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Haao (GeneName), 3-hydroxyanthranilate 3,4-dioxygenase (ProteinName), 3HAO_MOUSE.
Product Name:

Mouse Haao/ 3-hydroxyanthranilate 3,4-dioxygenase ELISA Kit

Cat.#:

E10868m

Brand:
EIAab®
Regulatory Status:
Alternative:

3-hydroxyanthranilate oxygenase, 3-HAO, 3-hydroxyanthranilic acid dioxygenase, HAD

Detection Method:
ELISA
Assay Type:
Sandwich
Detection Range:
0.312-20ng/mL
Sensitivity:
0.159ng/mL
Specificity:
Natural and recombinant mouse 3-hydroxyanthranilate 3,4-dioxygenase
Sample Type:
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Sample Data:
Assay Procedure:
Assay Procedure
Research Area:
Neurosciences
Mouse Haao ELISA Kit
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Product Datasheets
Instruction: Down Instruction
MSDS: MSDS


Precision

Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.

Intra-Assay CV: ≤8.7%

Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.

Inter-Assay CV: ≤10.7%

Recovery
Recovery was determined by spiking various levels of 3-hydroxyanthranilate 3,4-dioxygenase into serum and plasma.

Sample Type

Average(%)

Recovery Range(%)

Serum

95

89-101

Plasma

97

91-103

 

 

 

 

Linearity
The linearity of the kit was assayed by testing samples spiked with appropriate concentration of 3-hydroxyanthranilate 3,4-dioxygenase and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.

Sample

1:2

1:4

1:8

1:16

serum(n=5)

100-110%

112-122%

95-103%

93-103%

EDTA plasma(n=5)

101-111%

102-114%

86-96%

98-109%

heparin plasma(n=5)

100-110%

 

81-94%

105-117%

95-106%

 

General Annotation


Sub Unit:
Monomer.


Function:
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.


Subcellular Location:
Cytoplasm


This product has not yet been referenced specifically in any publications.

[1].
"Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase."

[2].
"NAD Deficiency, Congenital Malformations, and Niacin Supplementation."

[3].
"Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site."

[4].
"Evidence for genes on chromosome 2 contributing to alcohol dependence with conduct disorder and suicide attempts."

[5].
"Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling."

[6].
"Identification of candidate epigenetic biomarkers for ovarian cancer detection."

[7].
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."

[8].
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."

[9].
"Cloning of human 3-hydroxyanthranilic acid dioxygenase in Escherichia coli: characterisation of the purified enzyme and its in vitro inhibition by Zn2+."

[10].
"A proteome-scale map of the human interactome network."
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