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F7296
Fructosyl-Amino Acid Oxidase from Corynebacterium sp.
recombinant, expressed in E. coli, lyophilized powder, ≥0.45 units/mg protein
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| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| 25 units | Available to ship TODAYfromMILWAUKEE | $210.00 $178.50 | |
| 100 units | Available to ship TODAYfromMILWAUKEE | $642.00 $545.70 |
About This Item
Specific activity:
≥0.45 units/mg protein
Recombinant:
expressed in E. coli
$178.50
List Price$210.00Save 15%Web-Only Promotion
Available to ship TODAYDetails
recombinant
expressed in E. coli
Quality Level
form
lyophilized powder
specific activity
≥0.45 units/mg protein
mol wt
~88 kDa by electrophoresis
storage temp.
−20°C
General description
Enzyme Commission (E.C.) 1.5.3.x
Fructosyl amino acid oxidase [fructosyl-a-l-amino acid:oxygen oxidoreductase] is a flavoprotein that catalyzes the oxidation of fructosyl amino acids to form glucosone, amino acid and hydrogen peroxide.[1]
Application
Fructosyl-amino acid oxidase can be used to detect the levels of glycated proteins, which are markers for diabetes mellitus.
Fructosyl-Amino Acid Oxidase from Corynebacterium sp has been used in glycated haemoglobin HbA1c detection in blood samples using quartz crystal microbalance (QCM) based detection.
Biochem/physiol Actions
Fructosamines are formed when glucose is condensed amino group of amino acids or proteins.[2] Fructosamine oxidases (FAOX) catalyze the oxidative deglycation of low molecular weight fructosamines. Fructosyl amino acid oxidase catalyzes the oxidation of the C-N bond linking the C1 of the fructosyl moiety and the nitrogen of the amino group of fructosyl amino acids.[3]
Suitable for the determination of fructosyl-L-amino acid.
Fructosyl-Amino Acid Oxidase (FAOD) comprises of FAD-binding motifs and is classified into three types based on substrate specificity. The engineered Corynebacterium Fructosyl-Amino Acid Oxidase is stable at 45°C and could be exploited for the development of glycated protein biosensing system[3] and glycated hemoglobin HbA1c measurements. FAOD shares sequence homology with fructosyl peptide oxidase and both are effective on α-fructosyl substrates.
Other Notes
One unit will produce 1.0 μmole of hydrogen peroxide per minute at pH 8.0 at 37 °C.
1 of 1
This Item | |||
|---|---|---|---|
| specific activity ≥0.45 units/mg protein | specific activity ≥12 units/mg protein | specific activity 25-50 units/mg solid | specific activity ≥60 units/mg protein |
| form lyophilized powder | form powder | form lyophilized powder | form lyophilized powder |
| recombinant expressed in E. coli | recombinant expressed in E. coli ≥12 units/mg protein | recombinant - | recombinant - |
| mol wt ~88 kDa by electrophoresis | mol wt - | mol wt 44 kDa | mol wt 245 kDa |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum.
M. Fujiwara et al.
Applied Microbiology, 74, 813-819 (2007)
S A Schellini et al.
Acta ophthalmologica, 67(5), 601-604 (1989-10-01)
The authors report a case of fibrohistiocytoma of the limbus and discuss the clinical, histopathological and immunohistochemical findings concerning this type of lesion, with a comparison of their findings with those reported in the literature.
Y Sakai et al.
FEBS letters, 459(2), 233-237 (1999-10-13)
A high-level production of fructosyl amino acid oxidase (FAOD), whose production was toxic in Escherichia coli, was investigated through attempts to utilize the peroxisome of Candida boidinii as the place for protein accumulation. The alcohol oxidase-depleted strain (strain aod1Delta) produced
Global Trade Item Number
| SKU | GTIN |
|---|---|
| F7296-25UN | 04061832729510 |
| F7296-100UN | 04061832729503 |
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