核苷类似物 MANT ATP 的核糖基团经过修饰。MANT 荧光基团及其附着位置的紧凑性使得核苷类似物几乎不会干扰核苷酸-蛋白质相互作用。由于 MANT 荧光对荧光基团的环境敏感,因此可以直接检测核苷酸-蛋白质相互作用。MANT了解更多信息
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货号
数量
M12417
400 µL
货号 M12417
价格(CNY)
4,442.00
Online Exclusive
Ends: 31-Dec-2026
6,169.00
共减 1,727.00 (28%)
Each
添加至购物车
数量:
400 µL
价格(CNY)
4,442.00
Online Exclusive
Ends: 31-Dec-2026
6,169.00
共减 1,727.00 (28%)
Each
添加至购物车
核苷类似物 MANT ATP 的核糖基团经过修饰。MANT 荧光基团及其附着位置的紧凑性使得核苷类似物几乎不会干扰核苷酸-蛋白质相互作用。由于 MANT 荧光对荧光基团的环境敏感,因此可以直接检测核苷酸-蛋白质相互作用。MANT 核苷酸是用于检测核苷酸结合蛋白的结构及酶活性的重要探针。
仅供科研使用。不可用于诊断程序。
规格
标签或染料MANT(N-甲基氨茴酰)
产品类型MANT-ATP
数量400 µL
运输条件湿冰
最大浓度5 mM
Unit SizeEach
内容与储存
在冷冻冰箱(-5°C 至 -30°C)中避光储存。
引用和文献 (82)
引用和文献
Abstract
Authors:
Journal:
PubMed ID:11063593
A mechanistic model for Ncd directionality.
Authors:Foster KA, Mackey AT, Gilbert SP
Journal:J Biol Chem
PubMed ID:11278404
Ncd is a kinesin-related protein that drives movement to the minus-end of microtubules. Pre-steady-state kinetic experiments have been employed to investigate the cooperative interactions between the motor domains of the MC1 dimer and to establish the ATPase mechanism. Our results indicate that the active sites of dimeric Ncd free in ... More
Moving a microtubule may require two heads: a kinetic investigation of monomeric Ncd.
Authors:Mackey AT, Gilbert SP
Journal:Biochemistry
PubMed ID:10684615
'Ncd is a minus-end-directed microtubule motor and a member of the kinesin superfamily. The Ncd dimer contains two motor domains, and cooperative interactions between the heads influence the interactions of each respective motor domain with the microtubule. The approach we have taken to understand the cooperativity between the two motor ... More
Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein.
Authors:Galletto R, Rajendran S, Bujalowski W
Journal:Biochemistry
PubMed ID:11041861
'Quantitative analyses of the interactions of nucleotide cofactors with the Escherichia coli replicative factor DnaC protein have been performed using thermodynamically rigorous fluorescence titration techniques. This approach allowed us to obtain stoichiometries of the formed complexes and interaction parameters, without any assumptions about the relationship between the observed signal and ... More
The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity.
Authors:Murphy CT, Spudich JA
Journal:Biochemistry
PubMed ID:10090768
'We are interested in the role that solvent-exposed, proteolytically sensitive surface loops play in myosin function. The 25-50K loop, or loop 1, is near the ATP binding site, while the 50-20K loop (loop 2) is in the actin binding site. Through chimeric studies, we have found that loop 1 affects ... More