate by Protein A/G.
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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.
See full target information ODC1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Oncotarget 15:124-133 PubMed38329728

2024

GZ17-6.02 interacts with bexarotene to kill mycosis fungoides cells.

Applications

Unspecified application

Species

Unspecified reactive species

Michael R Booth,Laurence Booth,Jane L Roberts,Cameron West,Paul Dent
View all publications

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