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Merck
CN

F7296

Sigma-Aldrich

果糖基氨基酸氧化酶 来源于棒状杆菌

recombinant, expressed in E. coli, lyophilized powder, ≥0.45 units/mg protein

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EC 号:
1.5.3.x
EC 号:
MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54

重组

expressed in E. coli

质量水平

形式

lyophilized powder

比活

≥0.45 units/mg protein

分子量

~88 kDa by electrophoresis

储存温度

−20°C

一般描述

果糖基氨基酸氧化酶[果糖基-α-1-氨基酸:氧氧化还原酶]是一种黄素蛋白,其催化果糖基氨基酸氧化形成葡糖酮、氨基酸和过氧化氢。
酶委员会(E.C.)1.5.3.x

应用

棒状杆菌属的果糖基氨基酸氧化酶已用于通过基于石英晶体微量天平(QCM)检测血液样品中的糖化血红蛋白 HbA1c。
果糖基氨基酸氧化酶可用于检测糖化蛋白的水平,糖化蛋白是糖尿病的标志

生化/生理作用

果糖基氨基酸氧化酶(FAOD)由 FAD 结合基序组成,根据底物特异性分为三类。工程化棒杆菌属果糖基氨基酸氧化酶在 45°C 时稳定,可用于开发糖化蛋白质生物传感系统和测定糖化血红蛋白 HbA1c。FAOD 与果糖基肽氧化酶具有序列同源性,并且两者均对 α-果糖基底物有效。
果糖胺是葡萄糖与氨基酸或蛋白质的氨基缩合时形成的。果糖胺氧化酶(FAOX)催化低分子量果糖胺的氧化脱糖作用。果糖基氨基酸氧化酶催化连接果糖基 C1 的 C-N 键和果糖基氨基酸的氮的氧化。
适用于果糖基-L-氨基酸的测定。

单位定义

在 pH 8.0,37°C 下,一个单位每分钟将产生 1.0 μ摩尔的过氧化氢。

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品

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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.
Ryoichi Sakaue et al.
Applied and environmental microbiology, 69(1), 139-145 (2003-01-07)
We succeeded in isolating several thermostable mutant fructosyl-amino acid oxidase (FAOX; EC 1.5.3) without reduction of productivity by directed evolution that combined an in vivo mutagenesis and membrane assay screening system. Five amino acid substitutions (T60A, A188G, M244L, N257S, and
Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum.
M. Fujiwara et al.
Applied Microbiology, 74, 813-819 (2007)
Stefano Ferri et al.
Journal of diabetes science and technology, 3(3), 585-592 (2010-02-11)
Glycated proteins, particularly glycated hemoglobin A1c, are important markers for assessing the effectiveness of diabetes treatment. Convenient and reproducible assay systems based on the enzyme fructosyl amino acid oxidase (FAOD) have become attractive alternatives to conventional detection methods. We review
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

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