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AOX1 Antibody (Center) 精选

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - AOX1 Antibody (Center) AP6700c
    Anti-AOX1 Antibody (Center) at 1:1000 dilution + HepG2 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 148 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 4 - AOX1 Antibody (Center) AP6700c
    AOX1 Antibody (Center) (Cat.#AP6700c) flow cytometry analysis of HepG2 cells (bottom histogram) compared to a negative control cell (top histogram). FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
FC, WB, E
Primary Accession Q06278
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 147918 Da
Antigen Region 698-726 aa
Additional Information
Gene ID 316
Other Names Aldehyde oxidase, Aldehyde oxidase 1, Azaheterocycle hydroxylase, 1173-, AOX1, AO
Target/Specificity This AOX1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 698-726 amino acids from the Central region of human AOX1.
Dilution FC~~1:10~50
WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAOX1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name AOX1 (HGNC:553)
Synonyms AO
Function Primarily catalyzes oxidation reactions of a broad range of drug and xenobiotic substrates and participates in their metabolism through oxidative biotransformation (PubMed:14709625, PubMed:20444863, PubMed:22279051, PubMed:22996261, PubMed:23857892, PubMed:26322824, PubMed:26842593, PubMed:34415167, PubMed:7786031, PubMed:9224775). Oxidizes at least three structural types of substrates: aldehydes such as benzaldehyde, retinal, pyridoxal, and vanillin; aromatic azaheterocyclic compounds such as phthalazine, quinazoline and phenanthridine; and quaternary azaheterocyclic compounds such as 1- methylnicotinamide and nicotine imine (PubMed:14709625, PubMed:22279051, PubMed:22996261, PubMed:23857892, PubMed:26322824, PubMed:26842593, PubMed:34415167, PubMed:7786031, PubMed:9224775). Converts aldehydes to carboxylic acids, aromatic and quaternary azaheterocyclic compounds to lactams, typically by using molecular oxygen as the terminal electron acceptor and producing hydrogen peroxide as a by-product (PubMed:14709625, PubMed:22279051, PubMed:22996261, PubMed:23857892, PubMed:26322824, PubMed:26842593, PubMed:34415167, PubMed:7786031, PubMed:9224775). Under some conditions, especially with electron-deficient substrates or limited oxygen, can also catalyze reduction reactions using N- methylnicotinamide, 2-hydroxypyrimidine or benzaldehyde as electron donor substrate (Probable) (PubMed:15720138). These reductive activities include N-O bond reductions in nitro groups (e.g., imidacloprid, IMI), hydroxamic acids, and oxazoles (e.g., zonisamide), as well as N-S bond reductions of sulfoxides (e.g., sulindac) (By similarity).
Cellular Location Cytoplasm
Tissue Location Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level).
Research Areas

BACKGROUND

AOX1 catalyzes: An aldehyde + H2O + O2 = a carboxylic acid + H2O2.

REFERENCES

Wright,R.M., Proc. Natl. Acad. Sci. U.S.A. 90 (22), 10690-10694 (1993)

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