Rabbit Polyclonal SMOX antibody. Suitable for IHC-P, ICC/IF and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human SMOX aa 1-150.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: 59% PBS, 40% Glycerol (glycerin, glycerine)
IHC-P | ICC/IF | |
---|---|---|
Human | Tested | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/50.00000 - 1/200.00000 | Notes Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1.00000-4.00000 µg/mL | Notes Cells were fixed in 4% paraformaldehyde and then permealized with 0.1% Triton X-100. |
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Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.
C20orf16, SMO, UNQ3039/PRO9854, SMOX, Spermine oxidase, Polyamine oxidase 1, PAO-1, PAOh1
Rabbit Polyclonal SMOX antibody. Suitable for IHC-P, ICC/IF and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human SMOX aa 1-150.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: 59% PBS, 40% Glycerol (glycerin, glycerine)
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SMOX also known as spermine oxidase is an enzyme that catalyzes the oxidation of spermine to spermidine releasing hydrogen peroxide and 3-aminopropanal. This enzyme is important in the polyamine metabolism process. SMOX has a molecular mass of approximately 66 kDa. It is expressed in various tissues including the liver kidney and other tissues with high metabolic activity.
SMOX is essential for polyamine catabolism influencing cell growth and proliferation. It does not function as part of a complex but works independently to regulate intracellular levels of polyamines. The balance of polyamines like spermine and spermidine is critical for cellular functions impacting cell cycle regulation and apoptosis.
The enzymatic activity of SMOX plays an important role in the polyamine metabolic pathway. This pathway interconnects with the urea cycle and is involved in the regulation of cellular proliferation. SMOX influences the activity of proteins like ornithine decarboxylase (ODC) which is vital in polyamine synthesis. By controlling polyamine levels SMOX indirectly modulates signaling pathways associated with cellular responses and stress reactions.
SMOX has a connection with cancer and neurodegenerative diseases. Abnormal expression of SMOX can disrupt polyamine homeostasis leading to oxidative stress and promoting tumorigenesis. In cancer SMOX activity often pairs with increased levels of ODC contributing to tumor progression. In neurodegenerative diseases such as Alzheimer's disease SMOX activity is linked to elevated oxidative stress resulting in neuronal damage and cognitive decline. The regulation of SMOX and polyamine metabolism remains a focus of research for therapeutic strategies.
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Immunohistochemical analysis of paraffin-embedded Human colon tissue labeling Spermine oxidase with ab150971 at 1/50 dilution.
Immunofluorescent analysis of PFA/Triton X-100-fixed U20S cells labeling Spermine oxidase with ab150971 at 4 μg/ml.
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